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Information on EC 2.7.7.6 - DNA-directed RNA polymerase and Organism(s) Homo sapiens

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EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.6 DNA-directed RNA polymerase
IUBMB 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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Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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
h-mtRNAP
-
-
mitochondrial RNA polymerase
-
-
mitoRNAP
-
-
nucleotidyltransferase, ribonucleate
-
-
-
-
Pol II
Pol IIIalpha
-
-
Pol IIIbeta
-
-
PolIII
-
-
POLRMT
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 pol III
-
-
RNA polymerase
RNA polymerase I
RNA polymerase II
RNA polymerase III
RNA transcriptase
-
-
-
-
RNAP I
-
-
-
-
RNAP II
RNAP III
T7 RNAP
-
-
T7-like RNA polymerase
-
-
transcriptase
-
-
-
-
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
9014-24-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-C-methyl-ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
misincorporation frequency of approximately 1 in 7800 2'-C-methyl-ATP
-
-
?
2'-deoxy-ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
misincorporation
-
-
?
3'-deoxy-ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
misincorporation frequency of approximately 1 in 5 3'-dATP
-
-
?
ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
GTP + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + RNAn
diphosphate + RNAn+1
show the reaction diagram
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
-
RNA polymerase is a member of the iron-sulfur cluster protein family
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(3-C-ethynyl-beta-D-ribo-pentofuranosyl)cytosine
-
i.e. ECyd, TAS-106, a antitumor ribonucleoside that inhibits RNA polymerase, acts synergistically in inhibiting A-549 cancer cell growth and in tumor growth in vivo. The compound also inhibits the checkpoint-associated protein, the expression of Chk1 protein and the phosphorylation of Chk1 and Chk2, antitumour effects in combination with cisplatin, overview
2'-C-ethynyl-7-deaza-ATP
causes immediate chain termination
-
2'-C-Me-ATP
causes immediate chain termination
-
3'-dATP
causes immediate chain termination
3'-ethynylcytidine-5'-triphosphate
-
i.e. ECTP, competitive inhibition in the presence of isolated nuclei from FM3A mouse tumor cells
ara-ATP
causes partial chain termination
B2 RNA
-
the about 180-nt B2 RNA potently represses mRNA transcription by binding tightly to RNA polymerase II and assembling with it into complexes on promoter DNA, where it keeps the polymerase from properly engaging the promoter DNA. The C-terminal domain of the largest Pol II subunit is not involved. B2 RNA binds Pol II and assembles into complexes at promoters. Binding site anaylsis usig Pol II peptides, binding structure, and mechanism of transcriptional repression by B2 RNA, detailed overview
-
breast cancer susceptibility gene 1
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BRCA1, inhibits RNA pol III via inhibition of the essential transcription factor TFIIIB, mechanism, overview. BRCA1 is a tumor suppressor playing a role in DNA repair, cell cycle regulation, apoptosis, genome integrity, and ubiquitination, and it BRCA1 has a conserved N-terminal RING domain, an activation domain 1, AD1, and an acidic C-terminal domain, BRCA1 C-terminal region. Interaction with TFIIIB occurs via the BRCA1 C-terminal region domain of Fcp1p, an RNA polymerase II phosphatase. RNA pol III inhibition involves the TFIIB family members Brf1 and Brf2, overview
-
ML-60218
-
treatment of A-549 cells with the Pol III inhibitor ML-60218 decreased the cytosolic RNA:DNA hybrid staining
protein TLS
-
translocated in liposarcoma, a protein originally identified as the product of a chromosomal translocation, which associates with both RNAP II and the spliceosome, also represses transcription by RNAP III. It represses transcription from all three classes of RNAP III promoters in vitro and to associates with RNAP III genes in vivo. Depletion of TLS by siRNA in HeLa cells resulted in increased steady-state levels of RNAP III transcripts as well as increased RNAP III and TBP occupancy at RNAP III-transcribed genes
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Tagetitoxin
-
inhibition of RNA polymerase III
TFAM
-
DNA packaging by TFAM makes the DNA more resistant to unwinding
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
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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
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RNase P
-
required for Pol I and Pol III required
-
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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TFB2
-
the essential initiation factor forms a network of interactions with DNA near the transcription start site and facilitates promoter melting but may not be essential for promoter recognition, TFB2 bridges upstream and downstream promoter contacts of the initiation complex, mapping of TFB2-DNA interactions at the transcription start site, overview
-
TFB2M
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the requirement for TFB2M in transcription of dsDNA is that it can stabilize an incompletely single-stranded template established by negative supercoiling
-
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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transcription factor TFIIIB
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proper initiation by RNA pol III requires the transcription factor TFIIIB. Gene-external U6 snRNA transcription requires TFIIIB consisting of Bdp1, TBP, and Brf2. Transcription from the gene internal tRNA promoter requires TFIIIB composed of Bdp1, TBP, and Brf1. Breast cancer susceptibility gene 1, BRCA1, inhibits TFIIB, which interacts with the BRCA1 C-terminal region domain of Fcp1p, an RNA polymerase II phosphatase, TFIIIB regulation network, overview
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upstream binding factor
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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
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.9
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
35
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
in embryonic stem cells, silent developmental regulator genes that are repressed by Polycomb are associated with a form of RNAPII that can elongate through coding regions but that lacks the post-translational modifications that are important for cou­pling RNA synthesis to co-transcriptional maturation
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
mature
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the enzyme is encoded in the nucleus
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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human mitochondrial RNA polymerase is distantly related to the bacteriophage T7 class of single-subunit RNAPs with a probably similar mechanisms for nucleotide binding, substrate selection and catalysis/nucleotidyl transfer. The C-terminal domain contains the regions of highest similarity to the phage RNAPs. Early in the evolution of eukaryotes there has been a switch from a multi-subunit prokaryotic polymerase to a single-subunit, phage-derived polymerase, encoded in the nuclear genome and imported into the mitochondria, to serve as the transcriptase of the mitochondrial genome. The POLRMT CTD is characteristic of the Pol I family of nucleic acid polymerases, typically described as resembling the shape of a cupped right hand, containing the fingers, palm and thumb subdomains. The palm subdomain contains several key structural motifs that are highly conserved among the different classes of nucleic acid polymerases
malfunction
physiological function
additional information
-
POLRMT distinct mechanisms for promoter recognition and transcription initiation, kinetic mechanism for POLRMT-catalyzed nucleotide incorporation, and structure-function relationship, nucleotidyl transfer and the nucleotide-addition cycle, detailed overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RPB1_HUMAN
1970
0
217176
Swiss-Prot
other Location (Reliability: 3)
RPOM_HUMAN
1230
0
138620
Swiss-Prot
Mitochondrion (Reliability: 3)
RPC1_HUMAN
1390
0
155641
Swiss-Prot
other Location (Reliability: 2)
RPA2_HUMAN
1135
0
128229
Swiss-Prot
other Location (Reliability: 4)
RPA1_HUMAN
1720
0
194811
Swiss-Prot
Mitochondrion (Reliability: 4)
RPB2_HUMAN
1174
0
133897
Swiss-Prot
other Location (Reliability: 1)
RPC2_HUMAN
1133
0
127785
Swiss-Prot
other Location (Reliability: 1)
Q9NVC2_HUMAN
336
0
38531
TrEMBL
other Location (Reliability: 4)
B7Z284_HUMAN
1207
0
137031
TrEMBL
other Location (Reliability: 2)
Q4QRK8_HUMAN
594
0
66804
TrEMBL
other Location (Reliability: 3)
Q7Z755_HUMAN
162
0
18272
TrEMBL
other Location (Reliability: 2)
F8VRU2_HUMAN
169
0
19479
TrEMBL
other Location (Reliability: 1)
B2WTN6_HUMAN
49
0
5736
TrEMBL
other Location (Reliability: 2)
R4GMX2_HUMAN
199
0
22660
TrEMBL
other Location (Reliability: 3)
Q59E91_HUMAN
1072
0
121236
TrEMBL
other Location (Reliability: 2)
Q7Z3R8_HUMAN
1133
0
127819
TrEMBL
other Location (Reliability: 1)
Q4G0F4_HUMAN
1230
0
138515
TrEMBL
Mitochondrion (Reliability: 3)
B4DH29_HUMAN
1099
0
125219
TrEMBL
other Location (Reliability: 2)
Q15161_HUMAN
113
0
12747
TrEMBL
other Location (Reliability: 1)
K7ESD1_HUMAN
127
0
14861
TrEMBL
Mitochondrion (Reliability: 5)
B3KRQ8_HUMAN
838
0
94370
TrEMBL
other Location (Reliability: 2)
B7Z1W6_HUMAN
996
0
112852
TrEMBL
other Location (Reliability: 2)
B4DR40_HUMAN
1083
0
123365
TrEMBL
Mitochondrion (Reliability: 4)
B4DZE5_HUMAN
927
0
104648
TrEMBL
Mitochondrion (Reliability: 3)
A0A076N230_HUMAN
343
0
38224
TrEMBL
other Location (Reliability: 2)
Q9BSR4_HUMAN
582
0
65486
TrEMBL
other Location (Reliability: 2)
Q96NM2_HUMAN
260
0
29459
TrEMBL
Mitochondrion (Reliability: 3)
Q8TCW2_HUMAN
299
0
33609
TrEMBL
other Location (Reliability: 1)
Q53T12_HUMAN
922
0
105371
TrEMBL
other Location (Reliability: 1)
Q8TCW4_HUMAN
387
0
43119
TrEMBL
other Location (Reliability: 2)
Q9H6S8_HUMAN
459
0
51619
TrEMBL
other Location (Reliability: 2)
B9ZVN9_HUMAN
1659
0
187808
TrEMBL
Mitochondrion (Reliability: 4)
A0A6Q8PGB0_HUMAN
1970
0
217246
TrEMBL
other Location (Reliability: 3)
C9JZW8_HUMAN
76
0
8846
TrEMBL
other Location (Reliability: 1)
C9J4M6_HUMAN
1067
0
121373
TrEMBL
other Location (Reliability: 2)
B7ZKR9_HUMAN
1720
0
194786
TrEMBL
Mitochondrion (Reliability: 4)
B3KQY9_HUMAN
523
0
58820
TrEMBL
other Location (Reliability: 1)
Q8TCW3_HUMAN
435
0
48108
TrEMBL
other Location (Reliability: 2)
Q9H6T2_HUMAN
495
0
56749
TrEMBL
other Location (Reliability: 5)
C9JS83_HUMAN
128
0
14123
TrEMBL
other Location (Reliability: 4)
B7Z6H4_HUMAN
1369
0
153510
TrEMBL
other Location (Reliability: 2)
C9J2Y9_HUMAN
1167
0
133057
TrEMBL
other Location (Reliability: 1)
Q6DKI9_HUMAN
560
0
63176
TrEMBL
other Location (Reliability: 4)
H7C0D9_HUMAN
307
0
34287
TrEMBL
other Location (Reliability: 3)
B4DHJ3_HUMAN
1167
0
133027
TrEMBL
other Location (Reliability: 1)
B7Z8X7_HUMAN
1086
0
123478
TrEMBL
other Location (Reliability: 5)
C9JJG2_HUMAN
114
0
12695
TrEMBL
other Location (Reliability: 4)
B4DET1_HUMAN
855
0
91810
TrEMBL
other Location (Reliability: 3)
Q96AG9_HUMAN
574
0
65744
TrEMBL
other Location (Reliability: 1)
RPAB3_HUMAN
150
0
17143
Swiss-Prot
-
RPAB2_HUMAN
127
0
14478
Swiss-Prot
Secretory Pathway (Reliability: 1)
RPB4_HUMAN
142
0
16311
Swiss-Prot
-
RPC6_HUMAN
316
0
35684
Swiss-Prot
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
-
subunits with molecular weights of 60 kDa and 45 kDa and a subunit with a molecular weight of 52 kDa (which is probably one of the basal transcription factors of RNA polymerase III) are modified in the composition of the enzyme isolated from human cells. The three subunits are simultaneously phosphorylated and glycosylated
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
the three subunits are simultaneously glycosylated in vivo by O-N-acetylglucosamine residues, glycosylation and phosphorylation of the three subunits is dynamic and differs between the subunits, , also depending on the physiological state of the cell, overview
phosphoprotein
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure anaysis
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G711K/N926S/N1103S/N1117S
-
site-directed mutagenesis, the mutant mitoRNAP that lacks four natural hydroxylamine cleavage sites
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
RNA polymerase III subunits isolation from A-431 cells and placenta cell nuclei by anion exchange chromatography and ultrafiltration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293T cells, HAT-1080 cells, and Magi cells
-
expression in Escherichia coli
expression of the N-terminally His6-tagged intein fusion mitoRNAP protein
-
stable ectopic expression of subunit RPC32alpha in IMR90 fibroblasts
-
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 hide
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
Jacob, S.T.
Mammalian RNA polymerases
Prog. Nucleic Acid Res. Mol. Biol.
13
93-126
1973
Bos taurus, Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Steinberg, T.H.; Mathews, D.E.; Durbin, R.D.; Burgess, R.R.
Tagetitoxin: a new inhibitor of eukaryotic transcription by RNA polymerase III
J. Biol. Chem.
265
499-505
1990
Bombyx mori, Bos taurus, Saccharomyces cerevisiae, Homo sapiens, Xenopus laevis
Manually annotated by BRENDA team
Greco-Stewart, V.S.; Miron, P.; Abrahem, A.; Pelchat, M.
The human RNA polymerase II interacts with the terminal stem-loop regions of the hepatitis delta virus RNA genome
Virology
357
68-78
2007
Homo sapiens
Manually annotated by BRENDA team
Lo, H.; Chang, T.; Yam, P.; Marcovecchio, P.M.; Li, S.; Zaia, J.A.; Yee, J.
Inhibition of HIV-1 replication with designed miRNAs expressed from RNA polymerase II promoters
Gene Ther.
14
1503-1512
2007
Homo sapiens
Manually annotated by BRENDA team
Reiner, R.; Krasnov-Yoeli, N.; Dehtiar, Y.; Jarrous, N.
Function and assembly of a chromatin-associated RNase P that is required for efficient transcription by RNA polymerase I
PLoS ONE
3
e4072
2008
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Sologub, M.; Litonin, D.; Anikin, M.; Mustaev, A.; Temiakov, D.
TFB2 is a transient component of the catalytic site of the human mitochondrial RNA polymerase
Cell
139
934-944
2009
Homo sapiens
Manually annotated by BRENDA team
Hirata, A.; Murakami, K.S.
Archaeal RNA polymerase
Curr. Opin. Struct. Biol.
19
724-731
2009
Archaeoglobus fulgidus, Saccharomyces cerevisiae, Homo sapiens, Methanocaldococcus jannaschii, Pyrococcus furiosus, Thermococcus kodakarensis, Schizosaccharomyces pombe, Saccharolobus shibatae, Saccharolobus solfataricus
Manually annotated by BRENDA team
Brookes, E.; Pombo, A.
Modifications of RNA polymerase II are pivotal in regulating gene expression states
EMBO Rep.
10
1213-1219
2009
Homo sapiens
Manually annotated by BRENDA team
Fukuoh, A.; Ohgaki, K.; Hatae, H.; Kuraoka, I.; Aoki, Y.; Uchiumi, T.; Jacobs, H.T.; Kang, D.
DNA conformation-dependent activities of human mitochondrial RNA polymerase
Genes Cells
14
1029-1042
2009
Homo sapiens
Manually annotated by BRENDA team
Kazuno, H.; Fujioka, A.; Fukushima, M.; Wataya, Y.; Matsuda, A.; Sasaki, T.
1-(3-C-Ethynyl-beta-D-ribo-pentofuranosyl)cytosine (ECyd, TAS-106), a novel potent inhibitor of RNA polymerase, potentiates the cytotoxicity of CDDP in human cancer cells both in vitro and in vivo
Int. J. Oncol.
34
1373-1380
2009
Homo sapiens
Manually annotated by BRENDA team
Boeing, S.; Rigault, C.; Heidemann, M.; Eick, D.; Meisterernst, M.
RNA polymerase II C-terminal heptarepeat domain Ser-7 phosphorylation is established in a mediator-dependent fashion
J. Biol. Chem.
285
188-196
2010
Homo sapiens
Manually annotated by BRENDA team
Veras, I.; Rosen, E.M.; Schramm, L.
Inhibition of RNA polymerase III transcription by BRCA1
J. Mol. Biol.
387
523-531
2009
Homo sapiens
Manually annotated by BRENDA team
Tan, A.Y.; Manley, J.L.
TLS inhibits RNA polymerase III transcription
Mol. Cell. Biol.
30
186-196
2010
Homo sapiens
Manually annotated by BRENDA team
Baranello, L.; Bertozzi, D.; Fogli, M.V.; Pommier, Y.; Capranico, G.
DNA topoisomerase I inhibition by camptothecin induces escape of RNA polymerase II from promoter-proximal pause site, antisense transcription and histone acetylation at the human HIF-1alpha gene locus
Nucleic Acids Res.
38
159-171
2010
Homo sapiens
Manually annotated by BRENDA team
Arnold, J.J.; Smidansky, E.D.; Moustafa, I.M.; Cameron, C.E.
Human mitochondrial RNA polymerase: structure-function, mechanism and inhibition
Biochim. Biophys. Acta
1819
948-960
2012
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Ponicsan, S.L.; Houel, S.; Old, W.M.; Ahn, N.G.; Goodrich, J.A.; Kugel, J.F.
The non-coding B2 RNA binds to the DNA cleft and active-site region of RNA polymerase II
J. Mol. Biol.
425
3625-3638
2013
Homo sapiens
Manually annotated by BRENDA team
Fuste, J.M.; Wanrooij, S.; Jemt, E.; Granycome, C.E.; Cluett, T.J.; Shi, Y.; Atanassova, N.; Holt, I.J.; Gustafsson, C.M.; Falkenberg, M.
Mitochondrial RNA polymerase is needed for activation of the origin of light-strand DNA replication
Mol. Cell
37
67-78
2010
Homo sapiens
Manually annotated by BRENDA team
Haurie, V.; Durrieu-Gaillard, S.; Dumay-Odelot, H.; Da Silva, D.; Rey, C.; Prochazkova, M.; Roeder, R.G.; Besser, D.; Teichmann, M.
Two isoforms of human RNA polymerase III with specific functions in cell growth and transformation
Proc. Natl. Acad. Sci. USA
107
4176-4181
2010
Homo sapiens
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
Koo, C.X.; Kobiyama, K.; Shen, Y.J.; LeBert, N.; Ahmad, S.; Khatoo, M.; Aoshi, T.; Gasser, S.; Ishii, K.J.
RNA polymerase III regulates cytosolic RNA:DNA hybrids and intracellular microRNA expression
J. Biol. Chem.
290
7463-7473
2015
Homo sapiens
Manually annotated by BRENDA team
Lu, G.; Bluemling, G.R.; Mao, S.; Hager, M.; Gurale, B.P.; Collop, P.; Kuiper, D.; Sana, K.; Painter, G.R.; De La Rosa, A.; Kolykhalov, A.A.
Simple in vitro assay to evaluate the incorporation efficiency of ribonucleotide analog 5-triphosphates into RNA by human mitochondrial DNA-dependent RNA polymerase
Antimicrob. Agents Chemother.
62
e01830-17
2018
Homo sapiens (O00411), Homo sapiens
Manually annotated by BRENDA team