Centromeric histone variant CENP-A represses acetylation-dependent chromatin transcription that is relieved by histone chaperone NPM1

J Biochem. 2014 Oct;156(4):221-7. doi: 10.1093/jb/mvu034. Epub 2014 May 16.

Abstract

Mammalian centromeric histone H3 variant, CENP-A, is involved in maintaining the functional integrity and epigenetic inheritance of the centromere. CENP-A causes transcriptional repression of centromeric chromatin through an unknown mechanism. Here, we report that reconstituted CENP-A nucleosomes are amenable to ATP-dependent SWI/SNF-mediated remodelling but are less permissive to acetylation and acetylation-dependent in vitro chromatin transcription. Remarkably, the transcriptional repression of the CENP-A chromatinized template could be relieved by the ectopic addition of histone chaperone, nucleophosmin.

Keywords: CENP-A; NPM1; acetylation; histone chaperone; transcription.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Animals
  • Autoantigens / genetics
  • Autoantigens / metabolism*
  • Centromere / metabolism*
  • Centromere Protein A
  • Chromatin / genetics*
  • Chromatin / metabolism*
  • Chromosomal Proteins, Non-Histone / genetics
  • Chromosomal Proteins, Non-Histone / metabolism*
  • Histones / genetics
  • Histones / metabolism*
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Nucleophosmin
  • Xenopus laevis

Substances

  • Autoantigens
  • Centromere Protein A
  • Chromatin
  • Chromosomal Proteins, Non-Histone
  • Histones
  • Nuclear Proteins
  • Nucleophosmin