Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines
Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines
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DOI：
10.1101/gad.1250204
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发表时间：
2004-12-01
影响因子：
10.5
通讯作者：
Yu, XF
中科院分区：
文献类型：
--
作者：
Yu, YK;Xiao, ZX;Yu, XF
APOBEC3G在新合成的病毒DNA中诱导超突变，通过cul5 - elonginb - elongine3泛素连接酶被HIV-1 Vif抑制。我们现在已经在HIV-1 Vif中描述了一个新的SOCS盒子，它介导了它与longinc的相互作用。在这个SOCS盒子中，丙氨酸取代了之前确定的SOCS盒子中的共识半胱氨酸。这个新基序对于与Cul5- elonginb -ElonginC相互作用是必要的，但还不够，因为需要在SOCS盒外的两个高度保守的Cys残基才能与Cul5而不是与ElonginC相互作用。因此，Cul5与Cul2 E3的选择性组装可能需要除了SOCS-box-ElonginC相互作用之外的蛋白质界面。
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.