Topography of histone H3–H4 interaction with the Hat1–Hat2 acetyltransferase complex

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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.
Funding Information
  • Natural Science Foundation of China (91853204, 92153302, 31991162, 31521002)
  • Ministry of Science and Technology of China (2019YFA0508900, 2018YFE0203300)
  • Strategic Priority Research Program of Chinese Academy of Sciences (XDB37010101)
  • Youth Innovation Promotion Association of the CAS (2018125)

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