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

In this study, Yue et al. present the structure of the Hat1-Hat2 acetyltransferase complex bound to Asf1-H3-H4, which 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 extend our knowledge of histone-protein interaction and implicate a function of Hat2/RbAp46/48 in the passing of histones between chaperones. 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.

Automated summary

The study reveals the interaction between H3, H4, Hat1, and Hat2 in the Hat1-Hat2 acetyltransferase complex bound to Asf1-H3-H4. The findings expand our knowledge of histone-protein interaction and suggest a potential role of Hat2/RbAp46/48 in histone transfer.