Topography of histone H3-H4 interaction with the Hat1-Hat2 acetyltransferase complex [Research Communications]

Ye Yue1,2,4, Wen-Si Yang1,4, Lin Zhang1,3, Chao-Pei Liu1 and Rui-Ming Xu1,2 1National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China; 2University of Chinese Academy of Sciences, Beijing 100049, China Corresponding authors: rmxuibp.ac.cn

4 These authors contributed equally to this work.

3 Present address: Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, CA 94720, USA.

Abstract

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.

Received October 10, 2021. Accepted March 14, 2022.

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