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Crystal structure of Hat1-Hat2-Asf1-H3-H4
Structural highlights
FunctionC562_ECOLX Electron-transport protein of unknown function.HAT1_YEAST Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of free histone H4 in the cytoplasm. The complex is also found in the nucleus, however it is not certain that it modifies histone H4 when packaged in chromatin. Histone H4 'Lys-12' acetylation is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.[1] [2] [3] [4] [5] Publication Abstract from PubMedChaperones 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. Topography of histone H3-H4 interaction with the Hat1-Hat2 acetyltransferase complex.,Yue Y, Yang WS, Zhang L, Liu CP, Xu RM Genes Dev. 2022 Apr 1;36(7-8):408-413. doi: 10.1101/gad.349099.121. Epub 2022 Apr , 7. PMID:35393344[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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