期刊
SCIENCE
卷 348, 期 6235, 页码 699-703出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1259308
关键词
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资金
- NIH [GM082989, CA186430, GM008275, GM008216, GM007229]
- European Research Council [ERC-2013-CoG-615638]
- American Heart Association
- American Cancer Society
- NSF [DMR-0944772]
Inheritance of each chromosome depends upon its centromere. A histone H3 variant, centromere protein A (CENP-A), is essential for epigenetically marking centromere location. We find that CENP-A is quantitatively retained at the centromere upon which it is initially assembled. CENP-C binds to CENP-A nucleosomes and is a prime candidate to stabilize centromeric chromatin. Using purified components, we find that CENP-C reshapes the octameric histone core of CENP-A nucleosomes, rigidifies both surface and internal nucleosome structure, and modulates terminal DNA to match the loose wrap that is found on native CENP-A nucleosomes at functional human centromeres. Thus, CENP-C affects nucleosome shape and dynamics in a manner analogous to allosteric regulation of enzymes. CENP-C depletion leads to rapid removal of CENP-A from centromeres, indicating their collaboration in maintaining centromere identity.
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