Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics |
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| Authors: | Andrew J Antczak Toshiaki Tsubota Paul D Kaufman and James M Berger |
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| Institution: | (1) Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA;(2) Program in Gene Function and Expression, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA |
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| Abstract: | 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. |
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