The octamer is the major form of CENP-A nucleosomes at human centromeres

Dan Hasson, Tanya Panchenko, Kevan J. Salimian, Mishah U. Salman, Nikolina Sekulic, Alicia Alonso, Peter E. Warburton, Ben E. Black

Research output: Contribution to journalArticlepeer-review

Abstract

The centromere is the chromosomal locus that ensures fidelity in genome transmission at cell division. Centromere protein A (CENP-A) is a histone H3 variant that specifies centromere location independently of DNA sequence. Conflicting evidence has emerged regarding the histone composition and stoichiometry of CENP-A nucleosomes. Here we show that the predominant form of the CENP-A particle at human centromeres is an octameric nucleosome. CENP-A nucleosomes are very highly phased on α-satellite 171-base-pair monomers at normal centromeres and also display strong positioning at neocentromeres. At either type of functional centromere, CENP-A nucleosomes exhibit similar DNA-wrapping behavior, as do octameric CENP-A nucleosomes reconstituted with recombinant components, having looser DNA termini than those on conventional nucleosomes containing canonical histone H3. Thus, the fundamental unit of the chromatin that epigenetically specifies centromere location in mammals is an octameric nucleosome with loose termini.

Original languageEnglish (US)
Pages (from-to)687-695
Number of pages9
JournalNature Structural and Molecular Biology
Volume20
Issue number6
DOIs
StatePublished - Jun 2013
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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