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Proc Natl Acad Sci U S A. 2007 Mar 20;104(12):5008-13. Epub 2007 Mar 13.

An epigenetic mark generated by the incorporation of CENP-A into centromeric nucleosomes.

Author information

  • 1Ludwig Institute for Cancer Research, University of California at San Diego, La Jolla, CA 92093, USA.

Abstract

Mammalian centromeres are defined epigenetically. Although the physical nature of the epigenetic mark is unknown, nucleosomes in which CENP-A replaces histone H3 are at the foundation of centromeric chromatin. Hydrogen/deuterium exchange MS is now used to show that assembly into nucleosomes imposes stringent conformational constraints, reducing solvent accessibility in almost all histone regions by >3 orders of magnitude. Despite this, nucleosomes assembled with CENP-A are substantially more conformationally rigid than those assembled with histone H3 independent of DNA template. Substitution of the CENP-A centromere targeting domain into histone H3 to convert it into a centromere-targeted histone that can functionally replace CENP-A in centromere maintenance generates the same more rigid nucleosome, as does CENP-A. Thus, the targeting information directing CENP-A deposition at the centromere produces a structurally distinct nucleosome, supporting a CENP-A-driven self-assembly mechanism that mediates maintenance of centromere identity.

PMID:
17360341
[PubMed - indexed for MEDLINE]
PMCID:
PMC1829255
Free PMC Article

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