Ubch9 conjugates SUMO but not ubiquitin
Ubch9 conjugates SUMO but not ubiquitin
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DOI：
10.1016/s0014-5793(97)01305-7
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发表时间：
1997-11-17
期刊：
影响因子：
3.5
通讯作者：
Hay, RT
中科院分区：
文献类型：
--
作者：
Desterro, JMP;Thomson, J;Hay, RT
泛素结合酶参与导致蛋白质泛素化的硫酯级联反应，虽然Ubc 9与E2泛素结合酶同源，但我们已经证明它不能与泛素形成硫酯，但可以与小泛素样蛋白SUMO形成硫酯。因此，Ubc9是SUMO缀合酶而不是泛素缀合酶。SUMO对Ubc9的转乙酰化不是由E1泛素活化酶介导的，而是由不同的酶活性介导的。SUMO与靶蛋白的缀合是由与泛素化不同但平行的途径介导的。(C)1997年欧洲生物化学学会联合会。
Ubiquitin conjugating enzymes participate in the thioester cascade that leads to protein ubiquitination, Although Ubc9 is homologous to E2 ubiquitin conjugating enzymes we have shown that it is unable to form a thioester with ubiquitin, but can form a thioester with the small ubiquitin-like protein SUMO. Thus Ubc9 is a SUMO conjugating enzyme rather than a ubiquitin conjugating enzyme, Transacetylation of Ubc9 by SUMO is not mediated by the E1 ubiquitin activating enzyme, but by a distinct enzymatic activity, SUMO conjugation to target proteins is mediated by a different, but parallel pathway to ubiquitination. (C) 1997 Federation of European Biochemical Societies.