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

Authors
  • Antczak, Andrew J1
  • Tsubota, Toshiaki2
  • Kaufman, Paul D2
  • Berger, James M1
  • 1 University of California, Department of Molecular and Cell Biology, Berkeley, California, 94720, USA , Berkeley
  • 2 University of Massachusetts Medical School, Program in Gene Function and Expression, Worcester, Massachusetts, 01605, USA , Worcester
Type
Published Article
Journal
BMC Structural Biology
Publisher
Springer (Biomed Central Ltd.)
Publication Date
Dec 13, 2006
Volume
6
Issue
1
Identifiers
DOI: 10.1186/1472-6807-6-26
Source
Springer Nature
Keywords
License
Yellow

Abstract

BackgroundThe 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.ResultsHere 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.ConclusionThese data clarify how Asf1 regulates histone stoichiometry to modulate epigenetic inheritance. The structure further suggests a physical model in which Asf1 contributes to interpretation of a "histone H3 barcode" for sorting H3 isoforms into different deposition pathways.

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