A non-proteolytic role for ubiquitin in Tat-mediated transactivation of the HIV-1 promoter

被引：156

作者：

Brès, V

Kiernan, RE

Linares, LK

Chable-Bessia, C

Plechakova, O

Tréand, C

Emiliani, S

Peloponese, JM

Jeang, KT

Coux, O

Scheffner, M

Benkirane, M ^{[1
]}

机构：

[1] Inst Human Genet, Mol Virol Lab, CNRS, UPR 1142, Montpellier, France

[2] Univ Cologne, Zentrum Biochem, D-50931 Cologne, Germany

[3] Ctr Rech Biochim Macromol, UPR 1086, Montpellier, France

[4] Inst Cochin Genet Mol, Dept Malad Infect, F-75014 Paris, France

[5] NIAID, Mol Virol Lab, NIH, Bethesda, MD 20892 USA

来源：

NATURE CELL BIOLOGY | 2003年 / 5卷 / 08期

关键词：

D O I：

10.1038/ncb1023

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The human immunodeficiency virus type 1 (HIV-1) encodes a potent transactivator, Tat, which functions through binding to a short leader RNA, called transactivation responsive element (TAR). Recent studies suggest that Tat activates the HIV-1 long terminal repeat (LTR), mainly by adapting co-activator complexes, such as p300, PCAF and the positive transcription elongation factor P-TEFb, to the promoter. Here, we show that the proto-oncoprotein Hdm2 interacts with Tat and mediates its ubiquitination in vitro and in vivo. In addition, Hdm2 is a positive regulator of Tat-mediated transactivation, indicating that the transcriptional properties of Tat are stimulated by ubiquitination. Fusion of ubiquitin to Tat bypasses the requirement of Hdm2 for efficient transactivation, supporting the notion that ubiquitin has a non-proteolytic function in Tat-mediated transactivation.

引用

页码：754 / 761

页数：8

共 32 条

[1] Activation of integrated provirus requires histone acetyltransferase - p300 AND P/CAF are coactivators for HIV-1 Tat [J].