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首页> 外文期刊>Nature >Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade.
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Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade.

机译：蛋白质泛素化涉及E1-E2-E3酶泛素硫酯级联反应。

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摘要

Ubiquitination of proteins involves the concerted action of the E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzymes and E3 ubiquitin-protein ligases. It has been proposed that E3s function as 'docking proteins', specifically binding substrate proteins and specific E2s, and that ubiquitin is then transferred directly from E2s to substrates. We show here that formation of a ubiquitin thioester on E6-AP, an E3 involved in the human papillomavirus E6-induced ubiquitination of p53 (refs 6-10), is an intermediate step in E6-AP-dependent ubiquitination. The order of ubiquitin transfer is from E1 to E2, from E2 to E6-AP, and finally from E6-AP to a substrate. This cascade of ubiquitin thioester complexes suggests that E3s have a defined enzymatic activity and do not function simply as docking proteins. The cysteine residue of E6-AP responsible for ubiquitin thioester formation was mapped to a region that is highly conserved among several proteins of unknown function, suggesting that these proteinsshare the ability to form thioesters with ubiquitin.
机译：蛋白质的泛素化涉及E1泛素激活酶，E2泛素缀合酶和E3泛素蛋白连接酶的协同作用。已经提出E3s起“对接蛋白”的作用，特别是结合底物蛋白和特异性E2s，然后泛素直接从E2s转移到底物上。我们在此处显示，在E6-AP（参与人乳头瘤病毒E6诱导的p53泛素化（参考文献6-10））的E3上，泛素硫酯的形成是E6-AP依赖性泛素化的中间步骤。泛素转移的顺序是从E1到E2，从E2到E6-AP，最后是从E6-AP到底物。泛素硫酯复合物的级联反应表明E3具有确定的酶活性，不能简单地用作对接蛋白。负责泛素硫酯形成的E6-AP的半胱氨酸残基被定位到功能未知的几种蛋白质中高度保守的区域，这表明这些蛋白质具有与泛素形成硫酯的能力。

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