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Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics by Andrew J Antczak; Toshiaki Tsubota; Paul D Kaufman; James M Berger is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Background The histone H3/H4 chaperone Asf1 (anti-silencing function 1) is required for the establishment and maintenance of proper chromatin structure, as well as for genome stability in eukaryotes. Asf1 participates in both DNA replication-coupled (RC) and replication-independent (RI) histone deposition reactions __in vitro__ and interacts with complexes responsible for both pathways __in vivo__. Asf1 is known to directly bind histone H3, however, high-resolution structural information about the geometry of this interaction was previously unknown. ## Results Here we report the structure of a histone/histone chaperone interaction. We have solved the 2.2 Å crystal structure of the conserved N-terminal immunoglobulin fold domain of yeast Asf1 (residues 2–155) bound to the C-terminal helix of yeast histone H3 (residues 121–134). The structure defines a histone-binding patch on Asf1 consisting of both conserved and yeast-specific residues; mutation of these residues abrogates H3/H4 binding affinity. The geometry of the interaction indicates that Asf1 binds to histones H3/H4 in a manner that likely blocks sterically the H3/H3 interface of the nucleosomal four-helix bundle. ## Conclu

Who reads Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics?

Author

Andrew J Antczak; Toshiaki Tsubota; Paul D Kaufman; James M Berger

Publisher

BioMed Central; Springer (Biomed Central Ltd.); London: BioMed Central, 2001-; Springer Science and Business Media LLC (ISSN 1472-6807)

Published

2006

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)