Biology:POLR2A

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

DNA-directed RNA polymerase II subunit RPB1, also known as RPB1, is an enzyme that in humans is encoded by the POLR2A gene.

Function

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:


References

  1. "Entrez Gene: POLR2A polymerase (RNA) II (DNA directed) polypeptide A, 220kDa". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5430. 
  2. "BRCA1 associates with processive RNA polymerase II". J. Biol. Chem. 278 (52): 52012–20. December 2003. doi:10.1074/jbc.M308418200. PMID 14506230. 
  3. 3.0 3.1 3.2 3.3 3.4 3.5 3.6 3.7 "BRCA1 is a component of the RNA polymerase II holoenzyme". Proc. Natl. Acad. Sci. U.S.A. 94 (11): 5605–10. May 1997. doi:10.1073/pnas.94.11.5605. PMID 9159119. Bibcode1997PNAS...94.5605S. 
  4. "Redistribution of BRCA1 among four different protein complexes following replication blockage". J. Biol. Chem. 276 (42): 38549–54. October 2001. doi:10.1074/jbc.M105227200. PMID 11504724. 
  5. "Bovine BRCA1 shows classic responses to genotoxic stress but low in vitro transcriptional activation activity". Oncogene 22 (38): 6032–44. September 2003. doi:10.1038/sj.onc.1206515. PMID 12955082. 
  6. 6.0 6.1 6.2 6.3 6.4 6.5 6.6 "A human RNA polymerase II complex containing factors that modify chromatin structure". Mol. Cell. Biol. 18 (9): 5355–63. September 1998. doi:10.1128/MCB.18.9.5355. PMID 9710619. 
  7. "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. 17 (10): 6029–39. October 1997. doi:10.1128/MCB.17.10.6029. PMID 9315662. 
  8. "A set of consensus mammalian mediator subunits identified by multidimensional protein identification technology". Mol. Cell 14 (5): 685–91. June 2004. doi:10.1016/j.molcel.2004.05.006. PMID 15175163. 
  9. 9.0 9.1 9.2 9.3 "Interactions between the human RNA polymerase II subunits". J. Biol. Chem. 272 (27): 16815–21. July 1997. doi:10.1074/jbc.272.27.16815. PMID 9201987. 
  10. "Toward cell specificity in SCA1". Neuron 34 (5): 669–70. May 2002. doi:10.1016/s0896-6273(02)00715-8. PMID 12062012. 
  11. 11.0 11.1 11.2 "Purification and characterization of mSin3A-containing Brg1 and hBrm chromatin remodeling complexes". Genes Dev. 15 (5): 603–18. March 2001. doi:10.1101/gad.872801. PMID 11238380. 
  12. 12.0 12.1 12.2 "Purification and biochemical heterogeneity of the mammalian SWI-SNF complex". EMBO J. 15 (19): 5370–82. October 1996. doi:10.1002/j.1460-2075.1996.tb00921.x. PMID 8895581. 
  13. "Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling". Cell 95 (5): 625–36. November 1998. doi:10.1016/s0092-8674(00)81633-5. PMID 9845365. 
  14. "SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells". Nat. Cell Biol. 6 (8): 731–40. August 2004. doi:10.1038/ncb1151. PMID 15235609. 
  15. "Identification of p100 as a coactivator for STAT6 that bridges STAT6 with RNA polymerase II". EMBO J. 21 (18): 4950–8. September 2002. doi:10.1093/emboj/cdf463. PMID 12234934. 
  16. "Tat-SF1 protein associates with RAP30 and human SPT5 proteins". Mol. Cell. Biol. 19 (9): 5960–8. September 1999. doi:10.1128/mcb.19.9.5960. PMID 10454543. 
  17. "DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs". Genes Dev. 12 (3): 343–56. February 1998. doi:10.1101/gad.12.3.343. PMID 9450929. 
  18. "TFIIS and GreB: two like-minded transcription elongation factors with sticky fingers". Cell 114 (3): 272–4. August 2003. doi:10.1016/S0092-8674(03)00607-X. PMID 12914690. 
  19. "FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO". J. Biol. Chem. 273 (42): 27593–601. October 1998. doi:10.1074/jbc.273.42.27593. PMID 9765293. 
  20. "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. 272 (39): 24563–71. September 1997. doi:10.1074/jbc.272.39.24563. PMID 9305922. 
  21. "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. 97 (16): 9015–20. August 2000. doi:10.1073/pnas.160266597. PMID 10908677. Bibcode2000PNAS...97.9015C. 
  22. "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. 272 (44): 27877–85. October 1997. doi:10.1074/jbc.272.44.27877. PMID 9346935. 

Further reading