POLR2I

From Wikipedia, the free encyclopedia

Polymerase (RNA) II (DNA directed) polypeptide I, 14.5kDa

Identifiers

POLR2I; RPB9; hRPB14.5

External IDs

OMIM: 180662 MGI: 1917170 HomoloGene: 4541

Gene ontology
Molecular Function:	• DNA binding • RNA polymerase II transcription factor activity • DNA-directed RNA polymerase activity • zinc ion binding • transferase activity • metal ion binding
Cellular Component:	• nucleus • DNA-directed RNA polymerase II, core complex
Biological Process:	• RNA elongation • regulation of transcription, DNA-dependent • transcription from RNA polymerase II promoter

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006233 (mRNA)
NP_006224 (protein)

XM_001000377 (mRNA)
XP_001000377 (protein)

Location

Chr 19: 41.3 - 41.3 Mb

Chr 7: 29.94 - 29.94 Mb

Pubmed search

[1]

[2]

Polymerase (RNA) II (DNA directed) polypeptide I, 14.5kDa, also known as POLR2I, is a human gene.

This gene encodes a subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. This subunit, in combination with two other polymerase subunits, forms the DNA binding domain of the polymerase, a groove in which the DNA template is transcribed into RNA. The product of this gene has two zinc finger motifs with conserved cysteines and the subunit does possess zinc binding activity.^[1]

[edit] References

^ Entrez Gene: POLR2I polymerase (RNA) II (DNA directed) polypeptide I, 14.5kDa.

[edit] Further reading

Jeang KT (1998). "Tat, Tat-associated kinase, and transcription.". J. Biomed. Sci. 5 (1): 24–7. PMID 9570510.
Yankulov K, Bentley D (1998). "Transcriptional control: Tat cofactors and transcriptional elongation.". Curr. Biol. 8 (13): R447–9. PMID 9651670.
Romano G, Kasten M, De Falco G, et al. (2000). "Regulatory functions of Cdk9 and of cyclin T1 in HIV tat transactivation pathway gene expression.". J. Cell. Biochem. 75 (3): 357–68. PMID 10536359.
Marcello A, Zoppé M, Giacca M (2002). "Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator.". IUBMB Life 51 (3): 175–81. PMID 11547919.
Stevens M, De Clercq E, Balzarini J (2007). "The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention.". Med Res Rev 26 (5): 595–625. doi:10.1002/med.20081. PMID 16838299.
Harrich D, McMillan N, Munoz L, et al. (2007). "Will diverse Tat interactions lead to novel antiretroviral drug targets?". Current drug targets 7 (12): 1595–606. PMID 17168834.
Kato H, Sumimoto H, Pognonec P, et al. (1992). "HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors.". Genes Dev. 6 (4): 655–66. PMID 1559613.
Southgate C, Zapp ML, Green MR (1990). "Activation of transcription by HIV-1 Tat protein tethered to nascent RNA through another protein.". Nature 345 (6276): 640–2. doi:10.1038/345640a0. PMID 2190099.
Wu-Baer F, Sigman D, Gaynor RB (1995). "Specific binding of RNA polymerase II to the human immunodeficiency virus trans-activating region RNA is regulated by cellular cofactors and Tat.". Proc. Natl. Acad. Sci. U.S.A. 92 (16): 7153–7. PMID 7638159.
Herrmann CH, Rice AP (1995). "Lentivirus Tat proteins specifically associate with a cellular protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal domain of the large subunit of RNA polymerase II: candidate for a Tat cofactor.". J. Virol. 69 (3): 1612–20. PMID 7853496.
Acker J, Mattei MG, Wintzerith M, et al. (1994). "Chromosomal localization of human RNA polymerase II subunit genes.". Genomics 20 (3): 496–9. doi:10.1006/geno.1994.1208. PMID 8034326.
Acker J, Wintzerith M, Vigneron M, Kedinger C (1994). "Structure of the gene encoding the 14.5 kDa subunit of human RNA polymerase II.". Nucleic Acids Res. 21 (23): 5345–50. PMID 8265347.
Keen NJ, Gait MJ, Karn J (1996). "Human immunodeficiency virus type-1 Tat is an integral component of the activated transcription-elongation complex.". Proc. Natl. Acad. Sci. U.S.A. 93 (6): 2505–10. PMID 8637904.
Yang X, Herrmann CH, Rice AP (1996). "The human immunodeficiency virus Tat proteins specifically associate with TAK in vivo and require the carboxyl-terminal domain of RNA polymerase II for function.". J. Virol. 70 (7): 4576–84. PMID 8676484.
Agostini I, Navarro JM, Rey F, et al. (1996). "The human immunodeficiency virus type 1 Vpr transactivator: cooperation with promoter-bound activator domains and binding to TFIIB.". J. Mol. Biol. 261 (5): 599–606. doi:10.1006/jmbi.1996.0485. PMID 8800208.
Zhou Q, Sharp PA (1996). "Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat.". Science 274 (5287): 605–10. PMID 8849451.
Okamoto H, Sheline CT, Corden JL, et al. (1996). "Trans-activation by human immunodeficiency virus Tat protein requires the C-terminal domain of RNA polymerase II.". Proc. Natl. Acad. Sci. U.S.A. 93 (21): 11575–9. PMID 8876177.
Chun RF, Jeang KT (1996). "Requirements for RNA polymerase II carboxyl-terminal domain for activated transcription of human retroviruses human T-cell lymphotropic virus I and HIV-1.". J. Biol. Chem. 271 (44): 27888–94. PMID 8910388.
Parada CA, Roeder RG (1996). "Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain.". Nature 384 (6607): 375–8. doi:10.1038/384375a0. PMID 8934526.
García-Martínez LF, Ivanov D, Gaynor RB (1997). "Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes.". J. Biol. Chem. 272 (11): 6951–8. PMID 9054383.