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http://purl.uniprot.org/citations/16103164http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16103164http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16103164http://www.w3.org/2000/01/rdf-schema#comment"By recruiting the positive transcriptional elongation factor b (P-TEFb) to paused RNA polymerase II, the transactivator Tat stimulates transcriptional elongation of the human immunodeficiency virus type 1 (HIV-1) genome. We found that cyclin-dependent kinase 9 (Cdk9), the catalytic subunit of P-TEFb, is ubiquitylated in vivo. This ubiquitylation depended on the Skp1/Cul1/F-box protein E3 ubiquitin ligase Skp2. Likewise, Tat required Skp2 since its transactivation of the HIV-1 long terminal repeat decreased in primary mouse embryonic fibroblasts, which lacked Skp2. The ubiquitylation of Cdk9 by Skp2 facilitated the formation of the ternary complex between P-TEFb, Tat, and transactivation response element. Thus, our findings underscore the requirement of ubiquitylation for the coactivator function in regulating HIV-1 transcriptional elongation."xsd:string
http://purl.uniprot.org/citations/16103164http://purl.org/dc/terms/identifier"doi:10.1128/jvi.79.17.11135-11141.2005"xsd:string
http://purl.uniprot.org/citations/16103164http://purl.org/dc/terms/identifier"doi:10.1128/jvi.79.17.11135-11141.2005"xsd:string
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/author"Zhang F."xsd:string
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/author"Zhang F."xsd:string
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/author"Peterlin B.M."xsd:string
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/author"Peterlin B.M."xsd:string
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/author"Plemenitas A."xsd:string
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/author"Plemenitas A."xsd:string
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/author"Barboric M."xsd:string
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/author"Barboric M."xsd:string
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/author"Besenicar M."xsd:string
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/author"Besenicar M."xsd:string
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/pages"11135-11141"xsd:string
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/pages"11135-11141"xsd:string
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/title"Ubiquitylation of Cdk9 by Skp2 facilitates optimal Tat transactivation."xsd:string
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/title"Ubiquitylation of Cdk9 by Skp2 facilitates optimal Tat transactivation."xsd:string
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/volume"79"xsd:string
http://purl.uniprot.org/citations/16103164http://purl.uniprot.org/core/volume"79"xsd:string