H2B ubiquitination: Conserved molecular mechanism, diverse physiologic functions of the E3 ligase during meiosis
H2B ubiquitination: Conserved molecular mechanism, diverse physiologic functions of the E3 ligase during meiosis
复制标题
H2B 泛素化：减数分裂过程中 E3 连接酶的保守分子机制和多样化生理功能
DOI：
10.1080/19491034.2017.1330237
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发表时间：
2017-01-01
期刊：
影响因子：
3.7
通讯作者：
Li, Wei
中科院分区：
文献类型：
--
作者：
Wang, Liying;Cao, Chunwei;Li, Wei
RNF20/BRE1介导的H2B泛素化（H2BUB）具有各种生理功能。最近，我们发现H2BUB通过在减数分裂过程中促进染色质松弛来参与减数分裂重组。然后，我们分析了H2BUB的E3连接酶之间的系统发育关系，其E2 RAD6及其伴侣WW域含WW域的适配器使用盘绕型圈（WAC）或LGE1，发现H2Bub的分子机制是从酵母到哺乳动物的进化中的分子机制。但是，RNF20在不同生物体中具有多种生理功能，这可能是由于其域/基序架构的进化差异引起的。在当前的额外观点中，我们不仅阐明了H2BUB的进化保守的分子机制，而且还讨论了减数分裂过程中RNF20的不同生理功能。
ABSTRACT RNF20/Bre1 mediated H2B ubiquitination (H2Bub) has various physiologic functions. Recently, we found that H2Bub participates in meiotic recombination by promoting chromatin relaxation during meiosis. We then analyzed the phylogenetic relationships among the E3 ligase for H2Bub, its E2 Rad6 and their partner WW domain-containing adaptor with a coiled-coil (WAC) or Lge1, and found that the molecular mechanism underlying H2Bub is evolutionarily conserved from yeast to mammals. However, RNF20 has diverse physiologic functions in different organisms, which might be caused by the evolutionary divergency of their domain/motif architectures. In the current extra view, we not only elucidate the evolutionarily conserved molecular mechanism underlying H2Bub, but also discuss the diverse physiologic functions of RNF20 during meiosis.