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rdf:type |
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lifeskim:mentions |
umls-concept:C0014442,
umls-concept:C0024660,
umls-concept:C0035668,
umls-concept:C0039315,
umls-concept:C0302167,
umls-concept:C0965144,
umls-concept:C1100939,
umls-concept:C1506764,
umls-concept:C1566354,
umls-concept:C1723137,
umls-concept:C1957815
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pubmed:issue |
16
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pubmed:dateCreated |
2001-4-17
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pubmed:abstractText |
HIV gene expression is subject to a transcriptional checkpoint, whereby negative transcription elongation factors induce an elongation block that is overcome by HIV Tat protein in conjunction with P-TEFb. P-TEFb is a cyclin-dependent kinase that catalyzes Tat-dependent phosphorylation of Ser-5 of the Pol II C-terminal domain (CTD). Ser-5 phosphorylation confers on the CTD the ability to recruit the mammalian mRNA capping enzyme (Mce1) and stimulate its guanylyltransferase activity. Here we show that Tat spearheads a second and novel pathway of capping enzyme recruitment and activation via a direct physical interaction between the C-terminal domain of Tat and Mce1. Tat stimulates the guanylyltransferase and triphosphatase activities of Mce1 and thereby enhances the otherwise low efficiency of cap formation on a TAR stem-loop RNA. Our findings suggest that multiple mechanisms exist for coupling transcription elongation and mRNA processing.
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pubmed:grant |
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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/Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoserine,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Polymerase II,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/guanylyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/mRNA guanylyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/tat Gene Products, Human...
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12959-66
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:11278368-Animals,
pubmed-meshheading:11278368-Base Sequence,
pubmed-meshheading:11278368-Binding Sites,
pubmed-meshheading:11278368-Gene Products, tat,
pubmed-meshheading:11278368-HIV Long Terminal Repeat,
pubmed-meshheading:11278368-HIV-1,
pubmed-meshheading:11278368-Humans,
pubmed-meshheading:11278368-Kinetics,
pubmed-meshheading:11278368-Mammals,
pubmed-meshheading:11278368-Mice,
pubmed-meshheading:11278368-Nucleic Acid Conformation,
pubmed-meshheading:11278368-Nucleotidyltransferases,
pubmed-meshheading:11278368-Phosphorylation,
pubmed-meshheading:11278368-Phosphoserine,
pubmed-meshheading:11278368-RNA Polymerase II,
pubmed-meshheading:11278368-Recombinant Proteins,
pubmed-meshheading:11278368-Ribonucleases,
pubmed-meshheading:11278368-tat Gene Products, Human Immunodeficiency Virus
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pubmed:year |
2001
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pubmed:articleTitle |
HIV-1 Tat protein interacts with mammalian capping enzyme and stimulates capping of TAR RNA.
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pubmed:affiliation |
Department of Pharmacology, UMDNJ-Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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