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Literature summary for 3.1.13.1 extracted from

  • Garza-Sanchez, F.; Shoji, S.; Fredrick, K.; Hayes, C.S.
    RNase II is important for A-site mRNA cleavage during ribosome pausing (2009), Mol. Microbiol., 73, 882-897.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
pACYC184 derivative expressing RNase II, RNase II lacking cold shock domain-1 or mutant D209N under araBAD promoter. PACYC184 derivative expressing RNase R under araBAD promoter. RNase II and mutant D209N overexpressed from pET plasmid constructs in CH12 DELTArna cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
D209N catalytically inactive, is unable to complement RNase II deletion Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Purification (Commentary)

Purification (Comment) Organism
by centrifugation, ion exchange and hydrophobic interaction chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
mRNA + H2O purified RNase II is unable to directly catalyse A-site cleavage in vitro, RNase II-catalysed degradation of mRNA to the ribosome border is a prerequisite for A-site cleavage. Degrades ribosome-bound mRNA to positions +18 nucleotides downstream of the ribosomal A site Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
3'-5'exoribonuclease
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Escherichia coli
RNase II
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Escherichia coli
RNase R
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Escherichia coli

General Information

General Information Comment Organism
malfunction instead of A-site cleavage, translational pausing in DELTARNase II cells produces transcripts that are truncated +12 and +28 nucleotides downstream of the A-site codon. Deletion of RNase R has little effect on A-site cleavage. Polynucleotide phosphorylase overexpression restores A-site cleavage activity to DELTARNase II cells Escherichia coli
physiological function plays an important role in RelE-independent A-site cleavage Escherichia coli