The structure of (CENP-A–H4)2 reveals physical features that mark centromeres

Nikolina Sekulic, Emily A. Bassett, Danielle J. Rogers and Ben E. Black ()
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Nikolina Sekulic: University of Pennsylvania, School of Medicine
Emily A. Bassett: University of Pennsylvania, School of Medicine
Danielle J. Rogers: University of Pennsylvania, School of Medicine
Ben E. Black: University of Pennsylvania, School of Medicine

Nature, 2010, vol. 467, issue 7313, 347-351

Abstract: CENP-A makes its mark on centromeres The hallmark of all eukaryotic centromeres is the presence of a histone H3 variant, CENP-A, but the nature of the epigenetic centromere mark is the subject of great debate. The crystal structure of the human CENP-A–H4 complex has now been determined. It reveals the structural basis for the rigidity that CENP-A imparts to nucleosomes, as well as several surprising global and local structural alterations that have major implications for epigenetic centromere marking. CENP-A seems to alter the chromatin into which it assembles — not by switching the handedness of DNA wrapping or disrupting the octameric histone stoichiometry, but by altering nucleosome structure.

Date: 2010
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DOI: 10.1038/nature09323

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