POLR2K
DNA-directed RNA polymerases I, II, and III subunit RPABC4 is a protein that in humans is encoded by the POLR2K gene.
This gene encodes one of the smallest subunits of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. This subunit is shared by the other two DNA-directed RNA polymerases.[1]
Interactions
POLR2K has been shown to interact with POLR2C.[2]
References
- ↑ “Entrez Gene: POLR2K polymerase (RNA) II (DNA directed) polypeptide K, 7.0kDa”.
- ↑ Acker, J; de Graaff M; Cheynel I; Khazak V; Kedinger C; Vigneron M (July 1997). “Interactions between the human RNA polymerase II subunits”. J. Biol. Chem. UNITED STATES. 272 (27): 16815–21. doi:10.1074/jbc.272.27.16815. ISSN 0021-9258. PMID 9201987.
Further reading
- Jeang KT (1998). “Tat, Tat-associated kinase, and transcription”. J. Biomed. Sci. 5 (1): 24–7. doi:10.1007/BF02253352. PMID 9570510.
- Yankulov K, Bentley D (1998). “Transcriptional control: Tat cofactors and transcriptional elongation”. Curr. Biol. 8 (13): R447–9. doi:10.1016/S0960-9822(98)70289-1. 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. doi:10.1002/(SICI)1097-4644(19991201)75:3<357::AID-JCB1>3.0.CO;2-K. 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. doi:10.1080/152165401753544241. PMID 11547919.
- Howe KJ (2002). “RNA polymerase II conducts a symphony of pre-mRNA processing activities”. Biochim. Biophys. Acta. 1577 (2): 308–24. doi:10.1016/s0167-4781(02)00460-8. PMID 12213660.
- 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. doi:10.2174/138945006779025338. PMID 17168834.
- Jang KL, Collins MK, Latchman DS (1992). “The human immunodeficiency virus tat protein increases the transcription of human Alu repeated sequences by increasing the activity of the cellular transcription factor TFIIIC”. J. Acquir. Immune Defic. Syndr. 5 (11): 1142–7. PMID 1403646.
- 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. doi:10.1101/gad.6.4.655. 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. Bibcode:1990Natur.345..640S. 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. Bibcode:1995PNAS…92.7153W. doi:10.1073/pnas.92.16.7153. PMC 41297. PMID 7638159.
- Shpakovski GV, Acker J, Wintzerith M, et al. (1995). “Four subunits that are shared by the three classes of RNA polymerase are functionally interchangeable between Homo sapiens and Saccharomyces cerevisiae”. Mol. Cell. Biol. 15 (9): 4702–10. PMC 230713. PMID 7651387.
- 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. PMC 188757. PMID 7853496.
- 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. Bibcode:1996PNAS…93.2505K. doi:10.1073/pnas.93.6.2505. PMC 39827. 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. PMC 190394. 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. Bibcode:1996Sci…274..605Z. doi:10.1126/science.274.5287.605. 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. Bibcode:1996PNAS…9311575O. doi:10.1073/pnas.93.21.11575. PMC 38099. 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. doi:10.1074/jbc.271.44.27888. 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. Bibcode:1996Natur.384..375P. doi:10.1038/384375a0. PMID 8934526.
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