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- W2040109903 abstract "Centromere protein A (CENP-A) is a histone H3 variant that specifies centromere location, but the histone composition and stoichiometry of CENP-A nucleosomes have been controversial. ChIP-seq and biochemical analyses of in vitro–reconstituted CENP-A nucleosomes now demonstrate that the predominant form at functional centromeres is an octamer with loose DNA ends. 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." @default.
- W2040109903 created "2016-06-24" @default.
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- W2040109903 date "2013-05-05" @default.
- W2040109903 modified "2023-10-11" @default.
- W2040109903 title "The octamer is the major form of CENP-A nucleosomes at human centromeres" @default.
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- W2040109903 doi "https://doi.org/10.1038/nsmb.2562" @default.
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