Chromosomes. 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 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.

Keywords

Autoantigens Centromere Chromosomal Proteins, Non-Histone DNA Epigenesis, Genetic Fluorescence Resonance Energy Transfer Gene Knockdown Techniques Humans Nucleosomes Protein Structure, Secondary

URI

http://hdl.handle.net/10400.7/627

Citation

CENP-C reshapes and stabilizes CENP-A nucleosomes at the centromere By Samantha J. Falk, Lucie Y. Guo, Nikolina Sekulic, 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 Science08 May 2015 : 699-703