These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: A non-proteolytic role for ubiquitin in Tat-mediated transactivation of the HIV-1 promoter.
    Author: 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.
    Journal: Nat Cell Biol; 2003 Aug; 5(8):754-61. PubMed ID: 12883554.
    Abstract:
    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.
    [Abstract] [Full Text] [Related] [New Search]