Structural basis for binding diversity of acetyltransferase p300 to the nucleosome.
Structural basis for binding diversity of acetyltransferase p300 to the nucleosome.
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DOI：
10.1016/j.isci.2022.104563
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发表时间：
2022-07-15
期刊：
影响因子：
5.8
通讯作者：
Kurumizaka, Hitoshi
中科院分区：
文献类型：
--
作者：
Hatazawa, Suguru;Liu, Jiuyang;Takizawa, Yoshimasa;Zandian, Mohamad;Negishi, Lumi;Kutateladze, Tatiana G.;Kurumizaka, Hitoshi
p300是一种与染色质相关并介导重要细胞过程的人乙酰转移酶。我们现在报告的冷冻电子显微镜结构的p300催化核心与核小体核心颗粒（NCP）的复合物。在最清晰的结构中，p300的HAT结构域和布罗莫结构域在超螺旋位置2和3处接触核小体DNA，并且HAT结构域的催化位点位于组蛋白H4的N-末端尾部附近。p300的p300-DNA界面残基的突变显著降低了与NCP的结合。另外三类p300-NCP复合物显示了p300-NCP复合物形成的不同模式。我们的数据提供的结构细节至关重要的机制，其中p300乙酰化核小体上的多个网站的理解。确定了p300-核小体复合物的冷冻电镜结构，确定了p300的HAT和布罗莫结构域中的核小体结合残基，p300以多种结合模式与核小体结合生物科学;生物化学;结构生物学
p300 is a human acetyltransferase that associates with chromatin and mediates vital cellular processes. We now report the cryo-electron microscopy structures of the p300 catalytic core in complex with the nucleosome core particle (NCP). In the most resolved structure, the HAT domain and bromodomain of p300 contact nucleosomal DNA at superhelical locations 2 and 3, and the catalytic site of the HAT domain are positioned near the N-terminal tail of histone H4. Mutations of the p300-DNA interfacial residues of p300 substantially decrease binding to NCP. Three additional classes of p300-NCP complexes show different modes of the p300-NCP complex formation. Our data provide structural details critical to our understanding of the mechanism by which p300 acetylates multiple sites on the nucleosome. The cryo-EM structures of the p300-nucleosome complexes were determined The nucleosome binding residues in the HAT and bromodomain of p300 were identified p300 binds to the nucleosome in multiple binding modes Biological sciences; Biochemistry; Structural biology
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