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Information on EC 2.7.7.6 - DNA-directed RNA polymerase and Organism(s) Mus musculus
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2.7.7.6 DNA-directed RNA polymeraseIUBMB Comments
Catalyses DNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. In eukaryotes, three forms of the enzyme have been distinguished on the basis of sensitivity to alpha-amanitin, and the type of RNA synthesized. See also EC 2.7.7.19 (polynucleotide adenylyltransferase) and EC 2.7.7.48 (RNA-directed RNA polymerase).
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Word Map
- 2.7.7.6
- chromatin
- histone
- rrna
- strand
-
rnaps
- nucleosome
- tata
- drosophila
-
pausing
- pre-mrnas
- tbp
-
nucleolar
- bacteriophage
-
polyadenylation
-
single-stranded
-
cyclin-dependent
-
holoenzyme
- cyclin
-
spacers
- helicase
-
fidelity
- polya
-
coactivator
-
protein-coding
-
transactivation
- adenovirus
- xenopus
- ribonucleoproteins
-
sequence-specific
-
stall
-
pause
-
chip-seq
- vaccinia
-
multisubunit
-
ribozyme
- heptapeptide
- duplex
-
h3k4me3
-
spliceosome
- nucleoplasm
-
run-on
-
supercoiled
-
trimethylation
-
subcomplexes
-
exonuclease
- heterochromatin
-
translesion
- medicine
- primase
- molecular biology
- analysis
- diagnostics
- drug development
-
misincorporation
-
proofread
- synthesis
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
rna polymerase ii, pol ii, t7 rna polymerase, rna polymerase i, pol iii, rna polymerase iii, pol i, rnapii, rnap ii, dna-dependent rna polymerase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C RNA formation factors
-
-
-
-
chloroplast soluble RNA polymerase
-
-
-
-
deoxyribonucleic acid-dependent ribonucleic acid polymerase
-
-
-
-
DNA-dependent ribonucleate nucleotidyltransferase
-
-
-
-
DNA-dependent RNA nucleotidyltransferase
-
-
-
-
DNA-dependent RNA polymerase
-
-
-
-
nucleotidyltransferase, ribonucleate
-
-
-
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Pol II
-
-
-
-
ribonucleate nucleotidyltransferase
-
-
-
-
ribonucleate polymerase
-
-
-
-
ribonucleic acid formation factors, C
-
-
-
-
ribonucleic acid nucleotidyltransferase
-
-
-
-
ribonucleic acid polymerase
-
-
-
-
ribonucleic acid transcriptase
-
-
-
-
ribonucleic polymerase
-
-
-
-
ribonucleic transcriptase
-
-
-
-
RNA formation factors, C
-
-
-
-
RNA nucleotidyltransferase
-
-
-
-
RNA nucleotidyltransferase (DNA-directed)
-
-
-
-
RNA polymerase
-
-
-
-
RNA polymerase I
RNA polymerase II
RNA polymerase III
RNA transcriptase
-
-
-
-
RNAP
-
-
-
-
RNAP I
-
-
-
-
RNAP II
-
-
-
-
RNAP III
-
-
-
-
transcriptase
-
-
-
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RNA polymerase I
-
-
-
-
RNA polymerase II
-
-
-
-
RNA polymerase III
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
nucleoside-triphosphate:RNA nucleotidyltransferase (DNA-directed)
Catalyses DNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. In eukaryotes, three forms of the enzyme have been distinguished on the basis of sensitivity to alpha-amanitin, and the type of RNA synthesized. See also EC 2.7.7.19 (polynucleotide adenylyltransferase) and EC 2.7.7.48 (RNA-directed RNA polymerase).
CAS REGISTRY NUMBER
COMMENTARY
9014-24-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is DNA, epigenetic control of rDNA transcription, regulation system of RNA polymerase, detailed overview
-
-
?
additional information
?
-
-
intermittent hypoxia, a major pathological factor in the development of neural deficits associated with sleep-disordered breathing, regulates RNA polymerase II in hippocampus and prefrontal cortex. Chronic intermittent hypoxia, but not sustained hypoxia, stimulates hydroxylation of Pro1465 in large subunit of RNA polymerase II and phosphorylation of Ser5 of Rpb1, specifically in the CA1 region of the hippocampus and in the prefrontal cortex but not in other regions of the brain, requiring the von Hippel-Lindau tumor suppressor. Mice exposed to chronic IH demonstrated cognitive deficits related to dysfunction in those brain regions, overview
-
-
?
additional information
?
-
-
two distinct forms, Pol Ialpha and Pol Ibeta. Both forms are catalytically active, but only Pol Ibeta can assemble into productive transcription initiation complexes. Regulation of Pol I transcription during cell cycle progression involving cytokines, and structural organization of mammalian rDNA repeats and the basal factors required for transcription initiation, overview. The activity of basal Pol I factors is regulated by posttranslational modifications
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
template is DNA, epigenetic control of rDNA transcription, regulation system of RNA polymerase, detailed overview
-
-
?
additional information
?
-
-
intermittent hypoxia, a major pathological factor in the development of neural deficits associated with sleep-disordered breathing, regulates RNA polymerase II in hippocampus and prefrontal cortex. Chronic intermittent hypoxia, but not sustained hypoxia, stimulates hydroxylation of Pro1465 in large subunit of RNA polymerase II and phosphorylation of Ser5 of Rpb1, specifically in the CA1 region of the hippocampus and in the prefrontal cortex but not in other regions of the brain, requiring the von Hippel-Lindau tumor suppressor. Mice exposed to chronic IH demonstrated cognitive deficits related to dysfunction in those brain regions, overview
-
-
?
additional information
?
-
-
two distinct forms, Pol Ialpha and Pol Ibeta. Both forms are catalytically active, but only Pol Ibeta can assemble into productive transcription initiation complexes. Regulation of Pol I transcription during cell cycle progression involving cytokines, and structural organization of mammalian rDNA repeats and the basal factors required for transcription initiation, overview. The activity of basal Pol I factors is regulated by posttranslational modifications
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
etoposide
-
treatment with 0.02 mM etoposide leads to a transient inhibition of rRNA synthesis
additional information
-
gamma irradiation leads to a transient inhibition of rRNA synthesis, but Pol I transcription is not blocked by DNA damage itself, but by the action of DNA repair enzymes
-
additional information
-
oncogenes and tumor suppressors control Pol I transcription, overview. Development of drugs that target the Pol I transcription machinery at different points, overveiw
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CK2
-
is associated with Pol I, the initiation-competent subclass of Pol I, CK2 phosphorylates a number of proteins involved in Pol I transcription and pre-rRNA processing, including UBF, TIF-IA, SL1/TIF-IB, topoisomerase IIa, nucleolin, and nucleophosmin, overview
-
PAF53
-
a 53-kDa protein that is associated with Pol I, recruitment of Pol I to the pre-initiation complex requires the interaction of UBF with SL1/TIF-IB and with PAF53
-
TAFI protein
-
performs important tasks in transcription complex assembly, mediating specific interactions between the rDNA promoter and Pol I, thereby recruiting Pol I, together with a collection of Pol I-associated factors, to rDNA
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TIF-IB/SL 1
-
Pol I promoter specificity is conferred by TIF-IB/SL1, a protein complex containing the TATA binding protein and five TATA binding protein-associated factors, including TAFI110/95, TAFI68, TAFI48, TAFI35, and TAFI12
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upstream binding factor
-
UBF, activates rRNA gene transcription by several means, for example, by recruiting Pol I to the rDNA promoter, by stabilizing binding of TIF-IB/SL1, and by displacing nonspecific DNA binding proteins such as histone H1. And UBF has additional roles in regulation of Pol I promoter escape and transcription elongation
-
additional information
-
intermittent hypoxia, a major pathological factor in the development of neural deficits associated with sleep-disordered breathing, regulates RNA polymerase II in hippocampus and prefrontal cortex. Chronic intermittent hypoxia, but not sustained hypoxia, stimulates hydroxylation of Pro1465 in large subunit of RNA polymerase II and phosphorylation of Ser5 of Rpb1, specifically in the CA1 region of the hippocampus and in the prefrontal cortex but not in other regions of the brain, requiring the von Hippel-Lindau tumor suppressor. Mice exposed to chronic IH demonstrated cognitive deficits related to dysfunction in those brain regions
-
additional information
-
The activity of basal Pol I factors is regulated by posttranslational modifications
-
additional information
-
lipopolysaccharides enhance the binding of the enzyme to the iNOS promoter. GlcN enhances RNAPII O-GlcNAcylation, but inhibits iNOS promoter binding
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
aside from growth-dependent regulation, Pol I transcription also oscillates during cell cycle progression. Transcription is maximal during S- and G2-phase, subsides during mitosis, and then slowly recovers during G1-phase
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
basal transcriptional activity and RNAPII DNA binding might be associated with the O-GlcNAcylation and/or phosphorylation state of RNAPII, which can involve changed association with other transcription factors during inflammation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RPOM_MOUSE
1207
0
136705
Swiss-Prot
Mitochondrion (Reliability: 2)
RPA2_MOUSE
1135
0
128213
Swiss-Prot
other Location (Reliability: 2)
RPB2_MOUSE
1174
0
133911
Swiss-Prot
other Location (Reliability: 1)
RPA1_MOUSE
1717
0
194110
Swiss-Prot
Mitochondrion (Reliability: 4)
RPB1_MOUSE
1970
0
217176
Swiss-Prot
other Location (Reliability: 3)
RPC2_MOUSE
1133
0
127715
Swiss-Prot
other Location (Reliability: 1)
E9PWD9_MOUSE
1133
0
128335
TrEMBL
Mitochondrion (Reliability: 2)
O08847_MOUSE
1966
0
216762
TrEMBL
other Location (Reliability: 3)
A0A0U1RPM9_MOUSE
743
0
85040
TrEMBL
other Location (Reliability: 3)
Q3V3C0_MOUSE
1069
0
120744
TrEMBL
other Location (Reliability: 2)
Q9CSL3_MOUSE
112
0
12531
TrEMBL
Mitochondrion (Reliability: 5)
Q3UHI3_MOUSE
1717
0
194150
TrEMBL
Mitochondrion (Reliability: 4)
F6TLB0_MOUSE
393
0
44849
TrEMBL
other Location (Reliability: 4)
Q7TSI4_MOUSE
649
0
73639
TrEMBL
other Location (Reliability: 2)
Q05BP7_MOUSE
1366
0
154254
TrEMBL
Mitochondrion (Reliability: 4)
Q3U3J3_MOUSE
1207
0
136705
TrEMBL
Mitochondrion (Reliability: 2)
Q80Y46_MOUSE
1366
0
154215
TrEMBL
Mitochondrion (Reliability: 4)
B2WTN8_MOUSE
49
0
5736
TrEMBL
other Location (Reliability: 2)
Q8BNM6_MOUSE
1424
0
160712
TrEMBL
Mitochondrion (Reliability: 4)
Q3UZ02_MOUSE
742
0
84929
TrEMBL
other Location (Reliability: 3)
Q6P9Q2_MOUSE
1135
0
128247
TrEMBL
other Location (Reliability: 2)
A0A0R4J0V5_MOUSE
1932
0
213481
TrEMBL
other Location (Reliability: 3)
Q8C2X2_MOUSE
1012
0
112967
TrEMBL
Secretory Pathway (Reliability: 2)
Q3TUG2_MOUSE
1424
0
160710
TrEMBL
Mitochondrion (Reliability: 4)
E0CY15_MOUSE
903
0
102203
TrEMBL
Mitochondrion (Reliability: 2)
Q3TU49_MOUSE
1361
0
153562
TrEMBL
Mitochondrion (Reliability: 4)
Q9D196_MOUSE
462
0
52581
TrEMBL
Mitochondrion (Reliability: 3)
B2RXC6_MOUSE
1390
0
155738
TrEMBL
other Location (Reliability: 2)
A0A1L1SSC8_MOUSE
179
0
20294
TrEMBL
other Location (Reliability: 4)
A2AP84_MOUSE
754
0
85566
TrEMBL
other Location (Reliability: 2)
A0A0U1RPX8_MOUSE
282
0
31579
TrEMBL
Mitochondrion (Reliability: 4)
Q05DK4_MOUSE
1366
0
154196
TrEMBL
Mitochondrion (Reliability: 4)
Q3TC95_MOUSE
321
0
36069
TrEMBL
other Location (Reliability: 5)
Q8BR29_MOUSE
262
0
29488
TrEMBL
Mitochondrion (Reliability: 4)
Q3TMK3_MOUSE
369
0
41841
TrEMBL
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
subunits with molecular weights of 49 kDa and 42 kDa and a subunit with a molecular weight of 45 kDa (which is probably a component of the basal transcription factor of RNA polymerase III, since it is not identified in the mouse enzyme) are modified in the composition of the enzyme isolated from mouse fibroblasts. The two subunits are simultaneously phosphorylated and glycosylated (glycosylation by O-N-acetylglucosamine residues)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
phosphoprotein
additional information
glycoprotein
-
dynamic O-GlcNAcylation of RNA polymerase II. Lipopolysaccharides reduce the O-linked N-acetylglucosamine modification (O-GlcNAcylation) of RNAPII, but enhance the binding of this enzyme to the iNOS promoter. GlcN enhances RNAPII O-linked GlcNAcylation, but inhibits iNOS promoter binding
glycoprotein
-
the two subunits are simultaneously glycosylated by N-O-acetylglucosamine residues in vivo, glycosylation and phosphorylation of the two subunits is dynamic and differs between the subunits, , also depending on the physiological state of the cell, overview
phosphoprotein
-
RNA Pol II phosphorylation at Ser5 within the C-terminal domain
phosphoprotein
-
the two subunits are simultaneously phosphorylated on serine and threonine residues in vivo, glycosylation and phosphorylation of the three subunits is dynamic and differs between the subunits, also depending on the physiological state of the cell, overview
additional information
-
several posttranslational modifications of the large subunit of RNA polymerase II, Rpb1, including hydroxylation of Pro1465, nondegradative ubiquitylation of RNA Pol II, and phosphorylation of Ser5. Induction of Rpb1 hydroxylation, phosphorylation, and ubiquitylation requires the presence of the von Hippel-Lindau protein, overview
additional information
-
The activity of basal Pol I factors is regulated by posttranslational modifications, overview, e.g. acetylation is a posttranslational modification that regulates the activity of basal Pol I transcription factors, including UBF and SL1/TIF-IB
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
RNA polymerase III subunits isolation from fibroblast nuclei by anion exchange chromatography and ultrafiltration
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
at the end of mitosis, Cdc14B, a phosphatase that is sequestered in an inactive state in the nucleolus during interphase and is released from rDNA during mitosis, dephosphorylates Thr852, thereby activating SL1 and relieving mitotic repression of Pol I transcription
-
mitotic silencing of Pol I transcription is caused by Cdk1/cyclin B-dependent phosphorylation of a single threonine residue Thr852 at TAFI110 that impairs the interaction of SL1/TIF-IB with UBF
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
development of drugs that target the Pol I transcription machinery at different points for use in cancer therapies, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kruhlak, M.; Crouch, E.E.; Orlov, M.; Montano, C.; Gorski, S.A.; Nussenzweig, A.; Misteli, T.; Phair, R.D.; Casellas, R.
The ATM repair pathway inhibits RNA polymerase I transcription in response to chromosome breaks
Nature
447
730-734
2007
Mus musculus
Drygin, D.; Rice, W.G.; Grummt, I.
The RNA polymerase I transcription machinery: an emerging target for the treatment of cancer
Annu. Rev. Pharmacol. Toxicol.
50
131-156
2010
Homo sapiens, Mus musculus
Ignacak, M.L.; Harbaugh, S.V.; Dayyat, E.; Row, B.W.; Gozal, D.; Czyzyk-Krzeska, M.F.
Intermittent hypoxia regulates RNA polymerase II in hippocampus and prefrontal cortex
Neuroscience
158
1436-1445
2009
Mus musculus, Rattus norvegicus
Merkulova, N.; Sedova, V.
Modified in vivo subunits of DNA-dependent RNA polymerase III in mammals
Cell Tissue Biol.
9
284-289
2015
Homo sapiens, Mus musculus
-
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