POLR2L

Polymerase (RNA) II (DNA directed) polypeptide L, 7.6kDa, also known as POLR2L, is a human gene.

PBB_Summary
section_title =
summary_text = This gene encodes a subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. The product of this gene contains four conserved cysteines characteristic of an atypical zinc-binding domain. Like its counterpart in yeast, this subunit may be shared by the other two DNA-directed RNA polymerases. [cite web | title = Entrez Gene: POLR2L polymerase (RNA) II (DNA directed) polypeptide L, 7.6kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5441| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Jeang KT |title=Tat, Tat-associated kinase, and transcription. |journal=J. Biomed. Sci. |volume=5 |issue= 1 |pages= 24–7 |year= 1998 |pmid= 9570510 |doi=
*cite journal | author=Yankulov K, Bentley D |title=Transcriptional control: Tat cofactors and transcriptional elongation. |journal=Curr. Biol. |volume=8 |issue= 13 |pages= R447–9 |year= 1998 |pmid= 9651670 |doi=
*cite journal | author=Romano G, Kasten M, De Falco G, "et al." |title=Regulatory functions of Cdk9 and of cyclin T1 in HIV tat transactivation pathway gene expression. |journal=J. Cell. Biochem. |volume=75 |issue= 3 |pages= 357–68 |year= 2000 |pmid= 10536359 |doi=
*cite journal | author=Marcello A, Zoppé M, Giacca M |title=Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator. |journal=IUBMB Life |volume=51 |issue= 3 |pages= 175–81 |year= 2002 |pmid= 11547919 |doi=
*cite journal | author=Stevens M, De Clercq E, Balzarini J |title=The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention. |journal=Med Res Rev |volume=26 |issue= 5 |pages= 595–625 |year= 2007 |pmid= 16838299 |doi= 10.1002/med.20081
*cite journal | author=Harrich D, McMillan N, Munoz L, "et al." |title=Will diverse Tat interactions lead to novel antiretroviral drug targets? |journal=Current drug targets |volume=7 |issue= 12 |pages= 1595–606 |year= 2007 |pmid= 17168834 |doi=
*cite journal | author=Jang KL, Collins MK, Latchman DS |title=The human immunodeficiency virus tat protein increases the transcription of human Alu repeated sequences by increasing the activity of the cellular transcription factor TFIIIC. |journal=J. Acquir. Immune Defic. Syndr. |volume=5 |issue= 11 |pages= 1142–7 |year= 1992 |pmid= 1403646 |doi=
*cite journal | author=Kato H, Sumimoto H, Pognonec P, "et al." |title=HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors. |journal=Genes Dev. |volume=6 |issue= 4 |pages= 655–66 |year= 1992 |pmid= 1559613 |doi=
*cite journal | author=Southgate C, Zapp ML, Green MR |title=Activation of transcription by HIV-1 Tat protein tethered to nascent RNA through another protein. |journal=Nature |volume=345 |issue= 6276 |pages= 640–2 |year= 1990 |pmid= 2190099 |doi= 10.1038/345640a0
*cite journal | author=Wu-Baer F, Sigman D, Gaynor RB |title=Specific binding of RNA polymerase II to the human immunodeficiency virus trans-activating region RNA is regulated by cellular cofactors and Tat. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 16 |pages= 7153–7 |year= 1995 |pmid= 7638159 |doi=
*cite journal | author=Shpakovski GV, Acker J, Wintzerith M, "et al." |title=Four subunits that are shared by the three classes of RNA polymerase are functionally interchangeable between Homo sapiens and Saccharomyces cerevisiae. |journal=Mol. Cell. Biol. |volume=15 |issue= 9 |pages= 4702–10 |year= 1995 |pmid= 7651387 |doi=
*cite journal | author=Herrmann CH, Rice AP |title=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. |journal=J. Virol. |volume=69 |issue= 3 |pages= 1612–20 |year= 1995 |pmid= 7853496 |doi=
*cite journal | author=McKune K, Moore PA, Hull MW, Woychik NA |title=Six human RNA polymerase subunits functionally substitute for their yeast counterparts. |journal=Mol. Cell. Biol. |volume=15 |issue= 12 |pages= 6895–900 |year= 1996 |pmid= 8524256 |doi=
*cite journal | author=Keen NJ, Gait MJ, Karn J |title=Human immunodeficiency virus type-1 Tat is an integral component of the activated transcription-elongation complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 6 |pages= 2505–10 |year= 1996 |pmid= 8637904 |doi=
*cite journal | author=Yang X, Herrmann CH, Rice AP |title=The human immunodeficiency virus Tat proteins specifically associate with TAK in vivo and require the carboxyl-terminal domain of RNA polymerase II for function. |journal=J. Virol. |volume=70 |issue= 7 |pages= 4576–84 |year= 1996 |pmid= 8676484 |doi=
*cite journal | author=Acker J, Murroni O, Mattei MG, "et al." |title=The gene (POLR2L) encoding the hRPB7.6 subunit of human RNA polymerase. |journal=Genomics |volume=32 |issue= 1 |pages= 86–90 |year= 1996 |pmid= 8786124 |doi= 10.1006/geno.1996.0079
*cite journal | author=Agostini I, Navarro JM, Rey F, "et al." |title=The human immunodeficiency virus type 1 Vpr transactivator: cooperation with promoter-bound activator domains and binding to TFIIB. |journal=J. Mol. Biol. |volume=261 |issue= 5 |pages= 599–606 |year= 1996 |pmid= 8800208 |doi= 10.1006/jmbi.1996.0485
*cite journal | author=Zhou Q, Sharp PA |title=Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. |journal=Science |volume=274 |issue= 5287 |pages= 605–10 |year= 1996 |pmid= 8849451 |doi=
*cite journal | author=Okamoto H, Sheline CT, Corden JL, "et al." |title=Trans-activation by human immunodeficiency virus Tat protein requires the C-terminal domain of RNA polymerase II. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 21 |pages= 11575–9 |year= 1996 |pmid= 8876177 |doi=
*cite journal | author=Chun RF, Jeang KT |title=Requirements for RNA polymerase II carboxyl-terminal domain for activated transcription of human retroviruses human T-cell lymphotropic virus I and HIV-1. |journal=J. Biol. Chem. |volume=271 |issue= 44 |pages= 27888–94 |year= 1996 |pmid= 8910388 |doi=

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