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13mer nucleotide sequence of RNAI + H2O
?
-
endonucleolytic cleavage, a synthetic 13-nt oligoribonucleotide, representing the cleavage site of RNAI, from the 5' end, with the canonical RNase E cleavage site located between U5 and A6
-
-
?
23S rRNA + H2O
5.8S-like rRNA + ?
5' monophosphorylated RNA oligonucleotides + H2O
?
-
several synthetic substrates, overview
-
-
?
5'-capped RNA I.26 + H2O
?
-
low activity, cleavage of the 5' substrate end
-
-
?
5'-GAGACAGUAUUUG + H2O
5'-GAGACAGU + AUUUG
LU13 substrate, LU13 is a BR13 derivative that has the central G of the 5' triplet replaced with an A. 5'-biotinylated LU13 is cleaved more rapidly when conjugated to streptavidin prior to incubation with N-terminal half-RNase E. In the absence of streptavidin conjugation, 5'-biotinylated LU13 is cleaved as poorly as its 5' hydroxylated equivalent
-
-
?
5'-GGGACAGUAUUUG + H2O
5'-GGGACAGU + AUUUG
BR13 substrate, RNase E can cleave certain RNAs rapidly without requiring a 5'-monophosphorylated end. Cleavage of 5'-hydroxylated oligonucleotide substrate by the N-terminal half of RNase E. RNase E can bind with higher affinity to a 5'-hydroxylated substrate with multiple single-stranded regions than to a 5'-monophosphorylated substrate with one single-stranded site
-
-
?
5'-GGGACAGUAUUUG-3' + H2O
?
-
-
-
-
?
5'-hydroxylated fluorogenic oligonucleotide + H2O
?
-
-
-
-
?
5'-labeled RNA oligonucleotides + H2O
?
-
synthetic RNA substrate variants based on known enzyme RNA substrate sequences, recombinant Rne498 catalytic domain, cleavage site specificity, overview
-
-
?
5'-monophosphorylated fluorogenic oligonucleotide + H2O
?
-
-
-
-
?
5'-triphosphorylated cspA mRNA + H2O
?
RNase E recognizes multiple single-stranded regions in cspA mRNA
-
-
?
5'-triphosphorylated epd-pgk RNA + H2O
?
RNase E cleavage of 5'-triphosphorylated epd-pgkRNA is faster than 5'-triphosphorylated 9S RNA and RNAi, but not as fast as the rate of cleavage of 5'-triphosphorylated cspA mRNA
-
-
?
5'-triphosphorylated mRNA fragment + H2O
?
-
-
-
-
?
5'-triphosphorylated RNAi + H2O
?
-
-
-
?
5'ACAGUAUUUG-fluorescein + H2O
5'ACAGU + AUUUG-fluorescein
-
5' monophosphorylated, 3' fluorescein-labeled synthetic substrate with protective 2'-O-methyl groups at all positions based on the 5' cleavage site of pBR322 RNA I
-
-
?
5'AUCAAAGAAA + H2O
5'AUCAAAGA + AA
-
5'-labeled synthetic RNA substrate, modified 9S RNA sequence, recombinant Rne498 catalytic domain, no activity with the wild-type 9S RNA sequence 5'AUCAAAUAAA and with modified sequence 5'AUCAGAUAAA
-
-
?
5'AUCAAGUAAA + H2O
5'AUCAAGU + AAA
-
low activity, 5'-labeled synthetic RNA substrate, modified 9S RNA sequence, recombinant Rne498 catalytic domain, no activity with the wild-type 9S RNA sequence 5'AUCAAAUAAA and with modified sequence 5'AUCAGAUAAA
-
-
?
5'AUCGAAUAAA + H2O
5'AUCGA + AUAAA
-
5'-labeled synthetic RNA substrate, modified 9S RNA sequence, recombinant Rne498 catalytic domain, no activity with the wild-type 9S RNA sequence 5'AUCAAAUAAA and with modified sequence 5'AUCAGAUAAA
-
-
?
5'GGGA(D-dT)CAGUAUUU-fluorescein + H2O
?
5' monophosphorylated, 3' fluorescein-labeled synthetic substrate with protective 2'-O-methyl groups at all positions based on the 5' cleavage site of RNA I
-
-
?
82 nt of the NifA mRNA + H2O
?
9S mRNA + H2O
p5S RNA + ?
-
-
-
-
?
9S precursor RNA + H2O
p5S RNA + ?
-
-
-
-
?
9S RNA + H2O
5S RNA + ?
-
-
-
-
?
9S rRNA precursor + H2O
5S rRNA + ?
AAUUU-containing RNA oligonucleotide + H2O
?
Aquifex aeolicus 9S rRNA + H2O
?
-
-
-
-
?
Bacillus subtilis aprE leader-lacZ mRNA + H2O
?
-
wild-type and mutant substrate, the latter with an exchange of a G and an A at +31 and +32, respectively, cleavage of the Bacillus subtilis transcript in a structure-dependent manner at the 5' end to the U residue at +12 within a double-stranded segment of an AU-rich sequence, which is part of the stem-loop structure at the 5' end of the transcript
-
-
?
bacteriophage T4 gene 32 mRNA + H2O
?
-
processing at the -71 site, which forms a stem-loop essential for enzyme activity of RNase E, the putative consensus sequence is RAUUW, mutational disruption of the stem-loop leads to loss of activity, mechanism, overview
-
-
?
BR13N RNA + H2O
?
-
synthetic RNA substrate, the cleavage site is GGGACAGUCUGUG
-
-
?
CAUUU-containing RNA oligonucleotide + H2O
?
endonulceolytic cleavage of sodB mRNA
?
-
the enzyme cleaves within the sodB 5'-untranslated region in vitro, thereby removing the 5' stem-loop structure that facilitates Hfq and ribosome binding, RNase E cleavage can also occur at a cryptic site that becomes available upon sodB 5'-UTR/RyhB base pairing
-
-
?
Escherichia coli M1 RNA + H2O
?
-
-
-
-
?
fluorogenic oligonucleotides + H2O
?
-
5' monophosphorylated or 5' hydroxylated substrates, P-BR14-FD or OH-BR14-FD
-
-
?
GAUUU-containing RNA oligonucleotide + H2O
?
GUUUU-containing RNA oligonucleotide + H2O
?
immature 16S rRNA + H2O
mature 16S rRNA
MicX + H2O
?
-
endonucleolytic cleavage, wild-type substrate, RNase E-dependent processing stabilizes MicX, a Vibrio cholerae sRNA
-
-
?
MicX sRNA + H2O
?
-
cleavage involves protein Hfq
-
-
?
MicX_DELTA196-263 mutant + H2O
?
-
endonucleolytic cleavage, a truncated Vibrio cholerae sRNA
-
-
?
oligonucleotide + H2O
?
-
preference for decay intermediates whose 5' end is monophosphorylated. The enzyme can tolerate any unpaired nucleotide (A, G, C, or U) at either of the first two positions, with only modest biases. The optimal spacing between the 5' end and the scissile phosphate is eight nucleotides. 5'-Monophosphate-assisted cleavage also occurs, albeit more slowly, when that spacing is greater or at most one nucleotide shorter than the optimum
-
-
?
Omp11 RNA + H2O
?
-
-
-
-
?
pppRNA I.26 + H2O
?
-
low activity, cleavage of the 5' substrate end
-
-
?
pre-tRNACys + H2O
tRNACys + 3'-leader of tRNA
-
-
-
-
?
pre-tRNAHis + H2O
tRNAHis + 3'-leader of tRNA
-
-
-
-
?
pre-tRNAPro + H2O
tRNAPro + 3'-leader of tRNA
-
-
-
-
?
pRNA I.26 + H2O
?
-
a monophosphate at the 5' end of the RNA I substrate stimulates the enzyme 25-30fold, cleavage of the 5' substrate end
-
-
?
proK primary transcript + H2O
?
proL primary transcript + H2O
?
proM primary transcript + H2O
?
Rep mRNA + H2O
?
-
the arginine-rich RNA binding domain and the protein scaffold domain of RNase E are dispensable for degradation of the replication initiator protein (Rep) mRNA of the ColE2 plasmid
-
-
?
rne mRNA + H2O
?
-
the enzyme autoregulates its expression by cleavage and processing of its own rne mRNA
-
-
?
rne-lacZ transcript + H2O
?
-
-
-
-
?
S20 mRNA + H2O
?
-
mRNA encoding ribosomal proteins, a single cleavage site at residues 300/301 is preceded by variable 5' extensions
-
-
?
S20 mRNA t160D + H2O
?
-
ribosomal protein encoding RNA
-
-
?
S20 mRNA t175D + H2O
?
-
ribosomal protein encoding RNA, structure mapping, secondary structure modeling, overview
-
-
?
S20 mRNA t194D + H2O
?
-
ribosomal protein encoding RNA, structure mapping, secondary structure modeling, overview
-
-
?
S20 mRNA t84D + H2O
?
-
ribosomal protein encoding RNA, contains a 5' stem loop with three noncanonical A-G pairs, structure mapping, secondary structure modeling, overview
-
-
?
S20 mRNA t95D + H2O
?
-
processing
-
-
?
single-stranded RNA + H2O
?
sodB mRNA + H2O
?
-
RNase E and RNase III are required for sodB RNA decay in vivo
-
-
?
sodB192 mRNA + H2O
?
-
cleavage of the 5'-untranslated region in vitro thereby removing the stem loop structure that facilitates Hfq and ribosome binding, additional cleavage at a cryptic site, that becomes available upon sodB5'-UTR/RyhB base pairing, RyhB is a small regulatory RNA involved in sodB translation control, overview
-
-
?
sRNA MicX_2-346 + H2O
?
-
a truncated Vibrio cholerae sRNA
-
-
?
tRNA precursors + H2O
?
-
the enzyme, cuts intercistronic regions of putative tRNA precursors, overview
-
-
?
tRNAArgHisLeuPro precursor + H2O
tRNAArg + tRNAHis + tRNALeu + tRNAPro + ?
tRNAAsn precursor + H2O
?
-
-
-
-
?
tRNAGlyCysLeu precursor + H2O
tRNAGly + tRNACys + tRNALeu + ?
tRNAHis precursor + H2O
?
-
-
-
-
?
tRNAPhe precursor + H2O
?
tRNAPro precursor + H2O
?
-
-
-
-
?
tRNATyr precursor + H2O
tRNATyr + ?
tRNATyrSu3 precursor + H2O
?
tRNATyrsu3+ + H2O
tRNATyrsu3+ + ?
-
a construct of 404 nucleotides containing a leader sequence and the amber suppressor form of tRNATyr
-
-
?
UAUUU-containing RNA oligonucleotide + H2O
?
-
G378 mutant substrate, p23 RNA variant derived from linearized DraI plasmid, in vitro substrate synthesis by SP6 RNA poylmerase
-
-
?
UUUUU-containing RNA oligonucleotide + H2O
?
-
G378/A379 mutant substrate, p23 RNA variant derived from linearized DraI DN1 or DN34 plasmids, in vitro substrate synthesis by SP6 RNA poylmerase
-
-
?
additional information
?
-
16s rRNA + H2O
?
-
-
-
?
16s rRNA + H2O
?
RNase E completely suppresses the accumulation of the 16.5S RNA intermediate in the Escherichia coli rne-1 strain
-
-
?
23S rRNA + H2O
5.8S-like rRNA + ?
-
5'-end processing, removal of an internal, transcribed spacer consisting of helices 9 and 10, RNase E is responsible for helix 10 processing, while helix 9 is excised by RNase III
-
-
?
23S rRNA + H2O
5.8S-like rRNA + ?
-
5'-end processing, removal of an internal, transcribed spacer consisting of helices 9 and 10, RNase E is responsible for helix 10 processing, while helix 9 is excised by RNase III
-
-
?
23S rRNA + H2O
5.8S-like rRNA + ?
-
5'-end processing, removal of an internal, transcribed spacer consisting of helices 9 and 10, RNase E is responsible for helix 10 processing, while helix 9 is excised by RNase III
-
-
?
23S rRNA + H2O
?
-
RNase E is involved in 5'-end 23S rRNA processing, schematic overview, removal of an internal, transcribed spacer consisting of helices 9 and 10, RNase E is responsible for helix 10 processing, while helix 9 is excised by RNase III
-
-
?
23S rRNA + H2O
?
-
RNase E is involved in 5'-end 23S rRNA processing, schematic overview, removal of an internal, transcribed spacer consisting of helices 9 and 10, RNase E is responsible for helix 10 processing, while helix 9 is excised by RNase III
-
-
?
23S rRNA + H2O
?
-
RNase E is involved in 5'-end 23S rRNA processing, schematic overview, removal of an internal, transcribed spacer consisting of helices 9 and 10, RNase E is responsible for helix 10 processing, while helix 9 is excised by RNase III
-
-
?
5'P-BR14FD + H2O
?
synthetic RNA substrate 5'P-BR14FD
-
-
?
5'P-BR14FD + H2O
?
synthetic RNA substrate 5'P-BR14FD
-
-
?
82 nt of the NifA mRNA + H2O
?
-
host factor required-dependent RNase E cleavage of NifA mRNA is essential for NifA translation. Cleavage site is located at 32 nucleotides upstream of the NifA translational start codon
-
-
?
82 nt of the NifA mRNA + H2O
?
-
host factor required-dependent RNase E cleavage of NifA mRNA is essential for NifA translation. Cleavage site is located at 32 nucleotides upstream of the NifA translational start codon
-
-
?
9S RNA + H2O
?
-
processing
-
-
?
9S RNA + H2O
?
-
cleavage site specificity, overview
-
-
?
9S RNA + H2O
?
-
processing
-
-
?
9S rRNA + H2O
?
-
-
-
-
?
9S rRNA + H2O
?
-
the enzyme is essential for 9S RNA processing
-
-
?
9S rRNA + H2O
?
-
-
-
-
?
9S rRNA precursor + H2O
5S rRNA + ?
-
-
-
-
?
9S rRNA precursor + H2O
5S rRNA + ?
-
very low activity with a covalently closed circular variant of the substrate compared to the linear one, overview
-
-
?
9S rRNA precursor + H2O
5S rRNA + ?
-
-
-
-
?
9S rRNA precursor + H2O
5S rRNA + ?
-
very low activity with a covalently closed circular variant of the substrate compared to the linear one, overview
-
-
?
9S-RNA + H2O
?
-
-
-
-
?
9SA RNA + H2O
?
-
-
-
-
?
9SA RNA + H2O
?
-
9Sa is a fragment of the 9S precursor of 5S rRNA
-
-
?
9SA RNA + H2O
?
-
9Sa is a fragment of the 9S precursor of 5S rRNA
-
-
?
AAUUU-containing RNA oligonucleotide + H2O
?
-
G378 mutant substrate, p23 RNA variant derived from linearized DraI plasmid, in vitro substrate synthesis by SP6 RNA poylmerase
-
-
?
AAUUU-containing RNA oligonucleotide + H2O
?
-
G378 mutant substrate, p23 RNA variant derived from linearized DraI plasmid, in vitro substrate synthesis by SP6 RNA poylmerase
-
-
?
BR13 + H2O
?
endonucleolytic cleavage, BR13 is an oligoribonucleotide that contains the RNase E-cleaved sequence of RNA I
-
-
?
BR13 + H2O
?
i.e. an oligonucleotide that contains the RNase E target site of RNA I. The N-terminal part of the enzyme from Vibrio vulnificus shows the cleavage specificity and activity of the enzyme from Escherichia coli
-
-
?
BR13 RNA + H2O
?
-
i.e. 5'GGGACAGUAUUUG3', 3' fluorescein-labeled substrate
-
-
?
BR13 RNA + H2O
?
-
synthetic RNA substrate, the cleavage site is GGGACAGUAUUUG
-
-
?
BR30M + H2O
?
-
endonucleolytic cleavage, a synthetic 30-mer oligoribonucleotide substrate containing 2'-O-methylated nucleotides at positions 16 and 17
-
-
?
BR30M + H2O
?
endonucleolytic cleavage, a synthetic 30-mer oligoribonucleotide substrate containing 2'-O-methylated nucleotides at positions 16 and 17
-
-
?
CAUUU-containing RNA oligonucleotide + H2O
?
-
G378 mutant substrate, p23 RNA variant derived from linearized DraI plasmid, in vitro substrate synthesis by SP6 RNA poylmerase
-
-
?
CAUUU-containing RNA oligonucleotide + H2O
?
-
G378 mutant substrate, p23 RNA variant derived from linearized DraI plasmid, in vitro substrate synthesis by SP6 RNA poylmerase
-
-
?
cspA mRNA + H2O
?
-
degradation of the cspA mRNA in vivo is very rapid at temperatures greater than 30°C, overview
-
-
?
cspA mRNA + H2O
?
-
cleavage at a single site in vitro between two stem-loops about 24 residues 3' to the termination codon and about 31 residues from the 3' end. The site of cleavage is independent of the temperature and largely independent of the phosphorylation status of the 5' end of cspA mRNA, overview
-
-
?
GAUUU-containing RNA oligonucleotide + H2O
?
-
wild-type substrate, best substrate, p23 RNA variant derived from linearized DraI plasmid, in vitro substrate synthesis by SP6 RNA poylmerase
-
-
?
GAUUU-containing RNA oligonucleotide + H2O
?
-
wild-type substrate, best substrate, p23 RNA variant derived from linearized DraI plasmid, in vitro substrate synthesis by SP6 RNA poylmerase
-
-
?
GUUUU-containing RNA oligonucleotide + H2O
?
-
A379 mutant substrate, p23 RNA variant derived from linearized DraI plasmid, in vitro substrate synthesis by SP6 RNA poylmerase
-
-
?
GUUUU-containing RNA oligonucleotide + H2O
?
-
A379 mutant substrate, p23 RNA variant derived from linearized DraI plasmid, in vitro substrate synthesis by SP6 RNA poylmerase
-
-
?
immature 16S rRNA + H2O
mature 16S rRNA
-
RNase G, i.e. CafA protein, and RNase E are both required for the 5' maturation of 16S ribosomal RNA
-
-
?
immature 16S rRNA + H2O
mature 16S rRNA
-
secondary processing for formation of the mature 5' terminus
-
-
?
ompA mRNA + H2O
?
-
processing
-
-
?
ompA mRNA + H2O
?
-
ompA at a site which is rate determining for degradation and also cleaved by RNase K
-
-
?
p23 RNA + H2O
?
endonucleolytic cleavage
-
-
?
p23 RNA + H2O
?
-
-
-
-
?
pre-5S rRNA + H2O
?
-
processing
-
-
?
pre-5S rRNA + H2O
?
-
processing
-
-
?
proK primary transcript + H2O
?
-
RNase E is primarily responsible for the endonucleolytic removal of the entire Rho-independent transcription terminator associated with the proK, proL and proM primary transcripts by cleaving immediately downstream of the CCA determinant
-
-
?
proK primary transcript + H2O
?
-
RNase E is primarily responsible for the endonucleolytic removal of the entire Rho-independent transcription terminator associated with the proK, proL and proM primary transcripts by cleaving immediately downstream of the CCA determinant
-
-
?
proL primary transcript + H2O
?
-
RNase E is primarily responsible for the endonucleolytic removal of the entire Rho-independent transcription terminator associated with the proK, proL and proM primary transcripts by cleaving immediately downstream of the CCA determinant
-
-
?
proL primary transcript + H2O
?
-
RNase E is primarily responsible for the endonucleolytic removal of the entire Rho-independent transcription terminator associated with the proK, proL and proM primary transcripts by cleaving immediately downstream of the CCA determinant
-
-
?
proM primary transcript + H2O
?
-
RNase E is primarily responsible for the endonucleolytic removal of the entire Rho-independent transcription terminator associated with the proK, proL and proM primary transcripts by cleaving immediately downstream of the CCA determinant
-
-
?
proM primary transcript + H2O
?
-
RNase E is primarily responsible for the endonucleolytic removal of the entire Rho-independent transcription terminator associated with the proK, proL and proM primary transcripts by cleaving immediately downstream of the CCA determinant
-
-
?
pSu3 + H2O
?
-
endonucleolytic cleavage, the precursor of the Escherichia coli tRNATyrSu3, cleavage upstream of the RNase P cleavage site in vitro and in vivo
-
-
?
pSu3 + H2O
?
-
endonucleolytic cleavage, the precursor of the Escherichia coli tRNATyrSu3, cleavage upstream of the RNase P cleavage site in vitro and in vivo, cleavage site mapping, overview, very low activity with the substrate mutants K546A and K552A, lack of Mg2+ leads to unspecific cleavage of pSu3 RNA to small oligoribonucleotides
-
-
?
puf mRNA + H2O
?
-
degradation
-
-
?
puf mRNA + H2O
?
-
initiation of degradation of the 5' pufQ mRNA segment, expressed from plasmids pBPT8 or pBRMOD11 using the bla promoter of plasmid pBR322, the enzyme discriminates between the two sequences GGCUUU and GAUUUU preferring AU-rich sequences
-
-
?
puf mRNA + H2O
?
-
degradation
-
-
?
puf mRNA + H2O
?
-
initiation of degradation of the 5' pufQ mRNA segment, expressed from plasmids pBPT8 or pBRMOD11 using the bla promoter of plasmid pBR322, the enzyme discriminates between the two sequences GGCUUU and GAUUUU preferring AU-rich sequences
-
-
?
puf mRNA + H2O
?
-
degradation
-
-
?
puf mRNA + H2O
?
-
initiation of degradation of the pufLMX segment, the enzyme does not discriminate between the two sequences GGCUUU and GAUUUU
-
-
?
RNA + H2O
?
-
the enzyme is required for RNA processing and degradation
-
-
?
RNA + H2O
?
-
cleavage site specificity is not affected by temperature, selective cleavage at the 5' end of internucleotide bonds in 3' to 5' direction, cleavage pattern, overview
-
-
?
RNA + H2O
?
-
endonucleolytic cleavage, the Arabidopsis enzyme uses single-stranded oligoribonucleotide and chloroplast RNA as substrates, and depends on the number of phosphates at the 5' end, is inhibited by structured RNA, and preferentially cleaves A/U-rich sequences, catalytic domain structure, overview
-
-
?
RNA + H2O
?
-
-
693689, 694008, 694243, 694247, 694921, 729757, 729924, 730503, 730512, 730699, 730781, 730815 -
-
?
RNA + H2O
?
-
the enzyme or its isolated N-terminal catalytic domain cleave poly(A) tails on the 3' end of RNA substrates, the RNA degradosome cleaves 3' poly(A) tails of RNA irrespective of the 5' phosphorylation status, while the purified RNase E shows high preference for 5'-monophosphorylated RNA substrates, and low activity with 5'-triphosphate RNA, N-terminal ribonucleolytic domain RTD-RNase E is the catalytic domain and sufficient for activity
-
-
?
RNA + H2O
?
RNase E recognizes RNA secondary structure. Signature on the substrate 50 end recognizes and activates RNase E
-
-
?
RNA + H2O
?
-
the enzyme or its isolated N-terminal catalytic domain cleave poly(A) tails on the 3' end of RNA substrates, the RNA degradosome cleaves 3' poly(A) tails of RNA irrespective of the 5' phosphorylation status, while the purified RNase E shows high preference for 5'-monophosphorylated RNA substrates, and low activity with 5'-triphosphate RNA, N-terminal ribonucleolytic domain RTD-RNase E is the catalytic domain and sufficient for activity
-
-
?
RNA + H2O
?
-
the enzyme plays a key role in processing and degradation of RNA in Escherichia coli
-
-
?
RNA + H2O
?
RNase E recognizes RNA secondary structure. Signature on the substrate 50 end recognizes and activates RNase E
-
-
?
RNA + H2O
?
-
Mg2+ targets the mgtA transcript which encodes a Mg2+ transporter, for degradation by RNase E
-
-
?
RNA + H2O
?
-
RNase E processing of various precursor RNAs produces many small regulatory RNAs, constituting a major small-RNA biogenesis pathway in bacteria
-
-
?
RNA + H2O
?
-
RNase E cleaves numerous transcripts at preferred sites by sensing uridine as a 2-nt ruler
-
-
?
RNA I + H2O
?
-
-
-
-
?
RNA I + H2O
?
5' cleavage site
-
-
?
RNA I + H2O
?
-
full-length RNA I by plasmids pBR322 or pACY184, cleavage site specificity, overview
-
-
?
RNA I + H2O
?
-
the arginine-rich RNA binding domain of RNase E and the protein scaffold domain of RNase E is important for successive exoribonucleolytic degradation of RNAI, suggesting involvement of RhlB. RNase E-PNPase complex formation is not essential for RNAI degradation
-
-
?
RNA I + H2O
?
-
cleavage of the 5' substrate end
-
-
?
RNA I + H2O
?
-
full-length RNA I and GGGRNA I encoded by plasmids pBR322, pCML103, or pCML108, RNA binding domain structure, secondary structure of the substrate RNA, complex formation and mechanism, multiple cleavage sites, overview
several fragments, product mapping, overview
-
?
RNA I.26 + H2O
?
-
5' mono- or triphosphorylated, or 5' hydroxylated substrate
-
-
?
RNA I.26 + H2O
?
-
cleavage of the 5' substrate end
-
-
?
RNA I.26 + H2O
?
-
-
-
-
?
rpsT mRNA + H2O
?
-
the substrate encodes the ribosomal protein S20
-
-
?
rpsT mRNA + H2O
?
-
the substrate encodes the ribosomal protein S20, very low activity with a covalently closed circular variant of the substrate compared to the linear one, overview
-
-
?
rpsT mRNA + H2O
?
-
the substrate encodes the ribosomal protein S20
-
-
?
rpsT mRNA + H2O
?
-
the substrate encodes the ribosomal protein S20, very low activity with a covalently closed circular variant of the substrate compared to the linear one, overview
-
-
?
S20 mRNA t87D + H2O
?
-
processing
-
-
?
S20 mRNA t87D + H2O
?
-
ribosomal protein encoding RNA
-
-
?
S20 mRNA t87D + H2O
?
-
processing
-
-
?
single-stranded RNA + H2O
?
-
RhlB is an ATP-dependent motor that unfolds structured RNA for destruction by partner ribonucleases, RhlB associates with the essential endoribonuclease RNase E as part of the multi-enzyme RNA degradosome assembly, RNase E activates RhlB severalfold, determination and analysis of the specific protein interaction sites using limited protease digestion, domain cross-linking and homology modelling. The stoichiometry for RhlB-CTD/RNase E, residues 628-843, complex is 1:1, overview
-
-
?
single-stranded RNA + H2O
?
-
RNA substrate specificity of full-length and truncated RNase E in complex with RhlB, overview
-
-
?
single-stranded RNA + H2O
?
preferentially cleaves single-stranded RNAs within U-rich regions. Most cleavage sites contained one or two U. It cleaves the phosphodiester linkage on the 3'-side and generates 5'-phosphate- and 3'-hydroxyl-terminated oligonucleotides. The enzyme cleaves these substrates only in close proximity to the 5'- or 3'-ends suggesting that it requires the presence of a free RNA end. Oligoribonucleotides as short as 10 nt can serve as SSO1404 substrates. Tyr-9, Asp-10, Arg-17, Arg-19, Arg-31, and Phe-37 are important for enzymatic activity. Asp-10 might be the principal catalytic residue. No cleavage of dsRNA substrates prepared by annealing ssRNA substrates. No nuclease activity against either of the DNA substrates. The 39 nucleotide ssRNA substrate AAAUACG-/-U-/-U-/-UUCUCCAUUGUCAUAUUGCGCAUAAGUUGA shows the highest activity among the ssRNA substrates tested
-
-
?
single-stranded RNA + H2O
?
preferentially cleaves single-stranded RNAs within U-rich regions. Most cleavage sites contained one or two U. It cleaves the phosphodiester linkage on the 3'-side and generates 5'-phosphate- and 3'-hydroxyl-terminated oligonucleotides. The enzyme cleaves these substrates only in close proximity to the 5'- or 3'-ends suggesting that it requires the presence of a free RNA end. Oligoribonucleotides as short as 10 nt can serve as SSO1404 substrates. Tyr-9, Asp-10, Arg-17, Arg-19, Arg-31, and Phe-37 are important for enzymatic activity. Asp-10 might be the principal catalytic residue. No cleavage of dsRNA substrates prepared by annealing ssRNA substrates. No nuclease activity against either of the DNA substrates. The 39 nucleotide ssRNA substrate AAAUACG-/-U-/-U-/-UUCUCCAUUGUCAUAUUGCGCAUAAGUUGA shows the highest activity among the ssRNA substrates tested
-
-
?
tRNAArgHisLeuPro precursor + H2O
tRNAArg + tRNAHis + tRNALeu + tRNAPro + ?
-
polycistronic transcript, maturation, overview
-
-
?
tRNAArgHisLeuPro precursor + H2O
tRNAArg + tRNAHis + tRNALeu + tRNAPro + ?
-
polycistronic transcript, maturation
-
-
?
tRNAArgHisLeuPro precursor + H2O
tRNAArg + tRNAHis + tRNALeu + tRNAPro + ?
-
polycistronic transcript, maturation, overview
-
-
?
tRNAArgHisLeuPro precursor + H2O
tRNAArg + tRNAHis + tRNALeu + tRNAPro + ?
-
polycistronic transcript, maturation
-
-
?
tRNAGlyCysLeu precursor + H2O
tRNAGly + tRNACys + tRNALeu + ?
-
polycistronic transcript, maturation, cleavage downstream of each tRNA, overview
-
-
?
tRNAGlyCysLeu precursor + H2O
tRNAGly + tRNACys + tRNALeu + ?
-
polycistronic transcript, maturation, cleavage downstream of each tRNA
-
-
?
tRNAGlyCysLeu precursor + H2O
tRNAGly + tRNACys + tRNALeu + ?
-
polycistronic transcript, maturation, cleavage downstream of each tRNA, overview
-
-
?
tRNAGlyCysLeu precursor + H2O
tRNAGly + tRNACys + tRNALeu + ?
-
polycistronic transcript, maturation, cleavage downstream of each tRNA
-
-
?
tRNAPhe precursor + H2O
?
-
-
-
-
?
tRNAPhe precursor + H2O
?
-
-
-
?
tRNATyr precursor + H2O
tRNATyr + ?
-
maturation, cleavage of the tyrT transcript, containing two tRNATyr1 sequences separated by a 209-nt spacer region plus a downstream mRNA, at three sites in the speacer region, overview
-
-
?
tRNATyr precursor + H2O
tRNATyr + ?
-
maturation, cleavage of the tyrT transcript, containing two tRNATyr1 sequences separated by a 209-nt spacer region plus a downstream mRNA, at three sites in the spacer region
-
-
?
tRNATyrSu3 precursor + H2O
?
-
cleavage in the 5' leader sequence, the enzyme is involved in regulation of cellular tRNA levels
-
-
?
tRNATyrSu3 precursor + H2O
?
-
cleavage in the 5' leader sequence, cleavage sites and activity using wild-type and deletion mutant substrates, overview
-
-
?
unc mRNA + H2O
?
-
the unc operon encodes the eight subunits of the Escherichia coli F1F0-ATPase, processing of the unc mRNAs by the RNase E, overview, RNase E is essential for uncC processing
-
-
?
unc mRNA + H2O
?
-
the unc operon encodes the eight subunits of the Escherichia coli F1F0-ATPase, processing of the unc mRNAs by the RNase E, overview
-
-
?
upRNA + H2O
?
-
RNase E is a processing enzyme involved in 3' end formation of M1 RNA, and plays a dual role in processing and degradation to achieve tight control of M1 RNA biosynthesis
-
-
?
upRNA + H2O
?
-
M1 RNA, the gene product of rnpB, is the catalytic subunit of RNase P in Escherichia coli, M1 RNA is transcribed from a proximal promoter as pM1 RNA, a precursor M1 RNA, and then is processed at its 3' end by RNase E, the M1 RNA structural sequence in upRNA is much more vulnerable to the enzyme than the sequence in pM1 RNA, full-length enzyme and N-terminal domain of RNase E, cleavage patterns, overview
-
-
?
additional information
?
-
-
RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region
-
-
?
additional information
?
-
-
RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region
-
-
?
additional information
?
-
-
the enzyme prefers 5' monophosphorylated RNA substrates compared to nonphosphorylated or 5' triphosphorylated RNA substrates
-
-
?
additional information
?
-
-
Aquifex aeolicus RNase E/G is able to selectively cleave internucleotide bonds in the 3'-5' direction, and to cut in intercistronic regions of putative tRNA precursors
-
-
?
additional information
?
-
-
the bifunctional enzyme, exhibiting RNase E and RNase G activities, is involved in rRNA processing and maturation of tRNAs, that originated from polycistronic transcripts encoded by the Aquifex aeolicus tufA2 and rRNA operons, overview
-
-
?
additional information
?
-
-
site-specific RNase E/G cleavage of RNA using 5'-end-labelled substrates, e.g. L1 RNA, RNAI, and 9S RNA, overview. RNase E/G has a temperature-dependent, endoribonucleolytic activity that is dependent on the 5'-phosphorylation status of RNA. The enzyme site-specifically cleaves oligonucleotides and structured RNAs at locations that are partly overlapping or completely different when compared to the positions of Escherichia coli RNase E and RNase G cleavage sites, RNase E/G shows 3'-5' directionality in cleavage site selection, overview, the cleavage site selection of RNase E/G is temperature-dependent, overview
-
-
?
additional information
?
-
-
RNA degradation in the chloroplast occurs via the polyadenylation-assisted degradation pathway, plant RNase E participates in the initial endonucleolytic cleavage of the polyadenylation-stimulated RNA degradation process in the chloroplast, perhaps in collaboration with the two other chloroplast endonucleases, RNase J and CSP41, overview
-
-
?
additional information
?
-
-
reaction mechanism
-
-
?
additional information
?
-
-
initiation of tRNA 5' maturation by RNase E is essential for cell viability, the enzyme initiates the processing of polycistronic RNA of several operons, e.g. of glyW cysT leuZ, argX hisR leuT proM, or lysT valT lysW valZ lysY lysZlysQ, as well as of monocistronic transcripts such as pheU, pheV, asnT, asnU, asnV, or asnW, mapping of cleavage sites at the 3' end within tRNA precursors, overview, the enzyme is essential for degradation of many mRNAs, e.g. of rpsO
-
-
?
additional information
?
-
-
RNase E is involved in and interacts with functionally and physically polynucleotide phosphorylase, and also with other enzymes implicated in the processing and degradation of RNA, polynuclease phosphorylase, PNPase, degrades the reaction products generated by RNase E
-
-
?
additional information
?
-
-
the enzyme autoregulates its expression by cleavage and processing of its own rne mRNA
-
-
?
additional information
?
-
-
the enzyme is essential for regulation of mRNA turnover by specific processing and degradation and is involved in regulation of cell homeostasis, growth and development
-
-
?
additional information
?
-
the enzyme is essential for regulation of mRNA turnover by specific processing and degradation and is involved in regulation of cell homeostasis, growth and development
-
-
?
additional information
?
-
-
the enzyme is part of the RNA degradosome, a large multiprotein machine to process and degrade RNA
-
-
?
additional information
?
-
-
the enzyme is required for rapid decay and correct hydrolytic processing of RNA
-
-
?
additional information
?
-
-
the enzyme is the major endoribonuclease participating in mRNA turnover in Escherichia coli
-
-
?
additional information
?
-
-
the enzyme plays an important role in the processing and degradation of bacteriophage T4 and Escherichia coli mRNAs, mutational processing site analysis, overview
-
-
?
additional information
?
-
-
the enzyme, especially its catalytic N-terminal domain, is essential for RNA processing and degradation, and for cell growth and feedback regulation of RNase E synthesis
-
-
?
additional information
?
-
-
analysis of cleavage site specficity
-
-
?
additional information
?
-
-
cleavage site recognition mechanism, effect on substrate structure alteration by different treatments on cleavage site recognition, overview
-
-
?
additional information
?
-
-
identification of specific sequence determinants that either facilitate or impede the recognition and cleavage of RNA by the enzyme, RNA-enzyme interactions, overview
-
-
?
additional information
?
-
nucleic acid binding structure, structure-function relationship, overview
-
-
?
additional information
?
-
-
nucleic acid binding structure, structure-function relationship, overview
-
-
?
additional information
?
-
-
ribonuclease E is a 5'-end-dependent, single-strand-specific endonuclease that initiates the selective decay of mRNA having regulatory function, regulation of mRNA levels in response to environment, the enzyme proceeds in a 5' to 3' direction, the enzyme shows high activity with 5' monophosphorylated RNA, but low activity with 5' triphosphorylated RNA, poor activity with circular RNA substrates, overview
-
-
?
additional information
?
-
-
RNA processing reaction mechanism and involved functional groups, activity depends on protonated and unprotonated groups, the recognition of a guanosine sequence determinant upstream of the scissile bond via interaction with the exocyclic 2-amino group, the 7N of the nucleobase, and the imino proton or 6-keto group, overview
-
-
?
additional information
?
-
-
RNase E acts via a scanning mechanism in processing and degradation of RNA
-
-
?
additional information
?
-
-
RNase E shows preference for 5' monophosphorylated RNA substrates rather than RNA with a triphosphate or hydroxyl at the 5' end, the enzyme needs to be in a multimeric state for activation by 5' monophosphorylated RNA substrates
-
-
?
additional information
?
-
-
structural features required for RNA turnover, the enzyme attacks the 5' terminus of RNA substrates, RNA recognition mechanism, RNA-binding channel formed by the catalytic domain tetramer, cleavage site structure, and reaction mechanism, overview
-
-
?
additional information
?
-
structural features required for RNA turnover, the enzyme attacks the 5' terminus of RNA substrates, RNA recognition mechanism, RNA-binding channel formed by the catalytic domain tetramer, cleavage site structure, and reaction mechanism, overview
-
-
?
additional information
?
-
-
the catalytic domain of the multifunctional endoribonuclease determines inherent 3' to 5' directionality in cleavage site selection, cleavage site sequences overview
-
-
?
additional information
?
-
-
the enzyme binds RNA with high affinity
-
-
?
additional information
?
-
-
the enzyme shows similar cleavage site specificity as RNase G
-
-
?
additional information
?
-
-
the N-terminal catalytic domain is sufficient for catalytic activity, the enzyme shows high RNA binding ability, and cleavage of mRNA and rRNA, RNase E interacts with polynucleotide phosphorylase and other enzymes implicated in the processing and degradation of RNA, cleavage site specificity, overview, RNase E requires the stem loop structure in RNA substrates, altering of the substrate secondary structure alters substrate specificity, overview, the enzymes' arginine-rich RNA-binding site is not essential for activity but allows the degradosome to move progressively along the transcript during degradation
-
-
?
additional information
?
-
-
both RNase E and RNase III control the stability of sodB mRNA upon translational inhibition by the small regulatory RNA RyhB, iron-dependent variations in the steady-state concentration and translatability of sodB mRNA are modulated by the small regulatory RNA RyhB, the RNA chaperone Hfq, and RNase E, decay of sodB mRNA is retarded upon inactivation of RNaseE in vivo, mechanism, modelling, overview
-
-
?
additional information
?
-
ribonuclease E is an essential hydrolytic endonuclease in Escherichia coli, and it plays a central role in maintaining the balance and composition of the messenger RNA population
-
-
?
additional information
?
-
-
ribonuclease E is an essential hydrolytic endonuclease in Escherichia coli, and it plays a central role in maintaining the balance and composition of the messenger RNA population
-
-
?
additional information
?
-
RNase E is an essential bacterial endoribonuclease involved in the turnover of messenger RNA and the maturation of structured RNA precursors in Escherichia coli, RNA degradation mechanism, overview
-
-
?
additional information
?
-
-
RNase E is an essential bacterial endoribonuclease involved in the turnover of messenger RNA and the maturation of structured RNA precursors in Escherichia coli, RNA degradation mechanism, overview
-
-
?
additional information
?
-
-
RNase E is an essential endonuclease involved in the regulatory processing and/or degradation of tRNAs, rRNAs, and non-coding small RNAs as well as many mRNAs, the enzyme is regulated by an RNA-binding protein Hfq. RNase is required for induction of the glutamate-dependent acid resistance system in a RpoS-independent manner
-
-
?
additional information
?
-
RNase E is an essential Escherichia coli endoribonuclease that plays a major role in the decay and processing of a large fraction of RNAs in the cell, overview
-
-
?
additional information
?
-
-
RNase E is an essential Escherichia coli endoribonuclease that plays a major role in the decay and processing of a large fraction of RNAs in the cell, overview
-
-
?
additional information
?
-
-
RNaseE, as the main component of the RNA degradosome of Escherichia coli, plays an essential role in RNA processing and decay
-
-
?
additional information
?
-
-
the balance and composition of the transcript population is affected by RNase E, an essential endoribonuclease that not only turns over RNA but also processes certain key RNA precursors
-
-
?
additional information
?
-
the balance and composition of the transcript population is affected by RNase E, an essential endoribonuclease that not only turns over RNA but also processes certain key RNA precursors
-
-
?
additional information
?
-
-
endonucleolytic cleavage as selective processing via allosteric intermediates of RNA substrates, the catalytic activity is influenced by the 5'-end of the substrate, four subunits of RNase E catalytic domain are organized in an interwoven quaternary structure required for catalytic activity, catalytic site structure, overview
-
-
?
additional information
?
-
endonucleolytic cleavage as selective processing via allosteric intermediates of RNA substrates, the catalytic activity is influenced by the 5'-end of the substrate, four subunits of RNase E catalytic domain are organized in an interwoven quaternary structure required for catalytic activity, catalytic site structure, overview
-
-
?
additional information
?
-
RNA degradation mechanism, overview
-
-
?
additional information
?
-
-
RNA degradation mechanism, overview
-
-
?
additional information
?
-
-
the enzyme is active on mRNA and tRNA substrates, overview
-
-
?
additional information
?
-
-
a proportion of PNPase is recruited into a multi-enzyme assembly, known as the RNA degradosome, through an interaction with the scaffolding domain of the endoribonuclease RNase E
-
-
?
additional information
?
-
-
RNase E autoregulates its production by governing the decay rate of RNase E mRNA by binding directly to a stem-loop in the rne gene 5' untranslated region
-
-
?
additional information
?
-
RNase E preferres substrates possessing a 5'-monophosphate
-
-
?
additional information
?
-
-
RNase E preferres substrates possessing a 5'-monophosphate
-
-
?
additional information
?
-
-
the C-terminus of this enzyme serves as a scaffold to which other components of the RNA degradosome bind including the phosphorolytic 3'-exonuclease, polynucleotide phosphorylase, the DEAD-box RNA helicase RhlB, and the glycolytic enzyme enolase. The DEAD-box RNA helicases CsdA and RhlE and the RNA binding protein Hfq may bind to RNase E in place of one or more of the prototypical components.
-
-
?
additional information
?
-
upon catalytic activation, RNase E undergoes a marked conformational change characterized by the coupled movement of two RNA-binding domains to organize the active site
-
-
?
additional information
?
-
-
upon catalytic activation, RNase E undergoes a marked conformational change characterized by the coupled movement of two RNA-binding domains to organize the active site
-
-
?
additional information
?
-
Escherichia coli enolase and its RNase E enolase-binding site demonstrate positive interactions. PNPase-binding site of RNase E interacts with Vibrio angustum S14 or Escherichia coli PNPase
-
-
?
additional information
?
-
-
Escherichia coli enolase and its RNase E enolase-binding site demonstrate positive interactions. PNPase-binding site of RNase E interacts with Vibrio angustum S14 or Escherichia coli PNPase
-
-
?
additional information
?
-
-
RNase E cleaves the 217-nt RNAs at internal sites in an arginine-rich RNA binding domain-independent manner and about 180-nt degradation intermediates are formed
-
-
?
additional information
?
-
-
RNA chaperon Hfq along with Hfq-binding sRNAs stably binds to RNase E in Escherichia coli. The role of the Hfq-RNase E interaction is to recruit RNase E to target mRNAs of sRNAs resulting in the rapid degradation of the mRNA-sRNA hybrid. The scaffold region of RNase E can be deleted up to residue 750 without losing the ability to cause the rapid degradation of target mRNAs mediated by Hfq/sRNAs. The truncated RNase E750 can still bind to Hfq although the truncation significantly reduces the Hfq-binding ability. Deletion of the 702-50 region greatly impairs the ability of RNase E to cause the degradation of ptsG mRNA. A polypeptide corresponding to the scaffold region binds to Hfq without the help of RNA. Overexpression of RhlB partially inhibits the Hfq binding to RNase E and the rapid degradation of ptsG mRNA
-
-
?
additional information
?
-
-
RNase PH interacts with the carboxy-terminal end of RNase E
-
-
?
additional information
?
-
-
the enzyme is the major endoribonuclease participating in mRNA turnover in Escherichia coli
-
-
?
additional information
?
-
-
the enzyme binds RNA with high affinity
-
-
?
additional information
?
-
-
RNase PH interacts with the carboxy-terminal end of RNase E
-
-
?
additional information
?
-
-
ribonuclease E is a 5'-end-dependent, single-strand-specific endonuclease that initiates the selective decay of mRNA having regulatory function, regulation of mRNA levels in response to environment, the enzyme proceeds in a 5' to 3' direction, the enzyme shows high activity with 5' monophosphorylated RNA, but low activity with 5' triphosphorylated RNA, poor activity with circular RNA substrates, overview
-
-
?
additional information
?
-
-
the C-terminus of this enzyme serves as a scaffold to which other components of the RNA degradosome bind including the phosphorolytic 3'-exonuclease, polynucleotide phosphorylase, the DEAD-box RNA helicase RhlB, and the glycolytic enzyme enolase. The DEAD-box RNA helicases CsdA and RhlE and the RNA binding protein Hfq may bind to RNase E in place of one or more of the prototypical components.
-
-
?
additional information
?
-
-
analysis of cleavage site specficity
-
-
?
additional information
?
-
-
RNase E plays an essential role in the maturation of tRNA precursors, cleavage site and maturation process modeling, overview
-
-
?
additional information
?
-
-
the enzyme can cleave internucleotide bonds in the bubble regions of duplex RNA segments and in single-stranded regions, mechanism
-
-
?
additional information
?
-
-
RNase E plays an essential role in the maturation of tRNA precursors, cleavage site and maturation process modeling, overview
-
-
?
additional information
?
-
-
the enzyme is active on mRNA and tRNA substrates, overview
-
-
?
additional information
?
-
RNase E enolase-binding site interacts with enolase from both Vibrio angustum S14 and Escherichia coli. The C-terminal half of RNase E interacts with Vibrio angustum S14 or Escherichia coli PNPase. C-terminal half of RNase E is capable of self-interaction
-
-
?
additional information
?
-
-
RNase E enolase-binding site interacts with enolase from both Vibrio angustum S14 and Escherichia coli. The C-terminal half of RNase E interacts with Vibrio angustum S14 or Escherichia coli PNPase. C-terminal half of RNase E is capable of self-interaction
-
-
?
additional information
?
-
-
fluorogenic cleavage assay
-
-
?
additional information
?
-
-
fluorogenic cleavage assay
-
-
?
additional information
?
-
-
substrate specificity, the enzyme shows high activity with 5' monophosphorylated RNA, but low activity with 5' triphosphorylated RNA, overview
-
-
?
additional information
?
-
-
cleavage site specificity, overview
-
-
?
additional information
?
-
-
substrate specificity, the enzyme shows high activity with 5' monophosphorylated RNA, but low activity with 5' triphosphorylated RNA, overview
-
-
?
additional information
?
-
-
substrate specificity, the enzyme shows high activity with 5' monophosphorylated RNA, but low activity with 5' triphosphorylated RNA, overview
-
-
?
additional information
?
-
-
cleavage site specificity, overview
-
-
?
additional information
?
-
-
RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region
-
-
?
additional information
?
-
N-RneV has cleavage activity and specificity of RNase E on RNase E-targeted sequence of RNA I (BR13)
-
-
?
additional information
?
-
-
N-RneV has cleavage activity and specificity of RNase E on RNase E-targeted sequence of RNA I (BR13)
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
9S rRNA + H2O
?
-
the enzyme is essential for 9S RNA processing
-
-
?
9S rRNA precursor + H2O
5S rRNA + ?
Aquifex aeolicus 9S rRNA + H2O
?
-
-
-
-
?
Bacillus subtilis aprE leader-lacZ mRNA + H2O
?
-
wild-type and mutant substrate, the latter with an exchange of a G and an A at +31 and +32, respectively, cleavage of the Bacillus subtilis transcript in a structure-dependent manner at the 5' end to the U residue at +12 within a double-stranded segment of an AU-rich sequence, which is part of the stem-loop structure at the 5' end of the transcript
-
-
?
BR13 + H2O
?
endonucleolytic cleavage, BR13 is an oligoribonucleotide that contains the RNase E-cleaved sequence of RNA I
-
-
?
cspA mRNA + H2O
?
-
degradation of the cspA mRNA in vivo is very rapid at temperatures greater than 30°C, overview
-
-
?
Escherichia coli M1 RNA + H2O
?
-
-
-
-
?
immature 16S rRNA + H2O
mature 16S rRNA
-
RNase G, i.e. CafA protein, and RNase E are both required for the 5' maturation of 16S ribosomal RNA
-
-
?
MicX sRNA + H2O
?
-
cleavage involves protein Hfq
-
-
?
ompA mRNA + H2O
?
-
ompA at a site which is rate determining for degradation and also cleaved by RNase K
-
-
?
p23 RNA + H2O
?
endonucleolytic cleavage
-
-
?
pre-tRNACys + H2O
tRNACys + 3'-leader of tRNA
-
-
-
-
?
pre-tRNAHis + H2O
tRNAHis + 3'-leader of tRNA
-
-
-
-
?
pre-tRNAPro + H2O
tRNAPro + 3'-leader of tRNA
-
-
-
-
?
pSu3 + H2O
?
-
endonucleolytic cleavage, the precursor of the Escherichia coli tRNATyrSu3, cleavage upstream of the RNase P cleavage site in vitro and in vivo
-
-
?
rne mRNA + H2O
?
-
the enzyme autoregulates its expression by cleavage and processing of its own rne mRNA
-
-
?
single-stranded RNA + H2O
?
-
RhlB is an ATP-dependent motor that unfolds structured RNA for destruction by partner ribonucleases, RhlB associates with the essential endoribonuclease RNase E as part of the multi-enzyme RNA degradosome assembly, RNase E activates RhlB severalfold, determination and analysis of the specific protein interaction sites using limited protease digestion, domain cross-linking and homology modelling. The stoichiometry for RhlB-CTD/RNase E, residues 628-843, complex is 1:1, overview
-
-
?
sodB mRNA + H2O
?
-
RNase E and RNase III are required for sodB RNA decay in vivo
-
-
?
tRNAArgHisLeuPro precursor + H2O
tRNAArg + tRNAHis + tRNALeu + tRNAPro + ?
tRNAAsn precursor + H2O
?
-
-
-
-
?
tRNAGlyCysLeu precursor + H2O
tRNAGly + tRNACys + tRNALeu + ?
tRNAHis precursor + H2O
?
-
-
-
-
?
tRNAPhe precursor + H2O
?
-
-
-
-
?
tRNAPro precursor + H2O
?
-
-
-
-
?
tRNATyr precursor + H2O
tRNATyr + ?
-
maturation, cleavage of the tyrT transcript, containing two tRNATyr1 sequences separated by a 209-nt spacer region plus a downstream mRNA, at three sites in the speacer region, overview
-
-
?
tRNATyrSu3 precursor + H2O
?
-
cleavage in the 5' leader sequence, the enzyme is involved in regulation of cellular tRNA levels
-
-
?
unc mRNA + H2O
?
-
the unc operon encodes the eight subunits of the Escherichia coli F1F0-ATPase, processing of the unc mRNAs by the RNase E, overview, RNase E is essential for uncC processing
-
-
?
upRNA + H2O
?
-
RNase E is a processing enzyme involved in 3' end formation of M1 RNA, and plays a dual role in processing and degradation to achieve tight control of M1 RNA biosynthesis
-
-
?
additional information
?
-
23S rRNA + H2O
?
-
RNase E is involved in 5'-end 23S rRNA processing, schematic overview, removal of an internal, transcribed spacer consisting of helices 9 and 10, RNase E is responsible for helix 10 processing, while helix 9 is excised by RNase III
-
-
?
23S rRNA + H2O
?
-
RNase E is involved in 5'-end 23S rRNA processing, schematic overview, removal of an internal, transcribed spacer consisting of helices 9 and 10, RNase E is responsible for helix 10 processing, while helix 9 is excised by RNase III
-
-
?
23S rRNA + H2O
?
-
RNase E is involved in 5'-end 23S rRNA processing, schematic overview, removal of an internal, transcribed spacer consisting of helices 9 and 10, RNase E is responsible for helix 10 processing, while helix 9 is excised by RNase III
-
-
?
9S rRNA precursor + H2O
5S rRNA + ?
-
-
-
-
?
9S rRNA precursor + H2O
5S rRNA + ?
-
-
-
-
?
9S-RNA + H2O
?
-
-
-
-
?
pre-5S rRNA + H2O
?
-
processing
-
-
?
pre-5S rRNA + H2O
?
-
processing
-
-
?
puf mRNA + H2O
?
-
degradation
-
-
?
puf mRNA + H2O
?
-
degradation
-
-
?
puf mRNA + H2O
?
-
degradation
-
-
?
RNA + H2O
?
-
the enzyme is required for RNA processing and degradation
-
-
?
RNA + H2O
?
-
the enzyme plays a key role in processing and degradation of RNA in Escherichia coli
-
-
?
RNA + H2O
?
-
RNase E processing of various precursor RNAs produces many small regulatory RNAs, constituting a major small-RNA biogenesis pathway in bacteria
-
-
?
rpsT mRNA + H2O
?
-
the substrate encodes the ribosomal protein S20
-
-
?
rpsT mRNA + H2O
?
-
the substrate encodes the ribosomal protein S20
-
-
?
tRNAArgHisLeuPro precursor + H2O
tRNAArg + tRNAHis + tRNALeu + tRNAPro + ?
-
polycistronic transcript, maturation, overview
-
-
?
tRNAArgHisLeuPro precursor + H2O
tRNAArg + tRNAHis + tRNALeu + tRNAPro + ?
-
polycistronic transcript, maturation, overview
-
-
?
tRNAGlyCysLeu precursor + H2O
tRNAGly + tRNACys + tRNALeu + ?
-
polycistronic transcript, maturation, cleavage downstream of each tRNA, overview
-
-
?
tRNAGlyCysLeu precursor + H2O
tRNAGly + tRNACys + tRNALeu + ?
-
polycistronic transcript, maturation, cleavage downstream of each tRNA, overview
-
-
?
additional information
?
-
-
RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region
-
-
?
additional information
?
-
-
RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region
-
-
?
additional information
?
-
-
Aquifex aeolicus RNase E/G is able to selectively cleave internucleotide bonds in the 3'-5' direction, and to cut in intercistronic regions of putative tRNA precursors
-
-
?
additional information
?
-
-
the bifunctional enzyme, exhibiting RNase E and RNase G activities, is involved in rRNA processing and maturation of tRNAs, that originated from polycistronic transcripts encoded by the Aquifex aeolicus tufA2 and rRNA operons, overview
-
-
?
additional information
?
-
-
RNA degradation in the chloroplast occurs via the polyadenylation-assisted degradation pathway, plant RNase E participates in the initial endonucleolytic cleavage of the polyadenylation-stimulated RNA degradation process in the chloroplast, perhaps in collaboration with the two other chloroplast endonucleases, RNase J and CSP41, overview
-
-
?
additional information
?
-
-
initiation of tRNA 5' maturation by RNase E is essential for cell viability, the enzyme initiates the processing of polycistronic RNA of several operons, e.g. of glyW cysT leuZ, argX hisR leuT proM, or lysT valT lysW valZ lysY lysZlysQ, as well as of monocistronic transcripts such as pheU, pheV, asnT, asnU, asnV, or asnW, mapping of cleavage sites at the 3' end within tRNA precursors, overview, the enzyme is essential for degradation of many mRNAs, e.g. of rpsO
-
-
?
additional information
?
-
-
RNase E is involved in and interacts with functionally and physically polynucleotide phosphorylase, and also with other enzymes implicated in the processing and degradation of RNA, polynuclease phosphorylase, PNPase, degrades the reaction products generated by RNase E
-
-
?
additional information
?
-
-
the enzyme is essential for regulation of mRNA turnover by specific processing and degradation and is involved in regulation of cell homeostasis, growth and development
-
-
?
additional information
?
-
the enzyme is essential for regulation of mRNA turnover by specific processing and degradation and is involved in regulation of cell homeostasis, growth and development
-
-
?
additional information
?
-
-
the enzyme is part of the RNA degradosome, a large multiprotein machine to process and degrade RNA
-
-
?
additional information
?
-
-
the enzyme is required for rapid decay and correct hydrolytic processing of RNA
-
-
?
additional information
?
-
-
the enzyme is the major endoribonuclease participating in mRNA turnover in Escherichia coli
-
-
?
additional information
?
-
-
the enzyme plays an important role in the processing and degradation of bacteriophage T4 and Escherichia coli mRNAs, mutational processing site analysis, overview
-
-
?
additional information
?
-
-
the enzyme, especially its catalytic N-terminal domain, is essential for RNA processing and degradation, and for cell growth and feedback regulation of RNase E synthesis
-
-
?
additional information
?
-
-
both RNase E and RNase III control the stability of sodB mRNA upon translational inhibition by the small regulatory RNA RyhB, iron-dependent variations in the steady-state concentration and translatability of sodB mRNA are modulated by the small regulatory RNA RyhB, the RNA chaperone Hfq, and RNase E, decay of sodB mRNA is retarded upon inactivation of RNaseE in vivo, mechanism, modelling, overview
-
-
?
additional information
?
-
ribonuclease E is an essential hydrolytic endonuclease in Escherichia coli, and it plays a central role in maintaining the balance and composition of the messenger RNA population
-
-
?
additional information
?
-
-
ribonuclease E is an essential hydrolytic endonuclease in Escherichia coli, and it plays a central role in maintaining the balance and composition of the messenger RNA population
-
-
?
additional information
?
-
RNase E is an essential bacterial endoribonuclease involved in the turnover of messenger RNA and the maturation of structured RNA precursors in Escherichia coli, RNA degradation mechanism, overview
-
-
?
additional information
?
-
-
RNase E is an essential bacterial endoribonuclease involved in the turnover of messenger RNA and the maturation of structured RNA precursors in Escherichia coli, RNA degradation mechanism, overview
-
-
?
additional information
?
-
-
RNase E is an essential endonuclease involved in the regulatory processing and/or degradation of tRNAs, rRNAs, and non-coding small RNAs as well as many mRNAs, the enzyme is regulated by an RNA-binding protein Hfq. RNase is required for induction of the glutamate-dependent acid resistance system in a RpoS-independent manner
-
-
?
additional information
?
-
RNase E is an essential Escherichia coli endoribonuclease that plays a major role in the decay and processing of a large fraction of RNAs in the cell, overview
-
-
?
additional information
?
-
-
RNase E is an essential Escherichia coli endoribonuclease that plays a major role in the decay and processing of a large fraction of RNAs in the cell, overview
-
-
?
additional information
?
-
-
RNaseE, as the main component of the RNA degradosome of Escherichia coli, plays an essential role in RNA processing and decay
-
-
?
additional information
?
-
-
the balance and composition of the transcript population is affected by RNase E, an essential endoribonuclease that not only turns over RNA but also processes certain key RNA precursors
-
-
?
additional information
?
-
the balance and composition of the transcript population is affected by RNase E, an essential endoribonuclease that not only turns over RNA but also processes certain key RNA precursors
-
-
?
additional information
?
-
-
the enzyme is the major endoribonuclease participating in mRNA turnover in Escherichia coli
-
-
?
additional information
?
-
-
RNase E plays an essential role in the maturation of tRNA precursors, cleavage site and maturation process modeling, overview
-
-
?
additional information
?
-
-
RNase E plays an essential role in the maturation of tRNA precursors, cleavage site and maturation process modeling, overview
-
-
?
additional information
?
-
-
RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region
-
-
?
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evolution
characterization of the RNase E-PNPase interaction in alpha-proteobacteria, gamma-proteobacteria and cyanobacteria suggests that it arose independently several times during evolution, thus conferring an advantage in control and coordination of RNA processing and degradation
evolution
-
characterization of the RNase E-PNPase interaction in alpha-proteobacteria, gamma-proteobacteria and cyanobacteria suggests that it arose independently several times during evolution, thus conferring an advantage in control and coordination of RNA processing and degradation
-
malfunction
-
RNAI signals of the DELTA225 mutant lacking the PNPase binding region are similar to those of the wild-type strain. RNAI degradation intermediate accumulates in the DELTA374 mutant lacking the PNPase binding region and protein scaffold domain, which binds to RhlB and enolase, as compared with that in the wild-type strain
malfunction
-
absence of RNase E differentially affects the decay of specific mRNAs. Neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneD1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the predicted RNase H domain of RNase G, generating the rng-219 and rng-248 alleles, result in complementation of the growth defect associated with various RNase E mutants
malfunction
-
an NCgl2281 knockout mutant accumulates 5S rRNA precursor molecules. The processing of 16S and 23S rRNA, tRNA, and tmRNA is normal in the mutant cells. Primer extension analysis reveals that the RNase E/G orthologue cleaves at the -1 site of the 5' end of 5S rRNA. Mapping of the 5' and 3' ends of 5S rRNA precursors in NCgl2281 knockout mutant, overview
malfunction
-
mutations in endoribonucleases RNase E reduce Salmonella virulence capacity. Mutants display an impaired motility, by forming a barely detectable motility ring after 8 h of incubation that remains much smaller than the one formed by the wild type after 24 h of incubation
malfunction
-
RNase E deletion or inactivation of temperature-sensitive RNase E protein precludes normal initiation of the SOS response. RNase E-deficient cells remain able to produce RNA and protein during the period when SOS response is inhibited by lack of the enzyme
malfunction
-
an NCgl2281 knockout mutant accumulates 5S rRNA precursor molecules. The processing of 16S and 23S rRNA, tRNA, and tmRNA is normal in the mutant cells. Primer extension analysis reveals that the RNase E/G orthologue cleaves at the -1 site of the 5' end of 5S rRNA. Mapping of the 5' and 3' ends of 5S rRNA precursors in NCgl2281 knockout mutant, overview
-
metabolism
-
the endoribonuclease RNase E of Escherichia coli is an essential enzyme that plays a major role in all aspects of RNA metabolism
metabolism
-
direct entry by RNase E has a major role in bacterial RNA metabolism. Direct entry is mediated by specific unpaired regions that are adjacent to, but not contiguous with, segments cleaved by RNase E. A 5'-monophosphate is not required to activate the catalytic step
metabolism
-
RNase E-dependent degradation of sinI mRNA from the 5'-end is one of the steps mediating a high turnover of sinI mRNA, which allows the Sin quorum-sensing system to respond rapidly to changes in transcriptional control of N-acyl-homoserine lactone production. RNase E acts on the 5'-untranslated region of sinI independently of the posttranscriptional regulator Hfq
metabolism
-
the enzyme is required for glycolysis
metabolism
-
RNase E-dependent degradation of sinI mRNA from the 5'-end is one of the steps mediating a high turnover of sinI mRNA, which allows the Sin quorum-sensing system to respond rapidly to changes in transcriptional control of N-acyl-homoserine lactone production. RNase E acts on the 5'-untranslated region of sinI independently of the posttranscriptional regulator Hfq
-
metabolism
-
the enzyme is required for glycolysis
-
physiological function
-
RNase E is involved in the post-transcriptional regulation of NifA expression. Host factor required-dependent RNase E cleavage is essential for NifA translation, probably by making ribosome-binding sites accessible
physiological function
RNase E microdomain sequences are well-conserved with those described in Escherichia coli. The RNase E C-terminal half is less conserved and structured than its N-terminal half. RNase E is a hub protein with multiple interaction interfaces that are under different evolutionary pressures. RNase E can rescue the temperature sensitive rne-1 phenotype of Escherichia coli
physiological function
-
NCgl2281 endoribonuclease is involved in the 5' maturation of 5S rRNA
physiological function
-
RNase E is a key component of the RNA degradosome, a multienzyme complex hat plays a central role in mRNA turnover and the processing of stable RNA in eubacteria. The degradosome is composed of a tetramer of RNase E molecules interacting via their N-terminal regions, with the C-terminal end of each RNase E molecule complexed with a monomer of RhlB, a dimer of enolase, and a trimer of PNPase
physiological function
-
RNase E is essential for cell viability and plays a major role in mRNA decay, rRNA maturation, tRNA processing, and a variety of other aspects of RNA metabolism. Maturation of tRNACys, tRNAHis, and tRNAPro but not tRNAAsn is completely dependent on RNase E
physiological function
-
RNase E is responsible for the functional interaction with Hfq to cause the sRNA-mediated destabilization of target mRNAs. the RNA chaperon Hfq along with Hfq-binding sRNAs stably binds to RNase E in Escherichia coli. The role of the Hfq-RNase E interaction is to recruit RNase E to target mRNAs of sRNAs resulting in the rapid degradation of the mRNA-sRNA hybrid. The C-terminal scaffold region of RNase E is responsible for the interaction with Hfq. Mutational interaction analysis, overview
physiological function
the phosphate sensor domain in the enzyme is required for efficient autoregulation of RNase E synthesis. Impact of the 5'-sensor on mRNA stability, overview
physiological function
the role in the CRISPR-mediated anti-phage defense might involve degradation of phage or cellular mRNAs
physiological function
both the full-length and the N-terminal part of RNase EV functionally complement Escherichia coli RNase E and their expression consequently supports normal growth of RNase E-depleted Escherichia coli cells. Escherichia coli cells expressing N-RneV show copy numbers of ColE1-type plasmid similar to that of Escherichia coli cells expressing N-Rne
physiological function
-
extraordinarily long antisense RNAs of 3.5 and 7 kb protect a set of mRNAs from RNase E degradation that accumulate during phage infection. These antisense RNA-mRNA duplex formations mask single-stranded recognition sites of RNase E, leading to increased stability of the mRNAs. The interactions directly modulate RNA stability and provide an explanation for enhanced transcript abundance of certain mRNAs during phage infection
physiological function
-
knockout mutant cells accumulate 5S rRNA precursor molecules. The processing of 16S and 23S rRNA, tRNA, and tmRNA is normal. RNase E/G cleaves at the -1 site of the 5' end of 5S rRNA. 3' maturation is essentially unaffected
physiological function
-
neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with RNase E deletion mutants even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the predicted RNase H domain of RNase G, generating the rng-219 and rng-248 alleles, result in complementation of the growth defect associated with various RNase E mutants, suggesting that this region of the two proteins may help distinguish their in vivo biological activities
physiological function
viable mutations affecting the 5'-phosphate sensor of RNase E, including R169Q or T170A, become lethal when combined with deletions removing part of the non-catalytic C-terminal domain of RNase E. The phosphate sensor is required for efficient autoregulation of RNase E synthesis as RNase E R169Q is strongly overexpressed with accumulation of proteolytic fragments. In addition, mutation of the phosphate sensorstabilizes the rpsT P1 mRNA as much as sixfold and slows the maturation of 16S rRNA. The decay of other model mRNAs and the processing of several tRNA precursors are unaffected by mutations in the phosphate sensor
physiological function
-
Escherichia coli cells normally require RNase E activity to form colonies
physiological function
-
RNase E function is required to mount a normal SOS response
physiological function
Escherichia coli messenger RNAs are rapidly degraded immediately after bacteriophage T4 infection, and the host RNase E contributes to this process
physiological function
-
in the degradation pathway of mRNA for Escherichia coli, the initial cleavage of a transcript by RNase E is followed closely by exonucleolytic degradation of the products by PNPase (polynucleotide phosphorylase), RNase II, or RNase R
physiological function
in the degradation pathway of mRNA for Escherichia coli, the initial cleavage of a transcript by RNase E is followed closely by exonucleolytic degradation of the products by PNPase (polynucleotide phosphorylase), RNase II, or RNase R
physiological function
-
proline tRNAs are matured at the 3' end primarily by a direct RNase E endonucleolytic cleavage. RNase E is primarily responsible for the endonucleolytic removal of the entire Rho-independent transcription terminator associated with the proK, proL and proM primary transcripts by cleaving immediately downstream of the CCA determinant
physiological function
RNase E carries out the cleavages that initiate the degradation pathways of rRNA in the quality control process and during starvation
physiological function
RNase E endonuclease is the crRNA maturation enzyme in a CRISPR-Cas subtype III-Bv system. Overexpression of RNase E leads to overaccumulation and knock-down to the reduced accumulation of crRNAs in vivo. RNase E is the limiting factor for CRISPR complex formation
physiological function
RNase E is a central ribonuclease of RNA metabolism and post-transcriptional control of gene expression
physiological function
RNase E is involved in the processing and degradation of nearly every transcript in Escherichia coli
physiological function
RNase E is necessary to maintain the normal abundance of phosphoenolpyruvate synthetase (PpsA) in Escherichia coli. PpsA links the TCA cycle with glycolytic pathway for gluconeogenesis by converting pyruvate to phosphoenolpyruvate. RNase E may function to maintain appropriate carbon flux around phosphoenolpyruvate in Escherichia coli
physiological function
-
RNase E processing of various precursor RNAs produces many small regulatory RNAs, constituting a major small-RNA biogenesis pathway in bacteria
physiological function
RNaseE is the main component of the RNA degradosome of Escherichia coli, which plays an essential role in RNA processing and decay
physiological function
the enzyme is an essential bacterial endoribonuclease with a central role in processing tRNAs and rRNA, and turning over mRNAs
physiological function
the enzyme is required for S-adenosylmethionine homeostasis in Sinorhizobium meliloti
physiological function
the enzyme participates in most aspects of RNA processing and degradation
physiological function
-
the enzyme plays an important role in RNA processing and decay in Escherichia coli
physiological function
-
RNase E is involved in the post-transcriptional regulation of NifA expression. Host factor required-dependent RNase E cleavage is essential for NifA translation, probably by making ribosome-binding sites accessible
-
physiological function
-
the role in the CRISPR-mediated anti-phage defense might involve degradation of phage or cellular mRNAs
-
physiological function
-
the enzyme is required for S-adenosylmethionine homeostasis in Sinorhizobium meliloti
-
physiological function
-
extraordinarily long antisense RNAs of 3.5 and 7 kb protect a set of mRNAs from RNase E degradation that accumulate during phage infection. These antisense RNA-mRNA duplex formations mask single-stranded recognition sites of RNase E, leading to increased stability of the mRNAs. The interactions directly modulate RNA stability and provide an explanation for enhanced transcript abundance of certain mRNAs during phage infection
-
physiological function
-
RNaseE is the main component of the RNA degradosome of Escherichia coli, which plays an essential role in RNA processing and decay
-
physiological function
-
Escherichia coli cells normally require RNase E activity to form colonies
-
physiological function
-
the enzyme participates in most aspects of RNA processing and degradation
-
physiological function
-
in the degradation pathway of mRNA for Escherichia coli, the initial cleavage of a transcript by RNase E is followed closely by exonucleolytic degradation of the products by PNPase (polynucleotide phosphorylase), RNase II, or RNase R
-
physiological function
-
RNase E is a central ribonuclease of RNA metabolism and post-transcriptional control of gene expression
-
physiological function
-
RNase E is involved in the processing and degradation of nearly every transcript in Escherichia coli
-
physiological function
-
RNase E carries out the cleavages that initiate the degradation pathways of rRNA in the quality control process and during starvation
-
physiological function
-
RNase E is necessary to maintain the normal abundance of phosphoenolpyruvate synthetase (PpsA) in Escherichia coli. PpsA links the TCA cycle with glycolytic pathway for gluconeogenesis by converting pyruvate to phosphoenolpyruvate. RNase E may function to maintain appropriate carbon flux around phosphoenolpyruvate in Escherichia coli
-
physiological function
-
Escherichia coli messenger RNAs are rapidly degraded immediately after bacteriophage T4 infection, and the host RNase E contributes to this process
-
physiological function
-
proline tRNAs are matured at the 3' end primarily by a direct RNase E endonucleolytic cleavage. RNase E is primarily responsible for the endonucleolytic removal of the entire Rho-independent transcription terminator associated with the proK, proL and proM primary transcripts by cleaving immediately downstream of the CCA determinant
-
physiological function
-
NCgl2281 endoribonuclease is involved in the 5' maturation of 5S rRNA
-
physiological function
-
knockout mutant cells accumulate 5S rRNA precursor molecules. The processing of 16S and 23S rRNA, tRNA, and tmRNA is normal. RNase E/G cleaves at the -1 site of the 5' end of 5S rRNA. 3' maturation is essentially unaffected
-
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A326T
random mutagenesis, mutation in the DNase I subdomain, the mutant shows no detectable binding to p23 RNA due to a reduction in the substrate-binding ability
C404A
site-directed mutagenesis, mutation of a zinc binding residue, the mutant shows 200fold decreased activity relative to that of the wild-type enzyme for cleaving a 10-mer RNA substrate, and forms a dimer instead of a tetramer
C407A
site-directed mutagenesis, mutation of a zinc binding residue, the mutant shows 200fold decreased activity relative to that of the wild-type enzyme for cleaving a 10-mer RNA substrate, and forms a dimer instead of a tetramer
D303C
mutation results in nearly full loss of activity regardless of metal ion
D303N
site-directed mutagenesis of a residue located on the surface of the subdomain of RNase E, the mutant shows about 25fold reduced catalytic activity but almost unaltered RNA binding compared to the wild-type enzyme
D346C
the mutation leads to almost complete loss of activity dependent on Mg2+. The activity of the mutant enzyme is fully restored by the presence of Mn2+ with kinetic parameters fully equivalent to those of wild-type enzyme
E R169Q
mutant protein is strongly overexpressed with accumulation of proteolytic fragments
F186C
-
site-directed mutagenesis of a point mutation in the S1 RNA-binding domain of RNase E, which leads to temperature-sensitive growth along with defects in 5S rRNA processing, mRNA decay, and tRNA maturation, intragenic suppressors, rne-172, rne-186 and rne-187 alleles, of the temperature-sensitive rne mutant allele cause the dissociation of RNase E activity on mRNA and tRNA or rRNA substrates in Escherichia coli. Specifically, tRNA maturation and 9S rRNA processing are restored to wild-type levels in suppressor mutants, while mRNA decay remains defective, phenotypes, overview
G172A
-
site-directed mutagenesis of a point mutation in the S1 RNA-binding domain of RNase E, which leads to temperature-sensitive growth along with defects in 5S rRNA processing, mRNA decay, and tRNA maturation, intragenic suppressors, rne-172, rne-186 and rne-187 alleles, of the temperature-sensitive rne mutant allele cause the dissociation of RNase E activity on mRNA and tRNA or rRNA substrates in Escherichia coli. Specifically, tRNA maturation and 9S rRNA processing are restored to wild-type levels in suppressor mutants, while mRNA decay remains defective, phenotypes, overview
G66S
site-directed mutagenesis, the mutation leads to a dramatic destabilization of the OB fold of the S1 domain and leads to increased temperature sensitivity of the mutant compared to the wild-type enzyme
I41N
random mutagenesis, mutation in the SI subdomain, the mutant shows no detectable binding to p23 RNA due to a reduction in the substrate-binding ability
K106A
-
site-directed mutagenesis, 60% reduced feedback regulation activity compared to the wild-type enzyme
K112A
-
site-directed mutagenesis, 94% reduced feedback regulation activity compared to the wild-type enzyme
K37A
-
site-directed mutagenesis, 94% reduced feedback regulation activity compared to the wild-type enzyme
K38A
-
site-directed mutagenesis, 49% reduced feedback regulation activity compared to the wild-type enzyme
K43A
-
site-directed mutagenesis, 33% reduced feedback regulation activity compared to the wild-type enzyme
K71A
-
site-directed mutagenesis, 56% reduced feedback regulation activity compared to the wild-type enzyme
L112A
site-directed mutagenesis of a residue located at the hydrophobic pocket on the surface of the S1 domain, the mutant shows about 50fold reduced catalytic activity compared to the wild-type enzyme
L385P
random mutagenesis, mutation in the DNase I subdomain, the mutant shows no detectable binding to p23 RNA due to a reduction in the substrate-binding ability
N305L
site-directed mutagenesis of a residue located on the surface of the subdomain of RNase E, the mutant shows reduced catalytic activity compared to the wild-type enzyme
Q36R
-
the mutant is hyperactive in comparison to wild type enzyme. The mutation enhances the RNA binding to the catalytic site of the enzyme
R109A
-
site-directed mutagenesis, 78% reduced feedback regulation activity compared to the wild-type enzyme
R1269Q/DELTA530-1061
mutation is lethal
R1269Q/DELTA589-1061
mutation is lethal
R1269Q/DELTA730-1061
mutant is viable
R169Q
site-directed mutagensis, the viable mutation in the 5'-phosphate sensor of RNase E, becomes lethal in combination with deletions removing part of the non-catalytic C-terminal domain of RNase E. Loss of autoregulation in R169Q
R187L
-
site-directed mutagenesis of a point mutation in the S1 RNA-binding domain of RNase E, which leads to temperature-sensitive growth along with defects in 5S rRNA processing, mRNA decay, and tRNA maturation, intragenic suppressors, rne-172, rne-186 and rne-187 alleles, of the temperature-sensitive rne mutant allele cause the dissociation of RNase E activity on mRNA and tRNA or rRNA substrates in Escherichia coli. Specifically, tRNA maturation and 9S rRNA processing are restored to wild-type levels in suppressor mutants, while mRNA decay remains defective, phenotypes, overview
R48A
-
site-directed mutagenesis, 49% reduced feedback regulation activity compared to the wild-type enzyme
R64A
-
site-directed mutagenesis, 77% reduced feedback regulation activity compared to the wild-type enzyme
R87A
-
site-directed mutagenesis, 16% increased feedback regulation activity compared to the wild-type enzyme
R95A
-
site-directed mutagenesis, 19% increased feedback regulation activity compared to the wild-type enzyme
T170A
site-directed mutagensis, the viable mutation in the 5'-phosphate sensor of RNase E, becomes lethal in combination with deletions removing part of the non-catalytic C-terminal domain of RNase E
T170A/DELTA530-1061
mutant is viable, with small colony sizes
T170A/DELTA589-1061
mutant is viable, with small colony sizes
Y25A
-
the mutant is hypoactive in comparison to wild type enzyme. The mutation increases the RNA binding to the multimer formation interface between amino acid residues 427 and 433
Y42A
-
site-directed mutagenesis, 48% reduced feedback regulation activity compared to the wild-type enzyme
Y60A
-
site-directed mutagenesis, 99% reduced feedback regulation activity compared to the wild-type enzyme
Y77A
-
site-directed mutagenesis, 19% reduced feedback regulation activity compared to the wild-type enzyme
D303C
-
mutation results in nearly full loss of activity regardless of metal ion
-
D346C
-
the mutation leads to almost complete loss of activity dependent on Mg2+. The activity of the mutant enzyme is fully restored by the presence of Mn2+ with kinetic parameters fully equivalent to those of wild-type enzyme
-
N305D
-
the mutation is localized in the catalytic domain of RNase E
-
Q36R
-
the mutant is hyperactive in comparison to wild type enzyme. The mutation enhances the RNA binding to the catalytic site of the enzyme
-
Y25A
-
the mutant is hypoactive in comparison to wild type enzyme. The mutation increases the RNA binding to the multimer formation interface between amino acid residues 427 and 433
-
F186C
-
site-directed mutagenesis of a point mutation in the S1 RNA-binding domain of RNase E, which leads to temperature-sensitive growth along with defects in 5S rRNA processing, mRNA decay, and tRNA maturation, intragenic suppressors, rne-172, rne-186 and rne-187 alleles, of the temperature-sensitive rne mutant allele cause the dissociation of RNase E activity on mRNA and tRNA or rRNA substrates in Escherichia coli. Specifically, tRNA maturation and 9S rRNA processing are restored to wild-type levels in suppressor mutants, while mRNA decay remains defective, phenotypes, overview
-
G172A
-
site-directed mutagenesis of a point mutation in the S1 RNA-binding domain of RNase E, which leads to temperature-sensitive growth along with defects in 5S rRNA processing, mRNA decay, and tRNA maturation, intragenic suppressors, rne-172, rne-186 and rne-187 alleles, of the temperature-sensitive rne mutant allele cause the dissociation of RNase E activity on mRNA and tRNA or rRNA substrates in Escherichia coli. Specifically, tRNA maturation and 9S rRNA processing are restored to wild-type levels in suppressor mutants, while mRNA decay remains defective, phenotypes, overview
-
R187L
-
site-directed mutagenesis of a point mutation in the S1 RNA-binding domain of RNase E, which leads to temperature-sensitive growth along with defects in 5S rRNA processing, mRNA decay, and tRNA maturation, intragenic suppressors, rne-172, rne-186 and rne-187 alleles, of the temperature-sensitive rne mutant allele cause the dissociation of RNase E activity on mRNA and tRNA or rRNA substrates in Escherichia coli. Specifically, tRNA maturation and 9S rRNA processing are restored to wild-type levels in suppressor mutants, while mRNA decay remains defective, phenotypes, overview
-
D10A
inactive mutant enzyme
D13A
mutant enzyme shows wild-type level activity
D14A
mutant enzyme shows wild-type level activity
D65A
2fold drop in activity compared to wild-type
F37A
inactive mutant enzyme
N18A
mutant enzyme shows wild-type level activity
Q33A
slightly reduced activity
R31A
inactive mutant enzyme
R67A
mutant enzyme shows wild-type level activity
S35A
slightly reduced activity
T12A
2fold drop in activity compared to wild-type
Y34A
slightly reduced activity
D10A
-
inactive mutant enzyme
-
D13A
-
mutant enzyme shows wild-type level activity
-
R19A
-
very low activity
-
R31A
-
inactive mutant enzyme
-
R67A
-
mutant enzyme shows wild-type level activity
-
A448V
-
site-directed mutagensis, the mutation causes steric problemes and leads to conformational changes
C471Y
-
site-directed mutagensis, the mutation causes steric problemes and leads to conformational changes
G113D
-
site-directed mutagensis, the mutation causes steric problemes and leads to conformational changes
L424R
-
site-directed mutagensis, the mutation reduces the nonpolar contacts in the core, which may lead to a less stable protein
V459G
-
site-directed mutagensis, the mutation reduces the nonpolar contacts in the core, which may lead to a less stable protein
D346N
site-directed mutagenesis of a residue located on the surface of the subdomain of RNase E, the mutant shows about 25fold reduced catalytic activity but almost unaltered RNA binding compared to the wild-type enzyme
D346N
N-terminal half-RNase E mutant, at micromolar concentrations of enzyme, cleavage of cspA mRNA occurs to a detectable level: at several positions the primer extension reactions terminate independent of acylation
F57A
-
site-directed mutagenesis, 91% reduced feedback regulation activity compared to the wild-type enzyme
F57A
site-directed mutagenesis of a residue located at the hydrophobic pocket on the surface of the S1 domain, the mutant shows about 50fold reduced catalytic activity compared to the wild-type enzyme
F67A
-
site-directed mutagenesis, 94% reduced feedback regulation activity compared to the wild-type enzyme
F67A
site-directed mutagenesis of a residue located at the hydrophobic pocket on the surface of the S1 domain, the mutant shows about 50fold reduced catalytic activity compared to the wild-type enzyme
N305D
site-directed mutagenesis of a residue located on the surface of the subdomain of RNase E, the mutant shows reduced catalytic activity compared to the wild-type enzyme
N305D
-
the mutation is localized in the catalytic domain of RNase E
T170V
5'-end-sensing mutant of N-terminal half-RNase E, mRNA of cspA is still cleaved rapidly when incubated with the mutant. Relative to wild-type, the mutant cleaves 5'-monophosphorylated BR13 more than 15fold slower, without an obvious effect on the rate of cleavage of the 5'-hydroxylated equivalent
T170V
-
the mutant can cleave a 5'-triphosphorylated transcript efficiently at E3 or E5, but not both
T170V
-
the mutant shows considerably reduced activity compared to the wild type enzyme
A327P
-
site-directed mutagensis, temperature-sensitive mutant
A327P
-
mutation in N-terminal part of enzyme, temperature-sensitive mutation that is able to suppress the slow growth caused by the mutation tufA499 at permissive temperatures. In addition, mutation causes a large increase 503 in rne mRNA steady state levels
G66C
-
site-directed mutagensis, temperature-sensitive mutant, the mutation causes steric problemes and leads to conformational changes
G66C
-
mutation in N-terminal part of enzyme, temperature-sensitive mutation that is able to suppress the slow growth caused by the mutation tufA499 at permissive temperatures. In addition, mutation causes a large increase 503 in rne mRNA steady state levels
I207N
-
site-directed mutagensis, temperature-sensitive mutant, the mutation reduces the nonpolar contacts in the core, which may lead to a less stable protein
I207N
-
mutation in N-terminal part of enzyme, temperature-sensitive mutation that is able to suppress the slow growth caused by the mutation tufA499 at permissive temperatures. In addition, mutation causes a large increase 503 in rne mRNA steady state levels
I207S
-
site-directed mutagensis, temperature-sensitive mutant, the mutation reduces the nonpolar contacts in the core, which may lead to a less stable protein
I207S
-
mutation in N-terminal part of enzyme, temperature-sensitive mutation that is able to suppress the slow growth caused by the mutation tufA499 at permissive temperatures. In addition, mutation causes a large increase 503 in rne mRNA steady state levels
additional information
-
16S rRNA 5' maturation is reduced in an rne mutant, altered in a cafA mutant and completely blocked in an rne/cafA double mutant, phenotype, overview
additional information
-
construction of the rneDELTA645 allele with an introduced stop codon, the mutant strain shows reduced mRNA decay compared to rne wild-type or overexpressing strains
additional information
-
functional analysis of enzyme domains by using deletion mutants of RNase E, interaction with degradosome components, overview
additional information
-
modification of the RNase E recognition sequence at position 1205 within pufL affects the enzyme activity with substrate puf mRNA, overview
additional information
-
mutation of gene rne affect the rate of mRNA decay in vivo, construction of a truncated 110 kDa mutant enzyme
additional information
-
rne is an essential gene, its overexpression interferes with cell growth and viability
additional information
-
computational molecular modelling of mutation suppression, overview
additional information
-
construction of truncated enzyme forms comprising residues 628-843 and 694-790
additional information
-
genetic screen with a Tn5 transposon library to identify Escherichia coli functions involved in retromobility of the Lactobacillus lactis LtrB intron, i.e. a group II intron recruiting cellular polymerases, nucleases, and DNA ligase to complete the retromobility process in Escherichia coli, isolation of an rne promoter region mutant with elevated retrohoming and retrotransposition levels, overview
additional information
-
retention of core catalytic functions by a conserved minimal ribonuclease E peptide that lacks the domain required for tetramer formation, RNase E derivatives that are as short as 395 amino acid residues and that lack the Zn-link region shown previously to be essential for tetramer formation, residues 400-415, are catalytically active enzymes that retain the 5' to 3' scanning ability and cleavage site specificity characteristic of full-length RNase E and that also confer colony forming ability on rne null mutant bacteria. Further truncation leads to loss of these properties. A minimal catalytically active RNase E sequence proofs that a tetrameric quaternary structure is not required for RNase E to carry out its core enzymatic functions
additional information
-
rne-1 mutants show abolished regulatory protein GadY expression at 42°C, but normal RpoS expression, phenotypes of rne-1 and rne-1/hfq mutant strains, overview
additional information
-
the constructed rne mutant strains AT8, i.e. Prne-rne1-417, and AT14, i.e. Prne-rne1-659, show loss of the helical protein organization and reduced activity, AT8 cells grow slowly and show a defect in cell division as shown by a mixed population ranging from normal-length cells to long filaments, AT8 cells exhibit a chromosome segregation defect, phenotypes, overview
additional information
-
the half-life of cspA mRNA is nearly twofold longer in rne-1 knockout strains KCB1008 and SK5665
additional information
-
neither the native nor N-terminal extended form of RNase G can restore the growth defect associated with either the rne-1 or rneD1018 alleles even when expressed at very high protein levels. In contrast, two distinct spontaneously derived single amino acid substitutions within the predicted RNase H domain of RNase G, generating the rng-219 and rng-248 alleles, result in complementation of the growth defect associated with various RNase E mutants. Construction of rneD1018/rng-219 and rneD1018/rng-248 double mutants. Domain swaps between RNase E and RNase G generate proteins that do not complement RNase E deficiency
additional information
-
the scaffold region of RNase E to bind Hfq can be deleted up to residue 750 without losing the ability to cause the rapid degradation of target mRNAs mediated by Hfq/sRNAs. The truncated RNase E750 can still bind to Hfq although the truncation significantly reduces the Hfq-binding ability. Deletion of the 702-750 region greatly impairs the ability of RNase E to cause the degradation of ptsG mRNA
additional information
-
viable mutations affecting the 5'-phosphate sensor of RNase E, including R169Q or T170A, become lethal when combined with deletions removing part of the non-catalytic C-terminal domain of RNase E. Mutation of the phosphate sensor stabilizes the rpsT P1 mRNA as much as sixfold and slows the maturation of 16S rRNA. In contrast, the decay of other model mRNAs and the processing of several tRNA precursors are unaffected by mutations in the phosphate sensor
additional information
viable mutations affecting the 5'-phosphate sensor of RNase E, including R169Q or T170A, become lethal when combined with deletions removing part of the non-catalytic C-terminal domain of RNase E. Mutation of the phosphate sensor stabilizes the rpsT P1 mRNA as much as sixfold and slows the maturation of 16S rRNA. In contrast, the decay of other model mRNAs and the processing of several tRNA precursors are unaffected by mutations in the phosphate sensor
additional information
-
deletion of residues C-terminal to position 529 in the absence of other mutations still permit growth of cells. Deletion strain exhibits smaller colony size and reduced growth rates in liquid media. Additional shorter deletions spanning individual microdomains in the C-terminal scaffold region including the Arg-rich region, residues 608-644, the extended Arg-rich region with a putative coil-coil domain, residues 589-723, the RhlB binding site, residues 698762, the enolase binding site, residues 833-850, or the PNPase binding site, residues 1021-1061, are viable, too
additional information
deletion of residues C-terminal to position 529 in the absence of other mutations still permit growth of cells. Deletion strain exhibits smaller colony size and reduced growth rates in liquid media. Additional shorter deletions spanning individual microdomains in the C-terminal scaffold region including the Arg-rich region, residues 608-644, the extended Arg-rich region with a putative coil-coil domain, residues 589-723, the RhlB binding site, residues 698762, the enolase binding site, residues 833-850, or the PNPase binding site, residues 1021-1061, are viable, too
additional information
-
The scaffold region of RNase E can be deleted up to residue 750 without losing the ability to cause the rapid degradation of target mRNAs mediated by Hfq/sRNAs. The truncated RNase E750 can still bind to Hfq although the truncation significantly reduces the Hfq-binding ability. Deletion of the 702-750 region greatly impairs the ability of RNase E to cause the degradation of ptsG mRNA. A polypeptide corresponding to the scaffold region binds to Hfq without the help of RNA. Overexpression of RhlB partially inhibits the Hfq binding to RNase E and the rapid degradation of ptsG mRNA
additional information
-
construction of the truncated mutant enzyme N-RNase E consisting of the N-terminal catalytic site, residues 1-498, an enzyme-deficient strain CJ1832 can be complemented by expression of SynRne of Synechocystis sp., but not by Escherichia coli CafA, i.e. RNase G
additional information
-
generation of RNase E-defective mutants and of RNase E/RNase P double mutants, inactivation leads to accumulation of uncleaved tRNA precursors, overview
additional information
-
generation of RNase E-defective mutants and of RNase E/RNase P double mutants, inactivation leads to accumulation of uncleaved tRNA precursors, overview
-
additional information
-
computational molecular modelling of mutation suppression, overview
-
additional information
-
modification of the RNase E recognition sequence at position 1205 within pufL affects the enzyme activity with substrate puf mRNA, overview
-
additional information
retention of core catalytic functions by a conserved minimal ribonuclease E peptide that lacks the domain required for tetramer formation, RNase E derivatives that are as short as 395 amino acid residues and that lack the Zn-link region shown previously to be essential for tetramer formation, residues 400-415, are catalytically active enzymes that retain the 5' to 3' scanning ability and cleavage site specificity characteristic of full-length RNase E and that also confer colony forming ability on rne null mutant bacteria. Further truncation leads to loss of these properties. A minimal catalytically active RNase E sequence proofs that a tetrameric quaternary structure is not required for RNase E to carry out its core enzymatic functions
additional information
-
retention of core catalytic functions by a conserved minimal ribonuclease E peptide that lacks the domain required for tetramer formation, RNase E derivatives that are as short as 395 amino acid residues and that lack the Zn-link region shown previously to be essential for tetramer formation, residues 400-415, are catalytically active enzymes that retain the 5' to 3' scanning ability and cleavage site specificity characteristic of full-length RNase E and that also confer colony forming ability on rne null mutant bacteria. Further truncation leads to loss of these properties. A minimal catalytically active RNase E sequence proofs that a tetrameric quaternary structure is not required for RNase E to carry out its core enzymatic functions
additional information
-
modification of the RNase E recognition sequence at position 1205 within pufL only slightly affects the enzyme activity with substrate puf mRNA, overview
additional information
-
identification of the EF-Tu mutation, tufA499, with a slow-groth phenotype, structural basis of properties of suppressors of the mutation, overview. Isolation and identification of temperature-sensitive mutations in RNase E that suppress the slow growth of tufA499. Mutations in rne affect the steady-state level of RNase E mRNA. The rne ts and ts suppressor mutations affect 9S to 5S rRNA processing, growrh profiles, overview. The ts mutations in RNase E affect the maturation of hisR tRNAHis
additional information
both the full-length and the N-terminal part of RNase EV (N-RneV) functionally complement Escherichia coli RNase E and their expression consequently supports normal growth of RNase E-depleted Escherichia coli cells
additional information
-
both the full-length and the N-terminal part of RNase EV (N-RneV) functionally complement Escherichia coli RNase E and their expression consequently supports normal growth of RNase E-depleted Escherichia coli cells
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Streptomyces coelicolor
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Escherichia coli
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Escherichia coli, Escherichia coli GM402 BL21(DE3)
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Escherichia coli
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Salmonella enterica
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Escherichia coli, Escherichia coli KSL2000
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Schuck, A.; Diwa, A.; Belasco, J.G.
RNase E autoregulates its synthesis in Escherichia coli by binding directly to a stem-loop in the rne 5' untranslated region
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Escherichia coli
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Singh, D.; Chang, S.J.; Lin, P.H.; Averina, O.V.; Kaberdin, V.R.; Lin-Chao, S.
Regulation of ribonuclease E activity by the L4 ribosomal protein of Escherichia coli
Proc. Natl. Acad. Sci. USA
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Escherichia coli
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Zhang, Y.; Hong, G.
Post-transcriptional regulation of NifA expression by Hfq and RNase E complex in Rhizobium leguminosarum bv. viciae
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Rhizobium leguminosarum bv. viciae, Rhizobium leguminosarum bv. viciae 8401/pRL1JI
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Erce, M.A.; Low, J.K.; March, P.E.; Wilkins, M.R.; Takayama, K.M.
Identification and functional analysis of RNase E of Vibrio angustum S14 and two-hybrid analysis of its interaction partners
Biochim. Biophys. Acta
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Escherichia coli (P21513), Escherichia coli, Photobacterium angustum S14 (Q1ZS71), Photobacterium angustum S14
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Zhou, L.; Zhao, M.; Wolf, R.Z.; Graham, D.E.; Georgiou, G.
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Mol. Microbiol.
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Escherichia coli (P21513), Escherichia coli
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Nishio, S.Y.; Itoh, T.
Arginine-rich RNA binding domain and protein scaffold domain of RNase E are important for degradation of RNAI but not for that of the Rep mRNA of the ColE2 plasmid
Plasmid
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Escherichia coli
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Nurmohamed, S.; McKay, A.R.; Robinson, C.V.; Luisi, B.F.
Molecular recognition between Escherichia coli enolase and ribonuclease E
Acta Crystallogr. Sect. D
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Escherichia coli, Escherichia coli (P21513)
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Maeda, T.; Wachi, M.
Corynebacterium glutamicum RNase E/G-type endoribonuclease encoded by NCgl2281 is involved in the 5 maturation of 5S rRNA
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Studies on a Vibrio vulnificus functional ortholog of Escherichia coli RNase E imply a conserved function of RNase E-like enzymes in bacteria
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Vibrio vulnificus (Q7MM07), Vibrio vulnificus
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Salmonella enterica
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Hfq binding at RhlB-recognition region of RNase E is crucial for the rapid degradation of target mRNAs mediated by sRNAs in Escherichia coli
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Escherichia coli
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Escherichia coli, Escherichia coli (P21513)
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Stazic, D.; Lindell, D.; Steglich, C.
Antisense RNA protects mRNA from RNase E degradation by RNA-RNA duplex formation during phage infection
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Prochlorococcus sp., Prochlorococcus sp. MED4
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Chung, D.H.; Min, Z.; Wang, B.C.; Kushner, S.R.
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Escherichia coli
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Beloglazova, N.; Brown, G.; Zimmerman, M.D.; Proudfoot, M.; Makarova, K.S.; Kudritska, M.; Kochinyan, S.; Wang, S.; Chruszcz, M.; Minor, W.; Koonin, E.V.; Edwards, A.M.; Savchenko, A.; Yakunin, A.F.
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Saccharolobus solfataricus (Q97YC2), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97YC2)
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Viegas, S.C.; Mil-Homens, D.; Fialho, A.M.; Arraiano, C.M.
The virulence of Salmonella enterica serovar Typhimurium in the insect model Galleria mellonella is impaired by mutations in RNase E and RNase III
Appl. Environ. Microbiol.
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Salmonella enterica
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Martinez, V.P.; Deho, G.; Simons, R.W.; Garcia-Mena, J.
Ribonuclease PH interacts with an acidic ribonuclease E site through a basic 80-amino acid domain
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Escherichia coli, Escherichia coli CA244
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Escherichia coli, Escherichia coli MG1655
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Clarke, J.E.; Kime, L.; Romero A, D.; McDowall, K.J.
Direct entry by RNase E is a major pathway for the degradation and processing of RNA in Escherichia coli
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Escherichia coli
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Escherichia coli
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Ribonuclease E modulation of the bacterial SOS response
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Escherichia coli
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Kim, D.; Song, S.; Lee, M.; Go, H.; Shin, E.; Yeom, J.H.; Ha, N.C.; Lee, K.; Kim, Y.H.
Modulation of RNase E activity by alternative RNA binding sites
PLoS ONE
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Escherichia coli, Escherichia coli KSL2003
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Murashko, O.N.; Kaberdin, V.R.; Lin-Chao, S.
Membrane binding of Escherichia coli RNase E catalytic domain stabilizes protein structure and increases RNA substrate affinity
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Escherichia coli
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Zhang, J.Y.; Deng, X.M.; Li, F.P.; Wang, L.; Huang, Q.Y.; Zhang, C.C.; Chen, W.L.
RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region
RNA
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Anabaena sp., Synechocystis sp., Anabaena sp. PCC 7120
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Tamura, M.; Honda, N.; Fujimoto, H.; Cohen, S.N.; Kato, A.
PpsA-mediated alternative pathway to complement RNase E essentiality in Escherichia coli
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Escherichia coli (P21513), Escherichia coli, Escherichia coli K12 (P21513)
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Kim, D.; Kim, Y.H.; Jang, J.; Yeom, J.H.; Jun, J.W.; Hyun, S.; Lee, K.
Functional Analysis of Vibrio vulnificus orthologs of Escherichia coli RraA and RNase E
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Rapid degradation of host mRNAs by stimulation of RNase E activity by Srd of bacteriophage T4
Genetics
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Escherichia coli (P21513), Escherichia coli, Escherichia coli K12 (P21513)
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Thompson, K.; Zong, J.; Mackie, G.
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Escherichia coli (P21513), Escherichia coli K12 (P21513)
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Richards, J.; Belasco, J.G.
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Escherichia coli
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RNase E and the high-fidelity orchestration of RNA metabolism
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Caulobacter vibrioides, Escherichia coli (P21513), Escherichia coli K12 (P21513)
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Baumgardt, K.; Melior, H.; Madhugiri, R.; Thalmann, S.; Schikora, A.; McIntosh, M.; Becker, A.; Evguenieva-Hackenberg, E.
RNase E and RNase J are needed for S-adenosylmethionine homeostasis in Sinorhizobium meliloti
Microbiology
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Sinorhizobium meliloti (A0A2J0Z3F8), Sinorhizobium meliloti, Sinorhizobium meliloti Rm2011 (A0A2J0Z3F8)
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Chao, Y.; Li, L.; Girodat, D.; Foerstner, K.U.; Said, N.; Corcoran, C.; ?miga, M.; Papenfort, K.; Reinhardt, R.; Wieden, H.J.; Luisi, B.F.; Vogel, J.
InVivo cleavage map illuminates the central role of RNase E in coding and non-coding RNA pathways
Mol. Cell
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Salmonella enterica
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Bandyra, K.J.; Wandzik, J.M.; Luisi, B.F.
Substrate recognition and autoinhibition in the central ribonuclease RNase E
Mol. Cell
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275-285.e4
2018
Escherichia coli (P21513), Escherichia coli K12 (P21513)
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Ait-Bara, S.; Carpousis, A.J.
RNA degradosomes in bacteria and chloroplasts classification, distribution and evolution of RNase E homologs
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Escherichia coli (P21513), Escherichia coli, Escherichia coli K12 (P21513)
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Hammarloef, D.L.; Bergman, J.M.; Garmendia, E.; Hughes, D.
Turnover of mRNAs is one of the essential functions of RNase E
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Salmonella enterica subsp. enterica serovar Typhimurium (Q8ZQ17)
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Behler, J.; Sharma, K.; Reimann, V.; Wilde, A.; Urlaub, H.; Hess, W.
The host-encoded RNase e endonuclease as the crRNA maturation enzyme in a CRISPR-Cas subtype III-Bv system
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Synechocystis sp. PCC 6803 (P72656)
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Mohanty, B.K.; Petree, J.R.; Kushner, S.R.
Endonucleolytic cleavages by RNase E generate the mature 3 termini of the three proline tRNAs in Escherichia coli
Nucleic Acids Res.
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Escherichia coli, Escherichia coli MG1693
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Taghbalout, A.; Rothfield, L.
RNaseE and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton
Proc. Natl. Acad. Sci. USA
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Escherichia coli (P21513), Escherichia coli, Escherichia coli K12 PB103 (P21513)
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Bayas, C.A.; Wang, J.; Lee, M.K.; Schrader, J.M.; Shapiro, L.; Moerner, W.E.
Spatial organization and dynamics of RNase E and ribosomes in Caulobacter crescentus
Proc. Natl. Acad. Sci. USA
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Caulobacter vibrioides
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Sulthana, S.; Basturea, G.N.; Deutscher, M.P.
Elucidation of pathways of ribosomal RNA degradation an essential role for RNase E
RNA
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Escherichia coli (P21513), Escherichia coli K12 (P21513)
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