POLR2G: Difference between revisions

Jump to navigation Jump to search
m (Bot: HTTP→HTTPS)
imported>Bibcode Bot
m (Adding 0 arxiv eprint(s), 6 bibcode(s) and 0 doi(s). Did it miss something? Report bugs, errors, and suggestions at User talk:Bibcode Bot)
 
Line 9: Line 9:


==Interactions==
==Interactions==
POLR2G has been shown to [[Protein-protein interaction|interact]] with [[TAF15]],<ref name=pmid9488465>{{cite journal |last=Bertolotti |first=A |authorlink= |author2=Melot T |author3=Acker J |author4=Vigneron M |author5=Delattre O |author6=Tora L  |date=March 1998  |title=EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes |journal=Mol. Cell. Biol. |volume=18 |issue=3 |pages=1489–97 |publisher= |location = UNITED STATES| issn = 0270-7306| pmid = 9488465 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=108863 }}</ref> [[POLR2C]],<ref name=pmid9201987>{{cite journal |doi=10.1074/jbc.272.27.16815 |last=Acker |first=J |authorlink= |author2=de Graaff M |author3=Cheynel I |author4=Khazak V |author5=Kedinger C |author6=Vigneron M  |date=July 1997  |title=Interactions between the human RNA polymerase II subunits |journal=J. Biol. Chem. |volume=272 |issue=27 |pages=16815–21 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9201987 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[POLR2H]]<ref name=pmid9201987/> and [[POLR2E]].<ref name=pmid9201987/>
POLR2G has been shown to [[Protein-protein interaction|interact]] with [[TAF15]],<ref name=pmid9488465>{{cite journal |last=Bertolotti |first=A |authorlink= |author2=Melot T |author3=Acker J |author4=Vigneron M |author5=Delattre O |author6=Tora L  |date=March 1998  |title=EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes |journal=Mol. Cell. Biol. |volume=18 |issue=3 |pages=1489–97 |publisher= |location = UNITED STATES| issn = 0270-7306| pmid = 9488465 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=108863 | doi=10.1128/mcb.18.3.1489}}</ref> [[POLR2C]],<ref name=pmid9201987>{{cite journal |doi=10.1074/jbc.272.27.16815 |last=Acker |first=J |authorlink= |author2=de Graaff M |author3=Cheynel I |author4=Khazak V |author5=Kedinger C |author6=Vigneron M  |date=July 1997  |title=Interactions between the human RNA polymerase II subunits |journal=J. Biol. Chem. |volume=272 |issue=27 |pages=16815–21 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9201987 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[POLR2H]]<ref name=pmid9201987/> and [[POLR2E]].<ref name=pmid9201987/>


==References==
==References==
Line 25: Line 25:
*{{cite journal  |vauthors=Harrich D, McMillan N, Munoz L, etal |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=10.2174/138945006779025338  }}
*{{cite journal  |vauthors=Harrich D, McMillan N, Munoz L, etal |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=10.2174/138945006779025338  }}
*{{cite journal  |vauthors=Kato H, Sumimoto H, Pognonec P, etal |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=10.1101/gad.6.4.655  }}
*{{cite journal  |vauthors=Kato H, Sumimoto H, Pognonec P, etal |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=10.1101/gad.6.4.655  }}
*{{cite journal  |vauthors=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  |vauthors=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 |bibcode=1990Natur.345..640S }}
*{{cite journal  |vauthors=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=10.1073/pnas.92.16.7153  | pmc=41297  }}
*{{cite journal  |vauthors=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=10.1073/pnas.92.16.7153  | pmc=41297  |bibcode=1995PNAS...92.7153W }}
*{{cite journal  |vauthors=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=  | pmc=188757  }}
*{{cite journal  |vauthors=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=  | pmc=188757  }}
*{{cite journal  |vauthors=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=10.1073/pnas.93.6.2505  | pmc=39827  }}
*{{cite journal  |vauthors=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=10.1073/pnas.93.6.2505  | pmc=39827  |bibcode=1996PNAS...93.2505K }}
*{{cite journal  |vauthors=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=  | pmc=190394  }}
*{{cite journal  |vauthors=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=  | pmc=190394  }}
*{{cite journal  |vauthors=Agostini I, Navarro JM, Rey F, etal |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  |vauthors=Agostini I, Navarro JM, Rey F, etal |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  |vauthors=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=10.1126/science.274.5287.605  }}
*{{cite journal  |vauthors=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=10.1126/science.274.5287.605  |bibcode=1996Sci...274..605Z }}
*{{cite journal  |vauthors=Okamoto H, Sheline CT, Corden JL, etal |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=10.1073/pnas.93.21.11575  | pmc=38099  }}
*{{cite journal  |vauthors=Okamoto H, Sheline CT, Corden JL, etal |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=10.1073/pnas.93.21.11575  | pmc=38099  |bibcode=1996PNAS...9311575O }}
*{{cite journal  |vauthors=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=10.1074/jbc.271.44.27888  }}
*{{cite journal  |vauthors=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=10.1074/jbc.271.44.27888  }}
*{{cite journal  |vauthors=Parada CA, Roeder RG |title=Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain. |journal=Nature |volume=384 |issue= 6607 |pages= 375–8 |year= 1996 |pmid= 8934526 |doi= 10.1038/384375a0 }}
*{{cite journal  |vauthors=Parada CA, Roeder RG |title=Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain. |journal=Nature |volume=384 |issue= 6607 |pages= 375–8 |year= 1996 |pmid= 8934526 |doi= 10.1038/384375a0 |bibcode=1996Natur.384..375P }}
*{{cite journal  |vauthors=García-Martínez LF, Ivanov D, Gaynor RB |title=Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes. |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 6951–8 |year= 1997 |pmid= 9054383 |doi=10.1074/jbc.272.11.6951  }}
*{{cite journal  |vauthors=García-Martínez LF, Ivanov D, Gaynor RB |title=Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes. |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 6951–8 |year= 1997 |pmid= 9054383 |doi=10.1074/jbc.272.11.6951  }}
*{{cite journal  |vauthors=Cujec TP, Cho H, Maldonado E, etal |title=The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme. |journal=Mol. Cell. Biol. |volume=17 |issue= 4 |pages= 1817–23 |year= 1997 |pmid= 9121429 |doi=  | pmc=232028  }}
*{{cite journal  |vauthors=Cujec TP, Cho H, Maldonado E, etal |title=The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme. |journal=Mol. Cell. Biol. |volume=17 |issue= 4 |pages= 1817–23 |year= 1997 |pmid= 9121429 |doi=  | pmc=232028  }}

Latest revision as of 19:46, 25 June 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

DNA-directed RNA polymerase II subunit RPB7 is an enzyme that in humans is encoded by the POLR2G gene.[1][2]

This gene encodes the seventh largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. In yeast, the association of this subunit with the polymerase under suboptimal growth conditions indicates it may play a role in regulating polymerase function.[3]

Interactions

POLR2G has been shown to interact with TAF15,[4] POLR2C,[5] POLR2H[5] and POLR2E.[5]

References

  1. Khazak V, Sadhale PP, Woychik NA, Brent R, Golemis EA (December 1995). "Human RNA polymerase II subunit hsRPB7 functions in yeast and influences stress survival and cell morphology". Mol Biol Cell. 6 (7): 759–75. doi:10.1091/mbc.6.7.759. PMC 301239. PMID 7579693.
  2. Schoen TJ, Chandrasekharappa SC, Guru SC, Mazuruk K, Chader GJ, Rodriguez IR (August 1997). "Human gene for the RNA polymerase II seventh subunit (hsRPB7): structure, expression and chromosomal localization". Biochim Biophys Acta. 1353 (1): 39–49. doi:10.1016/s0167-4781(97)00041-9. PMID 9256063.
  3. "Entrez Gene: POLR2G polymerase (RNA) II (DNA directed) polypeptide G".
  4. Bertolotti, A; Melot T; Acker J; Vigneron M; Delattre O; Tora L (March 1998). "EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes". Mol. Cell. Biol. UNITED STATES. 18 (3): 1489–97. doi:10.1128/mcb.18.3.1489. ISSN 0270-7306. PMC 108863. PMID 9488465.
  5. 5.0 5.1 5.2 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