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首页> 外文期刊>Journal of Molecular Biology >Structure and Function of the RING Domains of RNF20 and RNF40, Dimeric E3 Ligases that Monoubiquitylate Histone H2B
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Structure and Function of the RING Domains of RNF20 and RNF40, Dimeric E3 Ligases that Monoubiquitylate Histone H2B

机译：单泛素化组蛋白H2B的RNF20和RNF40，二聚E3甘氨酸的RING域的结构和功能

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摘要

Monoubiquitylation of histone H2B is a post-translational mark that plays key roles in regulation of transcription and genome stability. In humans, attachment of ubiquitin to lysine 120 of histone H2B depends on the activity of the E2 ubiquitin-conjugating enzyme, Ube2B, and the really interesting new gene (RING) E3 ligases, RING finger protein (RNF) 20 and RNF40. To better understand the molecular basis of this modification, we have solved the crystal structure of the RNF20 RING domain and show that it is a homodimer that specifically interacts with the Ube2B similar to Ub conjugate. By mutating residues at the E3-E2 and E3-ubiquitin interfaces, we identify key contacts required for interaction of the RNF20 RING domain with the Ube2B similar to Ub conjugate. These mutants were used to generate a structure-based model of the RNF20-Ube2B similar to Ub complex that reveals differences from other RING-E2 similar to Ub complexes, and suggests how the RNF20-Ube2B similar to Ub complex might interact with its nucleosomal substrate. Additionally, we show that the RING domains of RNF20 and RNF40 can form a stable heterodimer that is active. Together, our studies provide new insights into the mechanisms that regulate RNF20-mediated ubiquitin transfer from Ube2B. (C) 2016 Elsevier Ltd. All rights reserved.
机译：组蛋白H2B的单泛素化是翻译后标记，在转录和基因组稳定性的调节中起关键作用。在人类中，泛素与组蛋白H2B赖氨酸120的结合取决于E2泛素结合酶Ube2B的活性，以及​​真正有趣的新基因（RING）E3连接酶，RING指蛋白（RNF）20和RNF40。为了更好地了解这种修饰的分子基础，我们已经解决了RNF20 RING域的晶体结构，并表明它是同Ub2B特异性相互作用的同源二聚体，类似于Ub共轭物。通过突变E3-E2和E3-泛素界面上的残基，我们确定了类似于Ub共轭物的RNF20 RING域与Ube2B相互作用所需的关键接触。这些突变体被用于生成类似于Ub复合物的RNF20-Ube2B的基于结构的模型，该模型揭示了与类似于Ub复合物的其他RING-E2的差异，并暗示了类似于Ub复合物的RNF20-Ube2B可能如何与其核小体底物相互作用。此外，我们显示RNF20和RNF40的RING域可以形成一个稳定的有活性的异二聚体。总之，我们的研究为调节RNF20介导的从Ube2B泛素转移的机制提供了新见解。 （C）2016 Elsevier Ltd.保留所有权利。

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