Tat-mediated elongation of the HIV-1 transcript

Barboric M, Peterlin BM. A New Paradigm in Eukaryotic Biology: HIV Tat and the Control of Transcriptional Elongation. PLoS Biol. 2005 Feb 15;3(2):e76. doi: 10.1371/journal.pbio.0030076.; Liou L, Herrmann CH, Rice AP. HIV-1 infection and regulation of Tat function in macrophages. The International Journal of Biochemistry & Cell Biology. 2004 Sep;36(9):1767–75. doi: 10.1016/j.biocel.2004.02.018.; Fujinaga K, Irwin D, Huang Y, Taube R, Kurosu T, Peterlin BM. Dynamics of Human Immunodeficiency Virus Transcription: P-TEFb Phosphorylates RD and Dissociates Negative Effectors from the Transactivation Response Element. Molecular and Cellular Biology. 2004 Jan 01;24(2):787–95. doi: 10.1128/mcb.24.2.787-795.2004.; Yamaguchi Y, Inukai N, Narita T, Wada T, Handa H. Evidence that Negative Elongation Factor Represses Transcription Elongation through Binding to a DRB Sensitivity-Inducing Factor/RNA Polymerase II Complex and RNA. Molecular and Cellular Biology. 2002 May 01;22(9):2918–27. doi: 10.1128/mcb.22.9.2918-2927.2002.; Zhou M, Halanski MA, Radonovich MF, Kashanchi F, Peng J, Price DH, Brady JN. 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. Molecular and Cellular Biology. 2000 Jul 01;20(14):5077–86. doi: 10.1128/mcb.20.14.5077-5086.2000.; Ivanov D, Kwak YT, Guo J, Gaynor RB. Domains in the SPT5 Protein That Modulate Its Transcriptional Regulatory Properties. Mol Cell Biol. 2000 May;20(9):2970–83. doi: 10.1128/mcb.20.9.2970-2983.2000.; Taube R, Fujinaga K, Wimmer J, Barboric M, Peterlin BM. Tat transactivation: a model for the regulation of eukaryotic transcriptional elongation. Virology. 1999 Nov 25;264(2):245–53. doi: 10.1006/viro.1999.9944. PMID: 10562489.; Karn J. Tackling Tat. J Mol Biol. 1999 Oct 22;293(2):235–54. doi: 10.1006/jmbi.1999.3060. PMID: 10550206.; Yamaguchi Y, Takagi T, Wada T, Yano K, Furuya A, Sugimoto S, Hasegawa J, Handa H. NELF, a multisubunit complex containing RD, cooperates with DSIF to repress RNA polymerase II elongation. Cell. 1999 Apr 02;97(1):41–51. doi: 10.1016/s0092-8674(00)80713-8. PMID: 10199401.; Wei P, Garber ME, Fang SM, Fischer WH, Jones KA. 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 Feb 20;92(4):451–62. doi: 10.1016/s0092-8674(00)80939-3. PMID: 9491887.; Wada T, Takagi T, Yamaguchi Y, Ferdous A, Imai T, Hirose S, Sugimoto S, Yano K, Hartzog GA, Winston F, Buratowski S, Handa H. DSIF, a novel transcription elongation factor that regulates RNA polymerase II processivity, is composed of human Spt4 and Spt5 homologs. Genes & Development. 1998 Feb 01;12(3):343–56. doi: 10.1101/gad.12.3.343.; Herrmann CH, Rice AP. 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 Mar;69(3):1612–20. doi: 10.1128/jvi.69.3.1612-1620.1995.; Dingwall C, Ernberg I, Gait MJ, Green SM, Heaphy S, Karn J, Lowe AD, Singh M, Skinner MA, Valerio R. Human immunodeficiency virus 1 tat protein binds trans-activation-responsive region (TAR) RNA in vitro. Proc. Natl. Acad. Sci. U.S.A. 1989 Sep;86(18):6925–9. doi: 10.1073/pnas.86.18.6925.; Kao SY, Calman AF, Luciw PA, Peterlin BM. Anti-termination of transcription within the long terminal repeat of HIV-1 by tat gene product. Nature. 1987 Dec;330(6147):489–93. doi: 10.1038/330489a0. PMID: 2825027.

Metabolites

ATP(4-)

Formula: C10H12N5O13P3 (502.9644492)

CAS ID:

ADP(3-)

Formula: C10H12N5O10P2 (424.0059412)

CAS ID:



Enzyme

EC Number name full name note
2.7.11.22 cyclin-dependent kinase ATP:cyclin phosphotransferase
2.7.11.23 [RNA-polymerase]-subunit kinase ATP:[DNA-directed RNA polymerase] phosphotransferase
3.1.3.16 protein-serine/threonine phosphatase protein-serine/threonine-phosphate phosphohydrolase
5.6.2.3 DNA 5'-3' helicase DNA 5'-3' helicase (ATP-hydrolysing)
5.6.2.4 DNA 3'-5' helicase DNA 3'-5' helicase (ATP-hydrolysing)


Proteins

Protein ID name full name