Topography of histone H3–H4 interaction with the Hat1–Hat2 acetyltransferase complex
Ye Yue, Wen-Si Yang, Lin Zhang, Chao-Pei Liu and Rui-Ming Xu
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.
附件下载：
Topography of histone H3–H4 interaction with the Hat1–Hat2 acetyltransferase complex, Gene Dev, 7 Apr 2022
Genes & Development, 7 April, 2022, DOI：https://doi.org/10.1101/gad.349099.121
Topography of histone H3–H4 interaction with the Hat1–Hat2 acetyltransferase complex
Ye Yue, Wen-Si Yang, Lin Zhang, Chao-Pei Liu and Rui-Ming Xu
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.
文章链接：http://genesdev.cshlp.org/content/early/2022/04/05/gad.349099.121.short?rss=1
相关报道：/kyjz/zxdt/202204/t20220408_6424212.html