National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
University of Chinese Academy of Sciences, Beijing 100049, China.
Genes Dev. 2022 Apr 1;36(7-8):408-413. doi: 10.1101/gad.349099.121. Epub 2022 Apr 7.
Chaperones influence histone conformation and intermolecular interaction in multiprotein complexes, and the structures obtained with full-length histones often provide more accurate and comprehensive views. Here, our structure of the Hat1-Hat2 acetyltransferase complex bound to Asf1-H3-H4 shows that the core domains of H3 and H4 are involved in binding Hat1 and Hat2, and the N-terminal tail of H3 makes extensive interaction with Hat2. These findings expand the knowledge about histone-protein interaction and implicate a function of Hat2/RbAp46/48, which is a versatile histone chaperone found in many chromatin-associated complexes, in the passing of histones between chaperones.
伴侣蛋白影响多蛋白复合物中的组蛋白构象和分子间相互作用，全长组蛋白获得的结构通常提供更准确和全面的视图。在这里，我们获得了结合 Asf1-H3-H4 的 Hat1-Hat2 乙酰转移酶复合物的结构，表明 H3 和 H4 的核心结构域参与结合 Hat1 和 Hat2，H3 的 N 端尾巴与 Hat2 进行广泛的相互作用。这些发现扩展了组蛋白-蛋白质相互作用的知识，并暗示了广泛存在于许多染色质相关复合物中的多功能组蛋白伴侣 Hat2/RbAp46/48 在伴侣蛋白之间传递组蛋白的功能。
