Histone Acetylation Inhibits RSC and Stabilizes the +1 Nucleosome
| Autor: | Yahli Lorch, Barbara Maier-Davis, Roger D. Kornberg |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Proteins Protein Conformation Dimer Saccharomyces cerevisiae Biology Chromatin remodeling Article Histones 03 medical and health sciences chemistry.chemical_compound Transcription (biology) Acetyl Coenzyme A Nucleosome Animals Chromatin structure remodeling (RSC) complex Molecular Biology Nucleosome Assembly Protein 1 Acetylation Cell Biology Chromatin Assembly and Disassembly Chromatin Nucleosomes Rats DNA-Binding Proteins 030104 developmental biology Histone chemistry biology.protein Biophysics Trans-Activators Protein Processing Post-Translational Transcription Factors |
| Popis: | Summary 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. |
| Databáze: | OpenAIRE |
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