Open AccessCENP-C reshapes and stabilizes CENP-A nucleosomes at the centromere
Author(s) -
Samantha J. Falk,
Lucie Y. Guo,
Nikolina Sekulić,
Evan M. Smoak,
Tomoyasu Mani,
Glennis A. Logsdon,
Kushol Gupta,
Lars E.T. Jansen,
Gregory D. Van Duyne,
Sergei A. Vinogradov,
Michael A. Lampson,
Ben E. Black
Publication year - 2015
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.1259308
Subject(s) - centromere , nucleosome , chromatin , histone , chromosome segregation , microbiology and biotechnology , chromosome , histone h3 , biology , genetics , dna , gene
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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