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    Biochemistry. 2005 Oct 25;44(42):13673-82.

    ASF1 binds to a heterodimer of histones H3 and H4: a two-step mechanism for the assembly of the H3-H4 heterotetramer on DNA.

    English CM, Maluf NK, Tripet B, Churchill ME, Tyler JK.

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    Department of Biochemistry and Molecular Genetics, University of Colorado Health Sciences Center at Fitzsimons, Aurora, Colorado 80045, USA.

    Abstract

    The first step in the formation of the nucleosome is commonly assumed to be the deposition of a histone H3-H4 heterotetramer onto DNA. Antisilencing function 1 (ASF1) is a major histone H3-H4 chaperone that deposits histones H3 and H4 onto DNA. With a goal of understanding the mechanism of deposition of histones H3 and H4 onto DNA, we have determined the stoichiometry of the Asf1-H3-H4 complex. We have established that a single molecule of Asf1 binds to an H3-H4 heterodimer using gel filtration, amino acid, reversed-phase chromatography, and analytical ultracentrifugation analyses. We demonstrate that Asf1 blocks formation of the H3-H4 heterotetramer by a mechanism that likely involves occlusion of the H3-H3 dimerization interface.

    PMID:
    16229457
    [PubMed - indexed for MEDLINE]

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