Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 104, Issue 12, Pages 5008-5013Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0700390104
Keywords
centromere; chromatin; hydrogen exchange
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Funding
- NCI NIH HHS [CA118595, R21 CA099835, R21 CA118595, CA099835, R33 CA099835] Funding Source: Medline
- NIGMS NIH HHS [R01 GM029513, GM29513, GM074150, R01 GM074150, R37 GM029513] Funding Source: Medline
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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.
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