Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines

  1. Yunkai Yu1,4,
  2. Zuoxiang Xiao2,4,
  3. Elana S. Ehrlich1,
  4. Xianghui Yu3, and
  5. Xiao-Fang Yu1,2,5
  1. 1Department of Molecular Microbiology and Immunology, Johns Hopkins University Bloomberg School of Public Health, Baltimore, Maryland 21205, USA; 2Zhejiang University, Zhejiang 310009, China; 3Jilin University, Jilin 130023, China

Abstract

APOBEC3G, which induces hypermutations in newly synthesized viral DNA, is suppressed by HIV-1 Vif, acting through Cul5-ElonginB-ElonginC E3 ubiquitin ligase. We have now characterized a novel SOCS box in HIV-1 Vif that mediates its interaction with ElonginC. In this SOCS box, alanine replaces the consensus cysteine in the previously identified SOCS box. This new motif was necessary but insufficient for interaction with Cul5-ElonginB-ElonginC, as two highly conserved Cys residues outside the SOCS box were required to interact with Cul5 but not ElonginC. Therefore, selective assembly with Cul5 versus Cul2 E3 may require protein interfaces besides the SOCS-box-ElonginC interaction.

Keywords

Footnotes

  • Article and publication are at http://www.genesdev.org/cgi/doi/10.1101/gad.1250204.

  • 4 These authors contributed equally to this work.

  • 5 Corresponding author. E-MAIL xfyu{at}jhsph.edu; FAX (410) 614-8263.

    • Accepted September 24, 2004.
    • Received August 16, 2004.
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