Structural attributes in the conjugation of ubiquitin, SUMO and RUB to protein substrates
Structural attributes in the conjugation of ubiquitin, SUMO and RUB to protein substrates
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DOI：
10.2741/goet
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发表时间：
2002-08-01
影响因子：
3.1
通讯作者：
Bayer, P
中科院分区：
文献类型：
--
作者：
Goettsch, S;Bayer, P
许多细胞和分泌的蛋白质在翻译完成后被化学修饰。多肽链（修饰物）与底物蛋白质的共价连接是翻译后修饰的特殊情况。在七十年代后期，人们观察到泛素，一种小的修饰剂，标记短寿命的蛋白质被26S蛋白酶体降解。在过去的十年中，许多其他泛素相关蛋白被发现和分离。多肽链与受体分子的连接成为调节蛋白质空间和时间组织的细胞途径的常见特征。本文重点介绍了泛素、RUB和SUMO这三种修饰剂的结构以及参与这些修饰途径的相关酶。我们已经描述了这些蛋白质的同源性和差异，并指出显着的拓扑标志共同修饰共轭酶。这种表征将有助于理解这些调控途径及其在控制蛋白质命运方面的相似性和差异性，从多聚泛素化产生的蛋白质降解信号到RUB和SUMO缀合带来的功能修饰。
Many cellular and secreted proteins are chemically modified after their translation is completed. The covalent linkage of a polypeptide chain (modifier) to a substrate protein is a special case of post-translational modification. In the late seventies it was observed that ubiquitin, a small modifier, marks short-lived proteins for degradation by the 26S proteasome. Over the last decade many other ubiquitin-related proteins were discovered and isolated. Attachment of polypeptide chains onto acceptor molecules became a common feature to regulate spatially and timely organized cellular pathways of proteins. This article focuses on the structures of the three modifiers: ubiquitin, RUB and SUMO and the cognate enzymes involved in these modification pathways. We have described the homologies and differences of these proteins and indicate salient topological hallmarks common to modifier-conjugating enzymes. This characterization will help in understanding these regulatory pathways and their similarities and differences in controlling protein fate, from protein degradation signals generated by polyubiquitination to functional modification brought about by RUB and SUMO conjugation.