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

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

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

    andrew j antczakAndrew J Antczak,toshiaki tsubotaToshiaki Tsubota,paul d kaufmanPaul D Kaufman,james m bergerJames M Berger,

    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 A 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. CONCLUSION: These 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.

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

    aj antczakAJ Antczak,t tsubotaT Tsubota,pd kaufmanPD Kaufman,jm bergerJM Berger,

    For similar biological phenomena, cell phenomena, and immunity: immunity: antibody specificity: species specificity research abstracts see: biological phenomena, cell phenomena, and immunity: immunity: antibody specificity: species specificity research

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

    PUBLICATION TYPE: Research Support, U.S. Gov't,

    Journal: BMC structural biology

    VOLUME: 6

    Page Numbers: 26

    Journal Abbreviation: BMC Struct. Biol.

    ISSN: 1472-6807

    DAY: 13

    MONTH: 12

    YEAR: 2006

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

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 101088689

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

    KEYWORDS: Species Specificity

    MESH TERMS: genetics

    Chemical & Substance for Abstract: Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics. Information

    Substance Name: Silent Information Regulator Proteins, S

    Registry Number: 0

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

    AFFILIATION: Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA. antczaka@berkeley.edu <antczaka@berkeley.edu>

    Country: England

    England Research PublicationEngland Research Publication

    AGENCY: United States NCI

    GRANT: CA077373

    ACRONYM: CA

    MEDLINETA: BMC Struct Biol

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER: 2IDC

    Number Hits: 0

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