POLR2J









































































Полипептид J РНК-полимеразы II (управляемой ДНК), 13.3kDa
Идентификаторы
Символ
POLR2J ; POLR2J1; RPB11; RPB11A; RPB11m; hRPB14
Внешние ID
OMIM: 604150 MGI: 109582 HomoloGene: 4542 GeneCards: POLR2J Gene
номер EC 2.7.7.6

















Профиль экспрессии РНК
PBB GE POLR2J 212782 x at tn.png
Больше информации
Ортологи
Вид Человек Мышь
Entrez 5439 20022
Ensembl ENSG00000005075 ENSMUSG00000039771
UniProt P52435 O08740
RefSeq (мРНК) NM_006234 NM_011293
RefSeq (белок) NP_006225 NP_035423
Локус (UCSC) Chr 7:
102.11 – 102.12 Mb
Chr 5:
136.12 – 136.12 Mb
Поиск в PubMed
[1] [2]

Субъединица RPB11 ДНК-управляемой РНК-полимеразы II  — фермент, кодируемый у человека геном POLR2J .




Содержание






  • 1 Функция


  • 2 Взаимодействия


  • 3 Примечания


  • 4 Литература





Функция |


Этот ген кодирует субъединицу РНК-полимеразы II, полимеразы, ответственной за синтез РНК у эукариот. Продукт этого гена существует в виде гетеродимера с другими полимеразными субъединицами; вместе они образуют основной блок полимеразы. Два аналогичных гена расположены рядом на хромосоме 7q22.1 и псевдоген находится на хромосоме 7p13.[1]



Взаимодействия |


POLR2J, как было выявлено, взаимодействуют с:




  • Apoptosis antagonizing transcription factor[en],[2]


  • POLR2C,[3][4]


  • SATB1.[5]



Примечания |





  1. Entrez Gene: POLR2J polymerase (RNA) II (DNA directed) polypeptide J, 13.3kDa.


  2. Fanciulli M, Bruno T, Di Padova M, De Angelis R, Iezzi S, Iacobini C, Floridi A, Passananti C (May 2000). “Identification of a novel partner of RNA polymerase II subunit 11, Che-1, which interacts with and affects the growth suppression function of Rb”. FASEB J. 14 (7): 904–12. PMID 10783144..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"""""""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}


  3. 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. 272 (27): 16815–21. DOI:10.1074/jbc.272.27.16815. PMID 9201987.


  4. Corbi N, Di Padova M, De Angelis R, Bruno T, Libri V, Iezzi S, Floridi A, Fanciulli M, Passananti C (October 2002). “The alpha-like RNA polymerase II core subunit 3 (RPB3) is involved in tissue-specific transcription and muscle differentiation via interaction with the myogenic factor myogenin”. FASEB J. 16 (12): 1639–41. DOI:10.1096/fj.02-0123fje. PMID 12207009.


  5. Durrin LK, Krontiris TG (June 2002). “The thymocyte-specific MAR binding protein, SATB1, interacts in vitro with a novel variant of DNA-directed RNA polymerase II, subunit 11”. Genomics. 79 (6): 809–17. DOI:10.1006/geno.2002.6772. PMID 12036295.




Литература |





  • Jeang KT (1998). “Tat, Tat-associated kinase, and transcription”. J. Biomed. Sci. 5 (1): 24—7. DOI:10.1007/BF02253352. PMID 9570510.


  • Yankulov K, Bentley D (1998). “Transcriptional control: Tat cofactors and transcriptional elongation”. Curr. Biol. 8 (13): R447—9. DOI:10.1016/S0960-9822(98)70289-1. PMID 9651670.


  • Romano G, Kasten M, De Falco G, Micheli P, Khalili K, Giordano A (2000). “Regulatory functions of Cdk9 and of cyclin T1 in HIV tat transactivation pathway gene expression”. J. Cell. Biochem. 75 (3): 357—68. DOI:10.1002/(SICI)1097-4644(19991201)75:3<357::AID-JCB1>3.0.CO;2-K. 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. DOI:10.1080/152165401753544241. 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, Apolloni A, Meredith L (2007). “Will diverse Tat interactions lead to novel antiretroviral drug targets?”. Current drug targets. 7 (12): 1595—606. DOI:10.2174/138945006779025338. PMID 17168834.


  • Kato H, Sumimoto H, Pognonec P, Chen CH, Rosen CA, Roeder RG (1992). “HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors”. Genes Dev. 6 (4): 655—66. DOI:10.1101/gad.6.4.655. 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. DOI:10.1073/pnas.92.16.7153. PMC 41297. 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. PMC 188757. 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. DOI:10.1073/pnas.93.6.2505. PMC 39827. 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. PMC 190394. PMID 8676484.


  • Fanciulli M, Bruno T, Cerboni C, Bonetto F, Iacobini C, Frati L, Piccoli M, Floridi A, Santoni A, Punturieri A (1996). “Cloning of a novel human RNA polymerase II subunit downregulated by doxorubicin: new potential mechanisms of drug related toxicity”. FEBS Lett. 384 (1): 48—52. DOI:10.1016/0014-5793(96)00277-3. PMID 8797801.


  • Agostini I, Navarro JM, Rey F, Bouhamdan M, Spire B, Vigne R, Sire J (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. DOI:10.1126/science.274.5287.605. PMID 8849451.


  • Okamoto H, Sheline CT, Corden JL, Jones KA, Peterlin BM (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. DOI:10.1073/pnas.93.21.11575. PMC 38099. 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. DOI:10.1074/jbc.271.44.27888. 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. DOI:10.1074/jbc.272.11.6951. PMID 9054383.


  • Cujec TP, Cho H, Maldonado E, Meyer J, Reinberg D, Peterlin BM (1997). “The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme”. Mol. Cell. Biol. 17 (4): 1817—23. PMC 232028. PMID 9121429.









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