Specific contributions of histone tails and their acetylation to the mechanical stability of nucleosomes

Brent Brower-Toland, David A. Wacker, Robert M. Fulbright, John T. Lis, W. Lee Kraus, Michelle D. Wang

Research output: Contribution to journalArticle

137 Scopus citations

Abstract

The distinct contributions of histone tails and their acetylation to nucleosomal stability were examined by mechanical disruption of individual nucleosomes in a single chromatin fiber using an optical trap. Enzymatic removal of H2A/H2B tails primarily decreased the strength of histone-DNA interactions located ∼±36 bp from the dyad axis of symmetry (off-dyad strong interactions), whereas removal of the H3/H4 tails played a greater role in regulating the total amount of DNA bound. Similarly, nucleosomes composed of histones acetylated to different degrees by the histone acetyltransferase p300 exhibited significant decreases in the off-dyad strong interactions and the total amount of DNA bound. Acetylation of H2A/H2B appears to play a particularly critical role in weakening the off-dyad strong interactions. Collectively, our results suggest that the destabilizing effects of tail acetylation may be due to elimination of specific key interactions in the nucleosome.

Original languageEnglish (US)
Pages (from-to)135-146
Number of pages12
JournalJournal of Molecular Biology
Volume346
Issue number1
DOIs
StatePublished - Feb 11 2005

Keywords

  • acetyation
  • histone tails
  • nucleosome
  • optical trapping
  • single molecule

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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