期刊
JOURNAL OF VIROLOGY
卷 79, 期 17, 页码 11135-11141出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.79.17.11135-11141.2005
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资金
- NIAID NIH HHS [R01 AI49104, R01 AI049104] Funding Source: Medline
By recruiting the positive transcriptional elongation factor b (P-TEFb) to paused RNA polymerase 11, 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 Skpl/Cull/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.
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