Structural determinants for generating centromeric chromatin

Ben E. Black, Daniel R. Foliz, Srinivas Chakravarthy, Karolin Luger, Virgil L. Woods, Don W. Cleveland*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

302 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)578-582
Number of pages5
JournalNature
Volume430
Issue number6999
DOIs
StatePublished - Jul 29 2004

ASJC Scopus subject areas

  • General

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