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Polr2a

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Title: Polr2a  
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Subject: Housekeeping gene, RNA polymerase II, TATA-binding protein, PCAF, CREB-binding protein, Transcription factor II B, SMARCA4, POLR2C, POLR2E, POLR2H
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Polr2a

Polymerase (RNA) II (DNA directed) polypeptide A, 220kDa

Rendering based on PDB .
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols  ; POLR2; POLRA; RPB1; RPBh1; RPO2; RPOL2; RpIILS; hRPB220; hsRPB1
External IDs ChEMBL: GeneCards:
EC number
RNA expression pattern
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

DNA-directed RNA polymerase II subunit RPB1 is an enzyme that in humans is encoded by the POLR2A gene. This gene encodes the largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. The product of this gene contains a carboxy terminal domain composed of heptapeptide repeats that are essential for polymerase activity. These repeats contain serine and threonine residues that are phosphorylated in actively transcribing RNA polymerase. In addition, this subunit, in combination with several other polymerase subunits, forms the DNA-binding domain of the polymerase, a groove in which the DNA template is transcribed into RNA.[1]

Interactions

POLR2A has been shown to interact with Transcription elongation regulator 1,[2] CREB-binding protein,[3] BRCA1,[4][5][6][7] GTF2H4,[5] TATA-binding protein,[5] PCAF,[3] GTF2F1,[3][5] SUPT5H,[8][9] Transcription Factor II B,[5] POLR2H,[10] POLR2L,[10] MED26,[11] Cyclin-dependent kinase 8,[3] ZNF74,[12] TCEA1,[13][14][15] SMYD3,[16] CTDP1,[5] POLR2C,[10] PQBP1,[17] SMARCA2,[3][18][19] SND1,[20] MED21,[3][5][21] SMARCB1,[3][18][19] POLR2E,[10] SMARCA4[18][19][22] and TAF11.[5]

References

  1. ^ "Entrez Gene: POLR2A polymerase (RNA) II (DNA directed) polypeptide A, 220kDa". 
  2. ^ Carty, S M; Goldstrohm A C; Suñé C; Garcia-Blanco M A; Greenleaf A L (August 2000). "Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 97 (16): 9015–20. ISSN 0027-8424. PMC 16813. PMID 10908677. doi:10.1073/pnas.160266597. 
  3. ^ a b c d e f g Cho, H; Orphanides G; Sun X; Yang X J; Ogryzko V; Lees E; Nakatani Y; Reinberg D (September 1998). "A Human RNA Polymerase II Complex Containing Factors That Modify Chromatin Structure". Mol. Cell. Biol. (UNITED STATES) 18 (9): 5355–63. ISSN 0270-7306. PMC 109120. PMID 9710619. 
  4. ^ Krum, Susan A; Miranda Gustavo A; Lin Chenwei; Lane Timothy F (December 2003). "BRCA1 associates with processive RNA polymerase II". J. Biol. Chem. (United States) 278 (52): 52012–20. ISSN 0021-9258. PMID 14506230. doi:10.1074/jbc.M308418200. 
  5. ^ a b c d e f g h Scully, R; Anderson S F; Chao D M; Wei W; Ye L; Young R A; Livingston D M; Parvin J D (May 1997). "BRCA1 is a component of the RNA polymerase II holoenzyme". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 94 (11): 5605–10. ISSN 0027-8424. PMC 20825. PMID 9159119. doi:10.1073/pnas.94.11.5605. 
  6. ^ Chiba, N; Parvin J D (October 2001). "Redistribution of BRCA1 among four different protein complexes following replication blockage". J. Biol. Chem. (United States) 276 (42): 38549–54. ISSN 0021-9258. PMID 11504724. doi:10.1074/jbc.M105227200. 
  7. ^ Krum, Susan A; Womack James E; Lane Timothy F (September 2003). "Bovine BRCA1 shows classic responses to genotoxic stress but low in vitro transcriptional activation activity". Oncogene (England) 22 (38): 6032–44. ISSN 0950-9232. PMID 12955082. doi:10.1038/sj.onc.1206515. 
  8. ^ Kim, J B; Yamaguchi Y; Wada T; Handa H; Sharp P A (September 1999). "Tat-SF1 Protein Associates with RAP30 and Human SPT5 Proteins". Mol. Cell. Biol. (UNITED STATES) 19 (9): 5960–8. ISSN 0270-7306. PMC 84462. PMID 10454543. 
  9. ^ Wada, T; Takagi T, Yamaguchi Y, Ferdous A, Imai T, Hirose S, Sugimoto S, Yano K, Hartzog G A, Winston F, Buratowski S, Handa H (February 1998). "DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs". Genes Dev. (UNITED STATES) 12 (3): 343–56. ISSN 0890-9369. PMC 316480. PMID 9450929. doi:10.1101/gad.12.3.343. 
  10. ^ a b c d 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. ISSN 0021-9258. PMID 9201987. doi:10.1074/jbc.272.27.16815. 
  11. ^ Sato, Shigeo; Tomomori-Sato Chieri, Parmely Tari J, Florens Laurence, Zybailov Boris, Swanson Selene K, Banks Charles A S, Jin Jingji, Cai Yong, Washburn Michael P, Conaway Joan Weliky, Conaway Ronald C (June 2004). "A set of consensus mammalian mediator subunits identified by multidimensional protein identification technology". Mol. Cell (United States) 14 (5): 685–91. ISSN 1097-2765. PMID 15175163. doi:10.1016/j.molcel.2004.05.006. 
  12. ^ Grondin, B; Côté F; Bazinet M; Vincent M; Aubry M (October 1997). "Direct interaction of the KRAB/Cys2-His2 zinc finger protein ZNF74 with a hyperphosphorylated form of the RNA polymerase II largest subunit". J. Biol. Chem. (UNITED STATES) 272 (44): 27877–85. ISSN 0021-9258. PMID 9346935. doi:10.1074/jbc.272.44.27877. 
  13. ^ Kettenberger, Hubert; Armache Karim-Jean; Cramer Patrick (August 2003). "Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage". Cell (United States) 114 (3): 347–57. ISSN 0092-8674. PMID 12914690. doi:10.1016/S0092-8674(03)00598-1. 
  14. ^ Archambault, J; Pan G; Dahmus G K; Cartier M; Marshall N; Zhang S; Dahmus M E; Greenblatt J (October 1998). "FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO". J. Biol. Chem. (UNITED STATES) 273 (42): 27593–601. ISSN 0021-9258. PMID 9765293. doi:10.1074/jbc.273.42.27593. 
  15. ^ Pan, G; Aso T; Greenblatt J (September 1997). "Interaction of elongation factors TFIIS and elongin A with a human RNA polymerase II holoenzyme capable of promoter-specific initiation and responsive to transcriptional activators". J. Biol. Chem. (UNITED STATES) 272 (39): 24563–71. ISSN 0021-9258. PMID 9305922. doi:10.1074/jbc.272.39.24563. 
  16. ^ Hamamoto, Ryuji; Furukawa Yoichi; Morita Masashi; Iimura Yuko; Silva Fabio Pittella; Li Meihua; Yagyu Ryuichiro; Nakamura Yusuke (August 2004). "SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells". Nat. Cell Biol. (England) 6 (8): 731–40. ISSN 1465-7392. PMID 15235609. doi:10.1038/ncb1151. 
  17. ^ Okazawa, Hitoshi; Rich Tina, Chang Alex, Lin Xi, Waragai Masaaki, Kajikawa Masunori, Enokido Yasushi, Komuro Akihiko, Kato Seishi, Shibata Masao, Hatanaka Hiroshi, Mouradian M Maral, Sudol Marius, Kanazawa Ichiro (May 2002). "Interaction between mutant ataxin-1 and PQBP-1 affects transcription and cell death". Neuron (United States) 34 (5): 701–13. ISSN 0896-6273. PMID 12062012. doi:10.1016/S0896-6273(02)00697-9. 
  18. ^ a b c Sif, S; Saurin A J; Imbalzano A N; Kingston R E (March 2001). "Purification and characterization of mSin3A-containing Brg1 and hBrm chromatin remodeling complexes". Genes Dev. (United States) 15 (5): 603–18. ISSN 0890-9369. PMC 312641. PMID 11238380. doi:10.1101/gad.872801. 
  19. ^ a b c Wang, W; Côté J, Xue Y, Zhou S, Khavari P A, Biggar S R, Muchardt C, Kalpana G V, Goff S P, Yaniv M, Workman J L, Crabtree G R (October 1996). "Purification and biochemical heterogeneity of the mammalian SWI-SNF complex". EMBO J. (ENGLAND) 15 (19): 5370–82. ISSN 0261-4189. PMC 452280. PMID 8895581. 
  20. ^ Yang, Jie; Aittomäki Saara; Pesu Marko; Carter Kara; Saarinen Jussi; Kalkkinen Nisse; Kieff Elliott; Silvennoinen Olli (September 2002). "Identification of p100 as a coactivator for STAT6 that bridges STAT6 with RNA polymerase II". EMBO J. (England) 21 (18): 4950–8. ISSN 0261-4189. PMC 126276. PMID 12234934. doi:10.1093/emboj/cdf463. 
  21. ^ Suñé, C; Hayashi T; Liu Y; Lane W S; Young R A; Garcia-Blanco M A (October 1997). "CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription". Mol. Cell. Biol. (UNITED STATES) 17 (10): 6029–39. ISSN 0270-7306. PMC 232452. PMID 9315662. 
  22. ^ Zhao, K; Wang W; Rando O J; Xue Y; Swiderek K; Kuo A; Crabtree G R (November 1998). "Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling". Cell (UNITED STATES) 95 (5): 625–36. ISSN 0092-8674. PMID 9845365. doi:10.1016/S0092-8674(00)81633-5. 

Further reading

  • Jeang KT (1998). "Tat, Tat-associated kinase, and transcription". J. Biomed. Sci. 5 (1): 24–7. PMID 9570510. doi:10.1007/BF02253352. 
  • Yankulov K, Bentley D (1998). "Transcriptional control: Tat cofactors and transcriptional elongation". Curr. Biol. 8 (13): R447–9. PMID 9651670. doi:10.1016/S0960-9822(98)70289-1. 
  • 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. doi:10.1002/(SICI)1097-4644(19991201)75:3<357::AID-JCB1>3.0.CO;2-K. 
  • Szentirmay MN, Sawadogo M (2000). "Spatial organization of RNA polymerase II transcription in the nucleus". Nucleic Acids Res. 28 (10): 2019–25. PMC 105382. PMID 10773068. doi:10.1093/nar/28.10.2019. 
  • 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. doi:10.1080/152165401753544241. 


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