CENP-C reshapes and stabilizes CENP-A nucleosomes at the centromere

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...

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Published in: Science (American Association for the Advancement of Science) Vol. 348; no. 6235; pp. 699 - 703
Main Authors: Falk, S. J, Guo, L. Y, Sekulic, N, Smoak, E. M, Mani, T, Logsdon, G. A, Gupta, K, Jansen, L. E. T, Van Duyne, G. D, Vinogradov, S. A, Lampson, M. A, Black, B. E
Format: Journal Article
Language: English
Published: American Association for the Advancement of Science 05-08-2015
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Summary: 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.
Bibliography: These authors contributed equally to this work
ISSN: 0036-8075
1095-9203
DOI: 10.1126/science.1259308