期刊
BIOCHEMISTRY
卷 44, 期 42, 页码 13673-13682出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi051333h
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资金
- NIGMS NIH HHS [R01 GM079154, R01 GM064475, GM64475, R01 GM079154-01A1] Funding Source: Medline
The first step in the formation of the nucleosome is commonly assumed to be the deposition of a histone H3-H4 heterotetramer onto DNA. Anti silencing function I (ASF1) is a major historic 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.
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