Differential Contributions of Ubiquitin-Modified APOBEC3G Lysine Residues to HIV-1 Vif-Induced Degradation
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- 作者：Tiffany Turner1 ; Qiujia Shao1 ; Weiran Wang1 ; 2 ; Yudi Wang1 ; Chenliang Wang1 ; Ballington Kinlock1 ; Bindong Liu1 ; bliu@mmc.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：A3G ; apolipoprotein B mRNA-editing enzyme-catalytic polypeptide-like 3G ; HAA3G20R ; lysine-free A3G mutant ; CHX ; cycloheximide ; CHX ; cycloheximide ; MAGI ; multinuclear activation of a galactosidase indicator
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：28 August 2016
- 年：2016
- 卷：428
- 期：17
- 页码：3529-3539
- 全文大小：953 K
文摘
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K48 linked polyubiquitination is essential for Vif-induced A3G degradation
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A3G lysine residues 297, 301, 303, and 334 were not sufficient to render A3G sensitive to Vif- mediated degradation.
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Ubiquitin-modified A3G lysine residues contribute differently to HIV-1 Vif-induced A3G degradation.
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Ubiquitin modification occurs on lysine residues interspersed throughout A3G.