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- Title
Structural determinants for generating centromeric chromatin.
- Authors
Black, Ben E; Foltz, Daniel R; Chakravarthy, Srinivas; Luger, Karolin; Woods, Virgil L, Jr; Cleveland, Don W
- Abstract
Mammalian centromeres are not defined by a consensus DNA sequence. In all eukaryotes a hallmark of functional centromeres--both normal ones and those formed aberrantly at atypical loci--is the accumulation of centromere protein A (CENP-A), a histone variant that replaces H3 in centromeric nucleosomes. Here we show using deuterium exchange/mass spectrometry coupled with hydrodynamic measures that CENP-A and histone H4 form sub-nucleosomal tetramers that are more compact and conformationally more rigid than the corresponding tetramers of histones H3 and H4. Substitution into histone H3 of the domain of CENP-A responsible for compaction is sufficient to direct it to centromeres. Thus, the centromere-targeting domain of CENP-A confers a unique structural rigidity to the nucleosomes into which it assembles, and is likely to have a role in maintaining centromere identity.
- Publication
Nature, 2004, Vol 430, Issue 6999, p578
- ISSN
1476-4687
- Publication type
Journal Article
- DOI
10.1038/nature02766