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rdf:type |
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lifeskim:mentions |
umls-concept:C0019704,
umls-concept:C0031715,
umls-concept:C0035679,
umls-concept:C0035696,
umls-concept:C0302167,
umls-concept:C0961954,
umls-concept:C1100939,
umls-concept:C1514562,
umls-concept:C1707271,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
22
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pubmed:dateCreated |
2003-10-29
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pubmed:abstractText |
The HIV type 1 (HIV-1) Tat protein stimulates transcription elongation by recruiting P-TEFb (CDK9/cyclin T1) to the transactivation response (TAR) RNA structure. Tat-induced CDK9 kinase has been shown to phosphorylate Ser-5 of RNA polymerase II (RNAP II) C-terminal domain (CTD). Results presented here demonstrate that Tat-induced Ser-5 phosphorylation of CTD by P-TEFb stimulates the guanylyltransferase activity of human capping enzyme and RNA cap formation. Sequential phosphorylation of CTD by Tat-induced P-TEFb enhances the stimulation of human capping enzyme guanylyltransferase activity and RNA cap formation by transcription factor IIH-mediated CTD phosphorylation. Using an immobilized template assay that permits isolation of transcription complexes, we show that Tat/TAR-dependent phosphorylation of RNAP II CTD stimulates cotranscriptional capping of HIV-1 mRNA. Upon transcriptional induction of latently infected cells, accumulation of capped transcripts occurs along with Ser-5-phosphorylated RNAP II in the promoter proximal region of the HIV-1 genome. Therefore, these observations suggest that Tat/TAR-dependent phosphorylation of RNAP II CTD is crucial not only in promoting transcription elongation but also in stimulating nascent viral RNA capping.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-10082552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-10198643,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-10421630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-10438593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-10594013,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-10733565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-10866664,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-11018011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-11018013,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-11050942,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-11051760,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-11278368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-11572868,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-11909521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-12067656,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-12213657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-12408826,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-12408827,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-12612070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-12702877,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-1738206,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-7511177,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-7601352,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-8001135,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-9371772,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-9407024,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-9407025,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-9506978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-9545288,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14569024-9651670
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Gene Products, tat,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Caps,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Polymerase II,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/tat Gene Products, Human...
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
28
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pubmed:volume |
100
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12666-71
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:14569024-Binding Sites,
pubmed-meshheading:14569024-Gene Products, tat,
pubmed-meshheading:14569024-HIV-1,
pubmed-meshheading:14569024-Humans,
pubmed-meshheading:14569024-Phosphorylation,
pubmed-meshheading:14569024-RNA, Messenger,
pubmed-meshheading:14569024-RNA, Viral,
pubmed-meshheading:14569024-RNA Caps,
pubmed-meshheading:14569024-RNA Polymerase II,
pubmed-meshheading:14569024-Recombinant Fusion Proteins,
pubmed-meshheading:14569024-Ribonucleotides,
pubmed-meshheading:14569024-Transcription, Genetic,
pubmed-meshheading:14569024-Transcription Factors,
pubmed-meshheading:14569024-tat Gene Products, Human Immunodeficiency Virus
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pubmed:year |
2003
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pubmed:articleTitle |
The Tat/TAR-dependent phosphorylation of RNA polymerase II C-terminal domain stimulates cotranscriptional capping of HIV-1 mRNA.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, George Washington University School of Medicine, Washington, DC 20037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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