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

Jayasha Shandilya, Parijat Senapati, Fabienne Hans, Hervé Menoni, Philippe Bouvet, Stefan Dimitrov, Dimitar Angelov, Tapas K. Kundu

Research output: Contribution to journalArticle

3 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)221-227
Number of pages7
JournalJournal of Biochemistry
Volume156
Issue number4
DOIs
Publication statusPublished - 2014
Externally publishedYes

    Fingerprint

Keywords

  • Acetylation
  • CENP-A
  • Histone chaperone
  • NPM1
  • Transcription

ASJC Scopus subject areas

  • Medicine(all)
  • Biochemistry
  • Molecular Biology

Cite this