RNA polymerase II subunit B4

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Polymerase (RNA) II (DNA directed) polypeptide D
PDB rendering based on 2c35.
Available structures: 2c35
Identifiers
Symbol(s) POLR2D; HSRBP4; HSRPB4; RBP4
External IDs OMIM: 606017 MGI: 1916491 HomoloGene: 37968
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 5433 69241
Ensembl ENSG00000144231 ENSMUSG00000024258
Uniprot O15514 Q9D7M8
Refseq NM_004805 (mRNA)
NP_004796 (protein)		 NM_027002 (mRNA)
NP_081278 (protein)
Location Chr 2: 128.32 - 128.33 Mb Chr 18: 31.93 - 31.94 Mb
Pubmed search [1] [2]

DNA-directed RNA polymerase II polypeptide D (or subunit B4), also known as POLR2D, is a human gene.

This gene encodes the fourth largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. In yeast, this polymerase subunit is associated with the polymerase under suboptimal growth conditions and may have a stress protective role. A sequence for a ribosomal pseudogene is contained within the 3' untranslated region of the transcript from this gene.[1]

[edit] References

  1. ^ Entrez Gene: POLR2D polymerase (RNA) II (DNA directed) polypeptide D.

[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. 
  • 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. 
  • Cujec TP, Cho H, Maldonado E, et al. (1997). "The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme.". Mol. Cell. Biol. 17 (4): 1817–23. PMID 9121429. 
  • García-Martínez LF, Mavankal G, Neveu JM, et al. (1997). "Purification of a Tat-associated kinase reveals a TFIIH complex that modulates HIV-1 transcription.". EMBO J. 16 (10): 2836–50. doi:10.1093/emboj/16.10.2836. PMID 9184228. 
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