Open AccessTopography of histone H3–H4 interaction with the Hat1–Hat2 acetyltransferase complex
Author(s) -
Ye Yue,
Wu Yang,
Lin Zhang,
Chao-Pei Liu,
Rui-Ming Xu
Publication year - 2022
Publication title -
genes and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.136
H-Index - 438
eISSN - 1549-5477
pISSN - 0890-9369
DOI - 10.1101/gad.349099.121
Subject(s) - biology , histone acetyltransferase , histone code , histone , histone h4 , histone h3 , chromatin , histone h2a , histone h1 , histone methyltransferase , chaperone (clinical) , microbiology and biotechnology , genetics , nucleosome , dna , medicine , pathology
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.