POLR2G

Summary

Gene Symbol: POLR2G
Description: RNA polymerase II subunit G
Alias: RPB19, RPB7, hRPB19, hsRPB7, DNA-directed RNA polymerase II subunit RPB7, DNA directed RNA polymerase II 19 kda polypeptide, DNA-directed RNA polymerase II 19 kDa polypeptide, DNA-directed RNA polymerase II subunit G, RNA polymerase II 19 kDa subunit, RNA polymerase II seventh subunit, RNA polymerase II subunit B7, polymerase (RNA) II (DNA directed) polypeptide G, polymerase (RNA) II subunit G
Species: human
Products:     POLR2G

Top Publications

  1. Agostini I, Navarro J, Rey F, Bouhamdan M, Spire B, Vigne R, et al. The human immunodeficiency virus type 1 Vpr transactivator: cooperation with promoter-bound activator domains and binding to TFIIB. J Mol Biol. 1996;261:599-606 pubmed
    ..We demonstrated that the portion of Vpr ranging from amino acids 15 to 77 interacts specifically with the basal transcription factor TFIIB. Also, our data indicated that the N-terminal domain of TFIIB is required for the interaction. ..
  2. Kim Y, Bourgeois C, Isel C, Churcher M, Karn J. Phosphorylation of the RNA polymerase II carboxyl-terminal domain by CDK9 is directly responsible for human immunodeficiency virus type 1 Tat-activated transcriptional elongation. Mol Cell Biol. 2002;22:4622-37 pubmed
    ..We conclude that phosphorylation of the RNA polymerase II CTD by CDK9 enhances transcription elongation directly. ..
  3. Petermann R, Mossier B, Aryee D, Khazak V, Golemis E, Kovar H. Oncogenic EWS-Fli1 interacts with hsRPB7, a subunit of human RNA polymerase II. Oncogene. 1998;17:603-10 pubmed
    ..Employing yeast two-hybrid cloning we isolated the seventh largest subunit of human RNA polymerase II (hsRPB7) as a protein that specifically interacts with the amino terminus of EWS...
  4. Isel C, Karn J. Direct evidence that HIV-1 Tat stimulates RNA polymerase II carboxyl-terminal domain hyperphosphorylation during transcriptional elongation. J Mol Biol. 1999;290:929-41 pubmed
    ..We conclude that activation of the CDK9 kinase, leading to CTD phosphorylation, occurs only in elongation complexes that have transcribed through the Tat-recognition element, TAR RNA. ..
  5. Bourgeois C, Kim Y, Churcher M, West M, Karn J. Spt5 cooperates with human immunodeficiency virus type 1 Tat by preventing premature RNA release at terminator sequences. Mol Cell Biol. 2002;22:1079-93 pubmed
    ..This novel biochemical function of Spt5 is analogous to the function of NusG, an elongation factor found in Escherichia coli that enhances RNA polymerase stability on templates and shows sequence similarity to Spt5. ..
  6. Garber M, Mayall T, Suess E, Meisenhelder J, Thompson N, Jones K. CDK9 autophosphorylation regulates high-affinity binding of the human immunodeficiency virus type 1 tat-P-TEFb complex to TAR RNA. Mol Cell Biol. 2000;20:6958-69 pubmed
    ..Taken together, these results demonstrate that CDK9 phosphorylation is required for high-affinity binding of Tat-P-TEFb to TAR RNA and that the state of P-TEFb phosphorylation may regulate Tat transactivation in vivo. ..
  7. Bertolotti A, Melot T, Acker J, Vigneron M, Delattre O, Tora L. 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. 1998;18:1489-97 pubmed
    ..These observations suggest that EWS and EWS-FLI-1 may play different roles in Pol II transcription. ..
  8. Hamasaki T, Okamoto M, Baba M. Identification of novel inhibitors of human immunodeficiency virus type 1 replication by in silico screening targeting cyclin T1/Tat interaction. Antimicrob Agents Chemother. 2013;57:1323-31 pubmed publisher
    ..Thus, a series of compounds described herein are novel inhibitors of HIV-1 transcription through inhibition of CycT1/Tat interaction. ..
  9. He N, Liu M, Hsu J, Xue Y, Chou S, Burlingame A, et al. HIV-1 Tat and host AFF4 recruit two transcription elongation factors into a bifunctional complex for coordinated activation of HIV-1 transcription. Mol Cell. 2010;38:428-38 pubmed publisher
    ..The ability of Tat to enable two different classes of elongation factors to cooperate and coordinate their actions on the same polymerase enzyme explains why Tat is such a powerful activator of HIV-1 transcription. ..

More Information

Publications86

  1. Nekhai S, Jeang K. Transcriptional and post-transcriptional regulation of HIV-1 gene expression: role of cellular factors for Tat and Rev. Future Microbiol. 2006;1:417-26 pubmed
    ..Rev primarily functions to export unspliced and partially spliced viral RNAs from the nucleus into the cytoplasm. For this activity, Rev cooperates with cellular transport protein CRM1 and RNA helicases DDX1 and DDX3, amongst others. ..
  2. Stevens M, De Clercq E, Balzarini J. The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention. Med Res Rev. 2006;26:595-625 pubmed
    ..As such, targeting of Tat protein (and/or cellular cofactors) provide an interesting perspective for therapeutic intervention in the HIV replicative cycle and may afford lifetime control of the HIV infection. ..
  3. Na X, Duan H, Messing E, Schoen S, Ryan C, di Sant agnese P, et al. Identification of the RNA polymerase II subunit hsRPB7 as a novel target of the von Hippel-Lindau protein. EMBO J. 2003;22:4249-59 pubmed
    ..Here, we report that the pVHL can directly bind to the human RNA polymerase II seventh subunit (hsRPB7) through its beta-domain, and naturally occurring beta-domain mutations can decrease the ..
  4. Ping Y, Rana T. DSIF and NELF interact with RNA polymerase II elongation complex and HIV-1 Tat stimulates P-TEFb-mediated phosphorylation of RNA polymerase II and DSIF during transcription elongation. J Biol Chem. 2001;276:12951-8 pubmed
    ..These findings reveal a molecular mechanism for the negative and positive regulation of transcriptional elongation at the HIV-1 promoter. ..
  5. Fujinaga K, Cujec T, Peng J, Garriga J, Price D, Grana X, et al. The ability of positive transcription elongation factor B to transactivate human immunodeficiency virus transcription depends on a functional kinase domain, cyclin T1, and Tat. J Virol. 1998;72:7154-9 pubmed
    ..Moreover, P-TEFb binds to TAR only in the presence of Tat. We conclude that Tat-P-TEFb complexes bind to TAR, where CDK9 modifies RNA polymerase II for the efficient copying of the viral genome. ..
  6. Wei P, Garber M, Fang S, Fischer W, Jones K. A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA. Cell. 1998;92:451-62 pubmed
    ..Moreover, overexpression of human cyclin T rescues Tat activity in nonpermissive rodent cells. We propose that Tat directs cyclin T-CDK9 to RNAPII through cooperative binding to TAR RNA. ..
  7. Keen N, Gait M, Karn J. Human immunodeficiency virus type-1 Tat is an integral component of the activated transcription-elongation complex. Proc Natl Acad Sci U S A. 1996;93:2505-10 pubmed
    ..We conclude that Tat and cellular cofactors become attached to the transcription complex during its transit through TAR. ..
  8. Herrmann C, Rice A. 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. 1995;69:1612-20 pubmed
    ..Taken together, these results imply that TAK is a very promising candidate for a cellular factor that mediates Tat transactivation. ..
  9. Ivanov D, Kwak Y, Guo J, Gaynor R. Domains in the SPT5 protein that modulate its transcriptional regulatory properties. Mol Cell Biol. 2000;20:2970-83 pubmed
    ..These results suggest that C-terminal repeats in SPT5, like those in the RNA polymerase II C-terminal domain, are sites for P-TEFb phosphorylation and function in modulating its transcriptional elongation properties. ..
  10. Kumar D, Sharma N. Modulating the level of the Rpb7 subunit of RNA polymerase II affects cell separation in Schizosaccharomyces pombe. Res Microbiol. 2015;166:20-7 pubmed publisher
    The rpb7(+) gene encodes the seventh largest subunit of RNA polymerase II and is essential for survival of yeast cells...
  11. Félix A, Ciudad C, Noe V. Functional pharmacogenomics and toxicity of PolyPurine Reverse Hoogsteen hairpins directed against survivin in human cells. Biochem Pharmacol. 2018;155:8-20 pubmed publisher
    ..interacting gene-nodes within the response of PC3 cells to treatment with the PPRH against survivin, mainly POLR2G, PAK1IP1, SMC3, SF3A1, PPARGC1A, NCOA6, UGT2B7, ALG5, VAMP7 and HIST1H2BE, the former six present in the Gene Sets ..
  12. Zhang Y, Zhang T, Chen Y. Comprehensive Analysis of Gene Expression Profiles and DNA Methylome reveals Oas1, Ppie, Polr2g as Pathogenic Target Genes of Gestational Diabetes Mellitus. Sci Rep. 2018;8:16244 pubmed publisher
    ..We identified Oas1, Ppie, Polr2g as possible pathogenic target genes of GDM by combining protein-protein interaction analysis...
  13. Paziewska A, Habior A, Rogowska A, Zych W, Goryca K, Karczmarski J, et al. A novel approach to genome-wide association analysis identifies genetic associations with primary biliary cholangitis and primary sclerosing cholangitis in Polish patients. BMC Med Genomics. 2017;10:2 pubmed publisher
    ..The SNP, rs35730843, mapping to the POLR2G gene promoter (P = 1.2 × 10-5, OR = 0...
  14. Plaschka C, Larivière L, Wenzeck L, Seizl M, Hemann M, Tegunov D, et al. Architecture of the RNA polymerase II-Mediator core initiation complex. Nature. 2015;518:376-80 pubmed publisher
    ..7 Å resolution. cMed binds Pol II around the Rpb4-Rpb7 stalk near the carboxy-terminal domain (CTD)...
  15. Villanyi Z, Ribaud V, Kassem S, Panasenko O, Pahi Z, Gupta I, et al. The Not5 subunit of the ccr4-not complex connects transcription and translation. PLoS Genet. 2014;10:e1004569 pubmed publisher
    Recent studies have suggested that a sub-complex of RNA polymerase II composed of Rpb4 and Rpb7 couples the nuclear and cytoplasmic stages of gene expression by associating with newly made mRNAs in the nucleus, and contributing to their ..
  16. Park S, Kwon S, Hwang J, Park D, Kim T, Kim C. Selection of appropriate reference genes for RT-qPCR analysis in Berkshire, Duroc, Landrace, and Yorkshire pigs. Gene. 2015;558:152-8 pubmed publisher
    ..the expression stability of 15 well-known candidate reference genes (ACTB, ALDOA, B2M, GAPDH, HPAR1, HSPCB, PGK1, POLR2G, PPIA, RPL4, RPS18, SDHA, TBP, TOP2B, and YWHAZ) in seven body tissues (liver, lung, kidney, spleen, stomach, ..
  17. Kershnar E, Wu S, Chiang C. Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes. J Biol Chem. 1998;273:34444-53 pubmed
  18. Chun R, Jeang K. 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. 1996;271:27888-94 pubmed
    ..Taken together, these observations address mechanistic corollaries between activators with(out) a linked CTD kinase and regulated transcription by RNA polymerase II moieties with(out) a CTD. ..
  19. Nogues G, Kadener S, Cramer P, Bentley D, Kornblihtt A. Transcriptional activators differ in their abilities to control alternative splicing. J Biol Chem. 2002;277:43110-4 pubmed
    ..Rapid, highly processive transcription favors EDI exon skipping, whereas slower, less processive transcription favors inclusion. ..
  20. Cramer P, Bushnell D, Fu J, Gnatt A, Maier Davis B, Thompson N, et al. Architecture of RNA polymerase II and implications for the transcription mechanism. Science. 2000;288:640-9 pubmed
    ..A pore in the protein complex beneath the active center may allow entry of substrates for polymerization and exit of the transcript during proofreading and passage through pause sites in the DNA. ..
  21. Meka H, Werner F, Cordell S, Onesti S, Brick P. Crystal structure and RNA binding of the Rpb4/Rpb7 subunits of human RNA polymerase II. Nucleic Acids Res. 2005;33:6435-44 pubmed
    The Rpb4 and Rpb7 subunits of eukaryotic RNA polymerase II (RNAP(II)) form a heterodimer that protrudes from the 10-subunit core of the enzyme. We have obtained crystals of the human Rpb4/Rpb7 heterodimer and determined the structure to 2...
  22. Yang X, Herrmann C, Rice A. 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. 1996;70:4576-84 pubmed
    ..These observations strengthen the proposal that the mechanism of action of Tat involves the recruitment or activation of TAK, resulting in activated transcription through phosphorylation of the CTD. ..
  23. De Graeve F, Bahr A, Chatton B, Kedinger C. A murine ATFa-associated factor with transcriptional repressing activity. Oncogene. 2000;19:1807-19 pubmed
    ..Together, these findings suggest that mAM may be involved in the fine-tuning of ATFa-regulated gene expression, by interfering with the assembly or stability of specific preinitiation transcription complexes. ..
  24. Li Z, Guo J, Wu Y, Zhou Q. The BET bromodomain inhibitor JQ1 activates HIV latency through antagonizing Brd4 inhibition of Tat-transactivation. Nucleic Acids Res. 2013;41:277-87 pubmed publisher
  25. Jeronimo C, Langelier M, Zeghouf M, Cojocaru M, Bergeron D, Baali D, et al. RPAP1, a novel human RNA polymerase II-associated protein affinity purified with recombinant wild-type and mutated polymerase subunits. Mol Cell Biol. 2004;24:7043-58 pubmed
  26. García Martínez L, Mavankal G, Neveu J, Lane W, Ivanov D, Gaynor R. Purification of a Tat-associated kinase reveals a TFIIH complex that modulates HIV-1 transcription. EMBO J. 1997;16:2836-50 pubmed
    ..These results define a cellular kinase complex whose activity is modulated by Tat to result in activation of HIV-1 trancription. ..
  27. Ivanov D, Kwak Y, Nee E, Guo J, García Martínez L, Gaynor R. Cyclin T1 domains involved in complex formation with Tat and TAR RNA are critical for tat-activation. J Mol Biol. 1999;288:41-56 pubmed
    ..These results demonstrate that cyclin T1 interactions with Tat and TAR RNA are critical for activation of HIV-1 gene expression. ..
  28. Agbottah E, Zhang N, Dadgar S, Pumfery A, Wade J, Zeng C, et al. Inhibition of HIV-1 virus replication using small soluble Tat peptides. Virology. 2006;345:373-89 pubmed
    ..Finally, we show that these peptides do not allow loading of the catalytic domain of the cdk/cyclin complex onto the HIV-1 promoter in vivo. ..
  29. Mbonye U, Karn J. Control of HIV latency by epigenetic and non-epigenetic mechanisms. Curr HIV Res. 2011;9:554-67 pubmed
  30. Montanuy I, Torremocha R, Hernández Munain C, Suñé C. Promoter influences transcription elongation: TATA-box element mediates the assembly of processive transcription complexes responsive to cyclin-dependent kinase 9. J Biol Chem. 2008;283:7368-78 pubmed publisher
  31. Wilusz J. Putting an 'End' to HIV mRNAs: capping and polyadenylation as potential therapeutic targets. AIDS Res Ther. 2013;10:31 pubmed publisher
    ..This review describes these post-transcriptional novelties of HIV gene expression as well as their implications in viral biology and as possible targets for therapeutic intervention. ..
  32. Schlegel B, Green V, Ladias J, Parvin J. BRCA1 interaction with RNA polymerase II reveals a role for hRPB2 and hRPB10alpha in activated transcription. Proc Natl Acad Sci U S A. 2000;97:3148-53 pubmed
    ..No other Pol II subunits tested inhibited activated transcription in these assays. Furthermore, hRPB10alpha, but not hRPB2, blocked Sp1-dependent activation. ..
  33. Acker J, de Graaff M, Cheynel I, Khazak V, Kedinger C, Vigneron M. Interactions between the human RNA polymerase II subunits. J Biol Chem. 1997;272:16815-21 pubmed
    ..These subunits, which are able to homodimerize and to interact, may constitute the nucleation center for polymerase assembly, by providing a large interface to most of the other subunits. ..
  34. Zhao Y, Li K, Ng K, Ng C, Lee K. The RNA Pol II sub-complex hsRpb4/7 is required for viability of multiple human cell lines. Protein Cell. 2012;3:846-54 pubmed publisher
    ..Protracted cell death occurs by an unknown mechanism and in some cases is accompanied by a pronounced elongated cell morphology. In conclusion we provide evidence for a gene-specific role of hsRpb4/7 in human cell viability. ..
  35. Suñé C, Garcia Blanco M. Transcriptional cofactor CA150 regulates RNA polymerase II elongation in a TATA-box-dependent manner. Mol Cell Biol. 1999;19:4719-28 pubmed
    ..In addition, we also provide evidence suggesting a role for CA150 in the regulation of cellular transcriptional processes. ..
  36. Zhou M, Halanski M, Radonovich M, Kashanchi F, Peng J, Price D, et al. Tat modifies the activity of CDK9 to phosphorylate serine 5 of the RNA polymerase II carboxyl-terminal domain during human immunodeficiency virus type 1 transcription. Mol Cell Biol. 2000;20:5077-86 pubmed
    ..These studies suggest that the ability of Tat to increase transcriptional elongation may be due to its ability to modify the substrate specificity of the CDK9 complex. ..
  37. Jeang K. Tat, Tat-associated kinase, and transcription. J Biomed Sci. 1998;5:24-7 pubmed
    ..Here we review, in brief, the role of Tat-associated kinase in Tat-activated transcription. We discuss evidence that suggests involvement of TFIIH and/or P-TEFb. ..
  38. Suñé C, Hayashi T, Liu Y, Lane W, Young R, Garcia Blanco M. 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. 1997;17:6029-39 pubmed
    ..Furthermore, we found that functional Tat associates with the holoenzyme whereas activation-deficient Tat mutants do not. Thus, we propose that Tat action is transduced via an RNA polymerase II holoenzyme that contains CA150. ..
  39. Agostini I, Navarro J, Bouhamdan M, Willetts K, Rey F, Spire B, et al. The HIV-1 Vpr co-activator induces a conformational change in TFIIB. FEBS Lett. 1999;450:235-9 pubmed
    ..Our data show a correlation between the ability of Vpr-mutated proteins to stimulate transcription and their ability to induce a conformational change in TFIIB, indicating a functional relevance of the Vpr-TFIIB interaction. ..
  40. Liu Y, Suñé C, Garcia Blanco M. Human immunodeficiency virus type 1 Tat-dependent activation of an arrested RNA polymerase II elongation complex. Virology. 1999;255:337-46 pubmed
    ..These data indicate that Tat can activate elongation of RNA polymerase by modifying an already elongating transcription complex. The data also suggest the possibility that Tat can interact with initiation complexes. ..
  41. Nilson K, Price D. The Role of RNA Polymerase II Elongation Control in HIV-1 Gene Expression, Replication, and Latency. Genet Res Int. 2011;2011:726901 pubmed publisher
    ..HIV, the causative agent of AIDS, is a worldwide health concern. It is hoped that knowledge of the mechanisms regulating the expression of the HIV genome will lead to treatments and ultimately a cure. ..
  42. Kaehlcke K, Dorr A, Hetzer Egger C, Kiermer V, Henklein P, Schnoelzer M, et al. Acetylation of Tat defines a cyclinT1-independent step in HIV transactivation. Mol Cell. 2003;12:167-76 pubmed
    ..We propose that Tat acetylation may help in dissociating the Tat cofactor CyclinT1 from TAR RNA and serve to transfer Tat onto the elongating RNA polymerase II. ..
  43. Poon B, Chen I. Human immunodeficiency virus type 1 (HIV-1) Vpr enhances expression from unintegrated HIV-1 DNA. J Virol. 2003;77:3962-72 pubmed
    ..These results attribute a new function to HIV-1 Vpr and implicate Vpr as a critical component in expression from unintegrated HIV-1 DNA...
  44. Kino T, Tsukamoto M, Chrousos G. Transcription factor TFIIH components enhance the GR coactivator activity but not the cell cycle-arresting activity of the human immunodeficiency virus type-1 protein Vpr. Biochem Biophys Res Commun. 2002;298:17-23 pubmed
    ..These findings suggest that TFIIH participates in Vpr's GR coactivating activity, at a step beyond its interaction with p300/CBP. ..
  45. Romano G, Kasten M, De Falco G, Micheli P, Khalili K, Giordano A. Regulatory functions of Cdk9 and of cyclin T1 in HIV tat transactivation pathway gene expression. J Cell Biochem. 1999;75:357-68 pubmed
  46. Zhou C, Rana T. A bimolecular mechanism of HIV-1 Tat protein interaction with RNA polymerase II transcription elongation complexes. J Mol Biol. 2002;320:925-42 pubmed
    ..These findings suggest that two Tat molecules are involved in performing various functions during a single round of HIV-1 mRNA synthesis. ..
  47. Schoen T, Chandrasekharappa S, Guru S, Mazuruk K, Chader G, Rodriguez I. Human gene for the RNA polymerase II seventh subunit (hsRPB7): structure, expression and chromosomal localization. Biochim Biophys Acta. 1997;1353:39-49 pubmed
    The human gene for the seventh largest subunit of RNA polymerase II complex, hsRPB7 was cloned, sequenced and mapped...
  48. Cai L, Rothbart S, Lu R, Xu B, Chen W, Tripathy A, et al. An H3K36 methylation-engaging Tudor motif of polycomb-like proteins mediates PRC2 complex targeting. Mol Cell. 2013;49:571-82 pubmed publisher
    ..Collectively, our data suggest that PCL recognition of H3K36me3 promotes intrusion of PRC2 complexes into active chromatin regions to promote gene silencing and modulate the chromatin landscape during development. ..
  49. Bokar J, Shambaugh M, Polayes D, Matera A, Rottman F. Purification and cDNA cloning of the AdoMet-binding subunit of the human mRNA (N6-adenosine)-methyltransferase. RNA. 1997;3:1233-47 pubmed
    ..MT-A70 also contains a long region of homology to the yeast protein SPO8, which is involved in induction of sporulation by an unknown mechanism. ..
  50. Okamoto H, Sheline C, Corden J, Jones K, Peterlin B. Trans-activation by human immunodeficiency virus Tat protein requires the C-terminal domain of RNA polymerase II. Proc Natl Acad Sci U S A. 1996;93:11575-9 pubmed
    ..These results suggest that effects of Tat on the processivity of RNA polymerase II require proteins that are associated with the CTD and may result in the phosphorylation of the CTD. ..
  51. Zhang H, Sun L, Liang J, Yu W, Zhang Y, Wang Y, et al. The catalytic subunit of the proteasome is engaged in the entire process of estrogen receptor-regulated transcription. EMBO J. 2006;25:4223-33 pubmed
    ..These results revealed a mechanism by which the proteasome machinery is recruited in ER-mediated gene transcription. Our experiments also provided evidence implicating SRC coactivators in gene transcription elongation. ..
  52. Kato H, Sumimoto H, Pognonec P, Chen C, Rosen C, Roeder R. HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors. Genes Dev. 1992;6:655-66 pubmed
    ..We propose the hypothesis that Tat acts as a processivity factor on RNA polymerase II in an analogous manner to TFIIF. ..
  53. Zhao W, Liu Y, Timani K, He J. Tip110 protein binds to unphosphorylated RNA polymerase II and promotes its phosphorylation and HIV-1 long terminal repeat transcription. J Biol Chem. 2014;289:190-202 pubmed publisher
    ..Taken together, these findings have provided additional and mechanistic evidence to support Tip110 function in HIV-1 transcription. ..
  54. HU W, Hughes S. HIV-1 reverse transcription. Cold Spring Harb Perspect Med. 2012;2: pubmed publisher
    ..In keeping with the theme of the collection, the emphasis is on HIV-1 and HIV-1 RT. ..
  55. Marcello A, Zoppe M, Giacca M. Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator. IUBMB Life. 2001;51:175-81 pubmed
  56. Deng L, Ammosova T, Pumfery A, Kashanchi F, Nekhai S. HIV-1 Tat interaction with RNA polymerase II C-terminal domain (CTD) and a dynamic association with CDK2 induce CTD phosphorylation and transcription from HIV-1 promoter. J Biol Chem. 2002;277:33922-9 pubmed
    ..We suggest that CDK2 is part of a transcription complex that is required for Tat-dependent transcription and that interaction of Tat with CTD and a dynamic association of Tat with CDK2/cyclin E stimulated CTD phosphorylation by CDK2. ..
  57. Cojocaru M, Jeronimo C, Forget D, Bouchard A, Bergeron D, Cote P, et al. Genomic location of the human RNA polymerase II general machinery: evidence for a role of TFIIF and Rpb7 at both early and late stages of transcription. Biochem J. 2008;409:139-47 pubmed
    ..Unexpectedly, we found that the Rpb7 subunit of RNAPII, known to be required only for the initiation phase of transcription, remains associated with the ..
  58. Sawaya B, Khalili K, Gordon J, Taube R, Amini S. Cooperative interaction between HIV-1 regulatory proteins Tat and Vpr modulates transcription of the viral genome. J Biol Chem. 2000;275:35209-14 pubmed
    ..Moreover identification of R73S mutant of Vpr provides a new therapeutic avenue for controlling HIV-1 gene transcription and replication in the infected cells. ..
  59. Siliciano R, Greene W. HIV latency. Cold Spring Harb Perspect Med. 2011;1:a007096 pubmed publisher
    ..Several approaches are under exploration for reactivating latent virus with the hope that this will allow elimination of the latent reservoir. ..
  60. Nekhai S, Zhou M, Fernandez A, Lane W, Lamb N, Brady J, et al. HIV-1 Tat-associated RNA polymerase C-terminal domain kinase, CDK2, phosphorylates CDK7 and stimulates Tat-mediated transcription. Biochem J. 2002;364:649-57 pubmed
    ..They are also consistent with the observed cell-cycle-specific induction of viral gene transactivation. ..
  61. Southgate C, Zapp M, Green M. Activation of transcription by HIV-1 Tat protein tethered to nascent RNA through another protein. Nature. 1990;345:640-2 pubmed
    ..Our results further suggest that cellular proteins that bind specifically to TAR RNA or TAR DNA may not be essential for Tat-responsiveness. ..
  62. Hogan T, Nonnemacher M, Krebs F, Henderson A, Wigdahl B. HIV-1 Vpr binding to HIV-1 LTR C/EBP cis-acting elements and adjacent regions is sequence-specific. Biomed Pharmacother. 2003;57:41-8 pubmed
    ..These studies suggest that Vpr may regulate the interaction of members of the C/EBP transcription factor family with the viral LTR. ..
  63. Xiao H, Palhan V, Yang Y, Roeder R. TIP30 has an intrinsic kinase activity required for up-regulation of a subset of apoptotic genes. EMBO J. 2000;19:956-63 pubmed
    ..These data demonstrate a molecular mechanism for TIP30/CC3 function and suggest a novel pathway for regulating apoptosis. ..
  64. Kiernan R, Vanhulle C, Schiltz L, Adam E, Xiao H, Maudoux F, et al. HIV-1 tat transcriptional activity is regulated by acetylation. EMBO J. 1999;18:6106-18 pubmed
    ..These data suggest that acetylation of Tat regulates two discrete and functionally critical steps in transcription, binding to an RNAP II CTD-kinase and release of Tat from TAR RNA. ..
  65. Yankulov K, Bentley D. Transcriptional control: Tat cofactors and transcriptional elongation. Curr Biol. 1998;8:R447-9 pubmed
    ..Recent results show that two cellular cyclin-dependent kinases, which phosphorylate the carboxy-terminal domain of the RNA polymerase II large subunit, contact Tat and contribute to the control of transcriptional elongation. ..
  66. Cujec T, Okamoto H, Fujinaga K, Meyer J, Chamberlin H, Morgan D, et al. The HIV transactivator TAT binds to the CDK-activating kinase and activates the phosphorylation of the carboxy-terminal domain of RNA polymerase II. Genes Dev. 1997;11:2645-57 pubmed
    ..Our data identify a cellular protein that interacts with the activation domain of Tat, demonstrate that this interaction is critical for the function of Tat, and provide a mechanism by which Tat increases the processivity of Pol II. ..
  67. Wu Baer F, Sigman D, Gaynor R. 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. 1995;92:7153-7 pubmed
    ..These results suggest that Tat may function to alter RNA polymerase II, which is paused due to its binding to HIV-1 TAR RNA with resultant stimulation of its transcriptional elongation properties. ..
  68. Schaller S, Grandemange S, Shpakovski G, Golemis E, Kedinger C, Vigneron M. Interactions between the full complement of human RNA polymerase II subunits. FEBS Lett. 1999;461:253-7 pubmed
    ..Finally, complementation experiments in yeast indicated that hRPB4 expression efficiently cured both heat and cold-sensitivity of RPB4-lacking strains, supporting the existence of conserved functional subunit interactions. ..
  69. Újvári A, Luse D. RNA emerging from the active site of RNA polymerase II interacts with the Rpb7 subunit. Nat Struct Mol Biol. 2006;13:49-54 pubmed
    ..two possible exit paths for the nascent RNA: groove 1, which points toward the subcomplex of subunits Rpb4 and Rpb7, and groove 2, which points toward Rpb8...
  70. Rice A. The HIV-1 Tat team gets bigger. Cell Host Microbe. 2010;7:179-81 pubmed publisher
    ..Now, Pagans and colleagues report that the lysine methyltransferase Set7/9-KMT7 associates with Tat to stimulate RNA polymerase II elongation of the integrated provirus. Set7/9-KMT7 also methylates Tat, and this enhances Tat function. ..
  71. Nekhai S, Shukla R, Kumar A. A human primary T-lymphocyte-derived human immunodeficiency virus type 1 Tat-associated kinase phosphorylates the C-terminal domain of RNA polymerase II and induces CAK activity. J Virol. 1997;71:7436-41 pubmed
    ..Importantly, the Tat-associated kinase markedly induced CAK. We suggest that the mechanism of Tat-mediated processive transcription of the HIV-1 promoter includes a Tat-associated CAK activator. ..
  72. Zhou M, Kashanchi F, Jiang H, Ge H, Brady J. Phosphorylation of the RAP74 subunit of TFIIF correlates with Tat-activated transcription of the HIV-1 long terminal repeat. Virology. 2000;268:452-60 pubmed
    ..Of importance, the exogenous RAP74 was rapidly phosphorylated in the presence of Tat. These results suggest that RAP74 phosphorylation is one important step, of several, in the Tat transactivation cascade. ..
  73. Khazak V, Estojak J, Cho H, Majors J, Sonoda G, Testa J, et al. Analysis of the interaction of the novel RNA polymerase II (pol II) subunit hsRPB4 with its partner hsRPB7 and with pol II. Mol Cell Biol. 1998;18:1935-45 pubmed
    ..Previously, we have shown that RPB7 possesses an evolutionarily conserved human homolog, hsRPB7, which was capable of partially interacting with RPB4 and the yeast transcriptional apparatus...
  74. Parada C, Roeder R. A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription. EMBO J. 1999;18:3688-701 pubmed
    ..Our results indicate that Tat-SF is a Tat cofactor-containing RNA Pol II complex whose recruitment to the promoter provides elongation factors important for Tat-enhanced HIV-1 transcription following TAR RNA synthesis. ..
  75. Ramanathan Y, Reza S, Young T, Mathews M, PE ERY T. Human and rodent transcription elongation factor P-TEFb: interactions with human immunodeficiency virus type 1 tat and carboxy-terminal domain substrate. J Virol. 1999;73:5448-58 pubmed
    ..We suggest a model in which Tat first interacts with P-TEFb to form the TAK complex that engages with TAR RNA and the elongating transcription complex, resulting in hyperphosphorylation of the CTD on serine 5 residues. ..
  76. Kino T, Gragerov A, Kopp J, Stauber R, Pavlakis G, Chrousos G. The HIV-1 virion-associated protein vpr is a coactivator of the human glucocorticoid receptor. J Exp Med. 1999;189:51-62 pubmed
    ..The glucocorticoid coactivator activity of Vpr may contribute to increased tissue glucocorticoid sensitivity in the absence of hypercortisolism and to the pathogenesis of AIDS. ..
  77. Okamoto T. [Positive and negative regulation of transcription from HIV provirus]. Uirusu. 2011;61:81-9 pubmed
    ..HIV is unique in that it contains virus-specific transcriptional activator called Tat. ..