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Stabilization of Nucleosomes by Histone Tails and by FACT Revealed by spFRET Microscopy

机译：spFRET显微镜揭示组蛋白尾巴和FACT对核小体的稳定作用

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A correct chromatin structure is important for cell viability and is tightly regulated by numerous factors. Human protein complex FACT (facilitates chromatin transcription) is an essential factor involved in chromatin transcription and cancer development. Here FACT-dependent changes in the structure of single nucleosomes were studied with single-particle F?rster resonance energy transfer (spFRET) microscopy using nucleosomes labeled with a donor-acceptor pair of fluorophores, which were attached to the adjacent gyres of DNA near the contact between H2A-H2B dimers. Human FACT and its version without the C-terminal domain (CTD) and the high mobility group (HMG) domain of the structure-specific recognition protein 1 (SSRP1) subunit did not change the structure of the nucleosomes, while FACT without the acidic C-terminal domains of the suppressor of Ty 16 (Spt16) and the SSRP1 subunits caused nucleosome aggregation. Proteolytic removal of histone tails significantly disturbed the nucleosome structure, inducing partial unwrapping of nucleosomal DNA. Human FACT reduced DNA unwrapping and stabilized the structure of tailless nucleosomes. CTD and/or HMG domains of SSRP1 are required for this FACT activity. In contrast, previously it has been shown that yeast FACT unfolds (reorganizes) nucleosomes using the CTD domain of SSRP1-like Pol I-binding protein 3 subunit (Pob3). Thus, yeast and human FACT complexes likely utilize the same domains for nucleosome reorganization and stabilization, respectively, and these processes are mechanistically similar.
机译：正确的染色质结构对于细胞生存力很重要，并受到众多因素的严格调控。人蛋白复合物FACT（促进染色质转录）是参与染色质转录和癌症发展的重要因素。在这里，通过单粒子F？ster共振能量转移（spFRET）显微镜研究了FACT依赖的单核小体结构的变化，该方法使用了标记有供体-受体对荧光团的核小体，该小体附着在DNA的邻近回旋体附近。 H2A-H2B二聚体之间的接触。人FACT及其不含C端结构域（CTD）和高迁移率基团（HMG）结构特异性识别蛋白1（SSRP1）亚基的版本不会改变核小体的结构，而FACT不具有酸性C Ty 16（Spt16）和SSRP1亚基的抑制剂的末端结构域导致核小体聚集。蛋白组蛋白尾巴的蛋白水解去除显着干扰了核小体的结构，诱导了核小体DNA的部分解缠。人类FACT可以减少DNA的解缠并稳定无尾核小体的结构。此FACT活动需要SSRP1的CTD和/或HMG域。相反，以前已经表明，酵母FACT使用SSRP1样Pol I结合蛋白3亚基（Pob3）的CTD域展开（重组）核小体。因此，酵母和人FACT复合物可能分别利用相同的域进行核小体的重组和稳定，并且这些过程在机理上相似。

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