| Literature DB >> 25954010 |
Samantha J Falk1, Lucie Y Guo2, Nikolina Sekulic3, Evan M Smoak4, Tomoyasu Mani2, Glennis A Logsdon2, Kushol Gupta3, Lars E T Jansen5, Gregory D Van Duyne2, Sergei A Vinogradov2, Michael A Lampson6, Ben E Black7.
Abstract
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.Entities:
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Year: 2015 PMID: 25954010 PMCID: PMC4610723 DOI: 10.1126/science.1259308
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728