Ubiquitination of APOBEC3 proteins by the Vif-Cullin5-ElonginB-ElonginC complex |
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Authors: | Shirakawa Kotaro Takaori-Kondo Akifumi Kobayashi Masayuki Tomonaga Mitsunori Izumi Taisuke Fukunaga Keiko Sasada Amane Abudu Aierken Miyauchi Yasuhiro Akari Hirofumi Iwai Kazuhiro Uchiyama Takashi |
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Affiliation: | Department of Hematology and Oncology, Graduate School of Medicine, Kyoto University, 54 Shogoin-Kawaracho, Sakyo-ku, Kyoto 606-8507, Japan. |
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Abstract: | APOBEC3 proteins are antiviral host factors for a wide variety of retroviruses. HIV-1 Vif overcomes the antiviral activity of APOBEC3G by ubiquitinating the protein. In this study, we examined the ability of Vif to antagonize other family members of APOBEC3 proteins, together with its mechanism. Using HIV infectivity, virion incorporation, immunoprecipitation, and in vitro ubiquitin conjugation assays, we show that the ability of Vif to inhibit antiviral activity of APOBEC3 proteins positively correlates with its ability to bind and ubiquitinate these proteins by a Vif-Cullin5-ElonginB-ElonginC (Vif-BC-Cul5) complex. These results suggest that Vif exhibits its anti-APOBEC3 activity by the ubiquitin ligase activity of the Vif-BC-Cul5 complex. |
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Keywords: | HIV-1 Cytidine deaminase Virion incorporation Ubiquitin Cullin5-ElonginB-ElonginC complex |
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