30 nm Chromatin Fibre Decompaction Requires both H4-K16 Acetylation and Linker Histone Eviction

Philip J.J. Robinson, Woojin An, Andrew Routh, Fabrizio Martino, Lynda Chapman, Robert G. Roeder, Daniela Rhodes

Research output: Contribution to journalArticle

211 Scopus citations

Abstract

The mechanism by which chromatin is decondensed to permit access to DNA is largely unknown. Here, using a model nucleosome array reconstituted from recombinant histone octamers, we have defined the relative contribution of the individual histone octamer N-terminal tails as well as the effect of a targeted histone tail acetylation on the compaction state of the 30 nm chromatin fiber. This study goes beyond previous studies as it is based on a nucleosome array that is very long (61 nucleosomes) and contains a stoichiometric concentration of bound linker histone, which is essential for the formation of the 30 nm chromatin fiber. We find that compaction is regulated in two steps: Introduction of H4 acetylated to 30% on K16 inhibits compaction to a greater degree than deletion of the H4 N-terminal tail. Further decompaction is achieved by removal of the linker histone.

Original languageEnglish (US)
Pages (from-to)816-825
Number of pages10
JournalJournal of Molecular Biology
Volume381
Issue number4
DOIs
StatePublished - Sep 12 2008
Externally publishedYes

Keywords

  • 30 nm fibre
  • MOF
  • chromatin
  • histone acetylation
  • linker histone

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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