Structural and biochemical analyses of the nuclear pore complex component ELYS identify residues responsible for nucleosome binding
Structural and biochemical analyses of the nuclear pore complex component ELYS identify residues responsible for nucleosome binding
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核孔复合体成分 ELYS 的结构和生化分析确定了负责核小体结合的残基
DOI：
10.1038/s42003-019-0385-7
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发表时间：
2019
影响因子：
5.9
通讯作者：
Kurumizaka Hitoshi
中科院分区：
文献类型：
--
作者：
Kobayashi Wataru;Takizawa Yoshimasa;Aihara Maya;Negishi Lumi;Ishii Hajime;Kurumizaka Hitoshi
核膜内的核孔复合体是蛋白质和RNA等大分子在细胞质和细胞核之间运输的基本结构。核孔复合体组装发生在细胞周期的有丝分裂后阶段的染色质上。ELYS(MEL-28/AHCTF1)与核小体结合，核小体是染色质的基本单位，并促进复合体在细胞染色体周围的组装。在这里，我们证明了C-末端Elys区域的Arg-Arg-Lys(RRK)延伸在核小体结合中起着至关重要的作用。冷冻-EM结构和交联质谱分析表明，Elys C-末端区域直接与核小体的酸性斑块结合。这些结果提供了对Elys-核小体相互作用的机械性见解，该相互作用促进了细胞中染色体周围有丝分裂后核孔复合体的形成。
The nuclear pore complex embedded within the nuclear envelope is the essential architecture for trafficking macromolecules, such as proteins and RNAs, between the cytoplasm and nucleus. The nuclear pore complex assembly occurs on chromatin in the post-mitotic phase of the cell cycle. ELYS (MEL-28/AHCTF1) binds to the nucleosome, which is the basic chromatin unit, and promotes assembly of the complex around the chromosomes in cells. Here we show that the Arg-Arg-Lys (RRK) stretch of the C-terminal ELYS region plays an essential role in the nucleosome binding. The cryo-EM structure and the crosslinking mass spectrometry reveal that the ELYS C-terminal region directly binds to the acidic patch of the nucleosome. These results provide mechanistic insight into the ELYS-nucleosome interaction, which promotes the post-mitotic nuclear pore complex formation around chromosomes in cells.