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Histone Acetylation Inhibits RSC and Stabilizes the +1 Nucleosome.

ABSTRACT: The +1 nucleosome of yeast genes, within which reside transcription start sites, is characterized by histone acetylation, by the displacement of an H2A-H2B dimer, and by a persistent association with the RSC chromatin-remodeling complex. Here we demonstrate the interrelationship of these characteristics and the conversion of a nucleosome to the +1 state in vitro. Contrary to expectation, acetylation performs an inhibitory role, preventing the removal of a nucleosome by RSC. Inhibition is due to both enhanced RSC-histone interaction and diminished histone-chaperone interaction. Acetylation does not prevent all RSC activity, because stably bound RSC removes an H2A-H2B dimer on a timescale of seconds in an irreversible manner.

SUBMITTER: Lorch Y

PROVIDER: S-EPMC6290470 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature

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Histone Acetylation Inhibits RSC and Stabilizes the +1 Nucleosome.

Lorch Yahli Y Maier-Davis Barbara B Kornberg Roger D RD

Molecular cell 20181025 3

The +1 nucleosome of yeast genes, within which reside transcription start sites, is characterized by histone acetylation, by the displacement of an H2A-H2B dimer, and by a persistent association with the RSC chromatin-remodeling complex. Here we demonstrate the interrelationship of these characteristics and the conversion of a nucleosome to the +1 state in vitro. Contrary to expectation, acetylation performs an inhibitory role, preventing the removal of a nucleosome by RSC. Inhibition is due to ...[more]

PMID: 30401433

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