|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0017337,
umls-concept:C0019644,
umls-concept:C0019704,
umls-concept:C0031727,
umls-concept:C0178539,
umls-concept:C0185117,
umls-concept:C0439855,
umls-concept:C0663446,
umls-concept:C0851285,
umls-concept:C2911684
|
|
pubmed:issue |
39
|
|
pubmed:dateCreated |
2010-9-20
|
|
pubmed:abstractText |
Transcription of HIV-1 genes depends on the RNA polymerase II kinase and elongation factor positive transcription elongation factor b (P-TEFb), the complex of cyclin T1 and CDK9. Recent evidence suggests that regulation of transcription by P-TEFb involves chromatin binding and modifying factors. To determine how P-TEFb may connect chromatin remodeling to transcription, we investigated the relationship between P-TEFb and histone H1. We identify histone H1 as a substrate for P-TEFb involved in cellular and HIV-1 transcription. We show that P-TEFb interacts with H1 and that P-TEFb inhibition by RNAi, flavopiridol, or dominant negative CDK9 expression correlates with loss of phosphorylation and mobility of H1 in vivo. Importantly, P-TEFb directs H1 phosphorylation in response to wild-type HIV-1 infection, but not Tat-mutant HIV-1 infection. Our results show that P-TEFb phosphorylates histone H1 at a specific C-terminal phosphorylation site. Expression of a mutant H1.1 that cannot be phosphorylated by P-TEFb also disrupts Tat transactivation in an HIV reporter cell line as well as transcription of the c-fos and hsp70 genes in HeLa cells. We identify histone H1 as a novel P-TEFb substrate, and our results suggest new roles for P-TEFb in both cellular and HIV-1 transcription.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CCNT1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CDK9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin T,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase 9,
http://linkedlifedata.com/resource/pubmed/chemical/Flavonoids,
http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Piperidines,
http://linkedlifedata.com/resource/pubmed/chemical/Positive Transcriptional...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-fos,
http://linkedlifedata.com/resource/pubmed/chemical/flavopiridol,
http://linkedlifedata.com/resource/pubmed/chemical/tat Gene Products, Human...
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Sep
|
|
pubmed:issn |
1083-351X
|
|
pubmed:author |
|
|
pubmed:issnType |
Electronic
|
|
pubmed:day |
24
|
|
pubmed:volume |
285
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
29713-20
|
|
pubmed:dateRevised |
2011-9-30
|
|
pubmed:meshHeading |
pubmed-meshheading:20551309-Cyclin T,
pubmed-meshheading:20551309-Cyclin-Dependent Kinase 9,
pubmed-meshheading:20551309-Flavonoids,
pubmed-meshheading:20551309-Gene Expression Regulation, Viral,
pubmed-meshheading:20551309-Genes, Viral,
pubmed-meshheading:20551309-HIV Infections,
pubmed-meshheading:20551309-HIV-1,
pubmed-meshheading:20551309-HSP70 Heat-Shock Proteins,
pubmed-meshheading:20551309-HeLa Cells,
pubmed-meshheading:20551309-Histones,
pubmed-meshheading:20551309-Humans,
pubmed-meshheading:20551309-Multienzyme Complexes,
pubmed-meshheading:20551309-Phosphorylation,
pubmed-meshheading:20551309-Piperidines,
pubmed-meshheading:20551309-Positive Transcriptional Elongation Factor B,
pubmed-meshheading:20551309-Protein Kinase Inhibitors,
pubmed-meshheading:20551309-Proto-Oncogene Proteins c-fos,
pubmed-meshheading:20551309-tat Gene Products, Human Immunodeficiency Virus
|
|
pubmed:year |
2010
|
|
pubmed:articleTitle |
P-TEFb kinase complex phosphorylates histone H1 to regulate expression of cellular and HIV-1 genes.
|
|
pubmed:affiliation |
Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
|
