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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The Fact Spt16 'peptidase' Domain Is A Histone H3-h4 Binding Module
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The Fact Spt16 'peptidase' Domain Is A Histone H3-h4 Binding Module

机译：事实Spt16'肽酶'域是组蛋白H3-h4绑定模块。

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摘要

The FACT complex is a conserved cofactor for RNA polymerase II elongation through nucleosomes. FACT bears histone chaperone activity and contributes to chromatin integrity. However, the molecular mechanisms behind FACT function remain elusive. Here we report biochemical, structural, and mutational analyses that identify the peptidase homology domain of the Schizosaccharo-myces pombe FACT large subunit Spt16 (Spt16-N) as a binding module for histones H3 and H4. The 2.1-A crystal structure of Spt16-N reveals an aminopeptidase P fold whose enzymatic activity has been lost. Instead, the highly conserved fold directly binds histones H3-H4 through a tight interaction with their globular core domains, as well as with their N-terminal tails. Mutations within a conserved surface pocket in Spt16-N or posttranslational modification of the histone H4 tail reduce interaction in vitro, whereas the globular domains of H3-H4 and the H3 tail bind distinct Spt16-N surfaces. Our analysis suggests that the N-terminal domain of Spt16 may add to the known H2A-H2B chaperone activity of FACT by including a H3-H4 tail and H3-H4 core binding function mediated by the N terminus of Spt16. We suggest that these interactions may aid FACT-mediated nucleosome reorganization events.
机译：FACT复合物是通过核小体进行RNA聚合酶II延伸的保守辅助因子。 FACT具有组蛋白伴侣活性并有助于染色质完整性。但是，FACT功能背后的分子机制仍然难以捉摸。在这里，我们报告生化，结构和突变分析，确定裂殖酵母-粟酒裂殖酵母FACT大亚基Spt16（Spt16-N）的肽酶同源结构域作为组蛋白H3和H4的绑定模块。 Spt16-N的2.1-A晶体结构揭示了一种氨肽酶P折叠，其酶活性已经丧失。相反，高度保守的折叠通过与其球状核心结构域及其N末端尾部的紧密相互作用，直接结合组蛋白H3-H4。 Spt16-N保守表面口袋内的突变或组蛋白H4尾部的翻译后修饰会降低体外的相互作用，而H3-H4和H3尾部的球状结构域则结合不同的Spt16-N表面。我们的分析表明，Spt16的N末端结构域可通过包含由Spt16的N端介导的H3-H4尾部和H3-H4核心结合功能，增加FACT已知的H2A-H2B伴侣活性。我们建议这些相互作用可能有助于FACT介导的核小体重组事件。

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