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

Yunkai Yu, Zuoxiang Xiao, Elana S. Ehrlich, Xianghui Yu, Xiao Fang Yu

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)2867-2872
Number of pages6
JournalGenes & development
Volume18
Issue number23
DOIs
StatePublished - Dec 1 2004

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Ubiquitin-Protein Ligases
Cysteine
HIV-1
Viral DNA
Alanine
Proteins

Keywords

  • APOBEC3G
  • Cul5
  • E3 ubiquitin ligase
  • ElonginC
  • HIV-1 Vif
  • SOCS box

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

Cite this

Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines. / Yu, Yunkai; Xiao, Zuoxiang; Ehrlich, Elana S.; Yu, Xianghui; Yu, Xiao Fang.

In: Genes & development, Vol. 18, No. 23, 01.12.2004, p. 2867-2872.

Research output: Contribution to journalArticle

Yu, Yunkai ; Xiao, Zuoxiang ; Ehrlich, Elana S. ; Yu, Xianghui ; Yu, Xiao Fang. / Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines. In: Genes & development. 2004 ; Vol. 18, No. 23. pp. 2867-2872.
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AU - Yu, Xiao Fang

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AB - 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.

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