Linked Life Data

12114499

Source:http://linkedlifedata.com/resource/pubmed/id/12114499

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
37
pubmed:dateCreated
2002-9-9
pubmed:abstractText
Human immunodeficiency virus, type 1 (HIV-1), Tat protein activates viral gene expression through promoting transcriptional elongation by RNA polymerase II (RNAPII). In this process Tat enhances phosphorylation of the C-terminal domain (CTD) of RNAPII by activating cell cycle-dependent kinases (CDKs) associated with general transcription factors of the promoter complex, specifically CDK7 and CDK9. We reported a Tat-associated T-cell-derived kinase, which contained CDK2. Here, we provide further evidence that CDK2 is involved in Tat-mediated CTD phosphorylation and in HIV-1 transcription in vitro. Tat-mediated CTD phosphorylation by CDK2 required cysteine 22 in the activation domain of Tat and amino acids 42-72 of Tat. CDK2 phosphorylated Tat itself, apparently by forming dynamic contacts with amino acids 15-24 and 36-49 of Tat. Also, amino acids 24-36 and 45-72 of Tat interacted with CTD. CDK2 associated with RNAPII and was found in elongation complexes assembled on HIV-1 long-terminal repeat template. Recombinant CDK2/cyclin E stimulated Tat-dependent HIV-1 transcription in reconstituted transcription assay. Immunodepletion of CDK2/cyclin E in HeLa nuclear extract blocked Tat-dependent transcription. 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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
277
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
33922-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12114499-Amino Acid Sequence, pubmed-meshheading:12114499-CDC2-CDC28 Kinases, pubmed-meshheading:12114499-Cyclin E, pubmed-meshheading:12114499-Cyclin-Dependent Kinase 2, pubmed-meshheading:12114499-Cyclin-Dependent Kinases, pubmed-meshheading:12114499-Gene Products, tat, pubmed-meshheading:12114499-HIV-1, pubmed-meshheading:12114499-HeLa Cells, pubmed-meshheading:12114499-Humans, pubmed-meshheading:12114499-Molecular Sequence Data, pubmed-meshheading:12114499-Phosphorylation, pubmed-meshheading:12114499-Promoter Regions, Genetic, pubmed-meshheading:12114499-Protein-Serine-Threonine Kinases, pubmed-meshheading:12114499-RNA Polymerase II, pubmed-meshheading:12114499-Repetitive Sequences, Amino Acid, pubmed-meshheading:12114499-Transcription, Genetic, pubmed-meshheading:12114499-tat Gene Products, Human Immunodeficiency Virus
pubmed:year
2002
pubmed:articleTitle
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.
pubmed:affiliation
Department of Biochemistry & Molecular Biology, George Washington University Medical Center, Washington, D.C. 20037, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't