Specific contributions of histone tails and their acetylation to the mechanical stability of nucleosomes. Academic Article uri icon

Overview

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 approximately +/-36bp 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.

publication date

  • December 22, 2004

Research

keywords

  • Histones
  • Nucleosomes

Identity

Scopus Document Identifier

  • 12344284012

Digital Object Identifier (DOI)

  • 10.1016/j.jmb.2004.11.056

PubMed ID

  • 15663933

Additional Document Info

volume

  • 346

issue

  • 1