Structural determinants for generating centromeric chromatin. Journal Article uri icon

Overview

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 date

  • July 29, 2004

Full Author List

  • Black BE; Foltz DR; Chakravarthy S; Luger K; Woods VL; Cleveland DW

Other Profiles

Additional Document Info

start page

  • 578

end page

  • 582

volume

  • 430

issue

  • 6999