Histone acetylation and the maintenance of chromatin compaction by Polycomb repressive complexes

• Published in: Cold Spring Harbor Symposia on Quantitative Biology Vol. 75; p. 71
• Main Authors: Eskeland, R, Freyer, E, Leeb, M, Wutz, A, Bickmore, W A
• Format: Journal Article
• Language: English
• Published: United States 2010
• Subjects: Acetylation - drug effects; Animals; Chromatin - metabolism; Chromatin Immunoprecipitation; Embryonic Stem Cells - metabolism; Genetic Loci - genetics; Histones - metabolism; Homeodomain Proteins - genetics; Hydroxamic Acids - pharmacology; Mice; Mutation - genetics; Polycomb Repressive Complex 1; Polycomb-Group Proteins; Promoter Regions, Genetic - genetics; Repressor Proteins - deficiency; Repressor Proteins - metabolism; Transcription, Genetic - drug effects; Ubiquitin-Protein Ligases; Ubiquitination - drug effects
• ISSN: 1943-4456
• DOI: 10.1101/sqb.2010.75.053

Mechanisms controlling higher-order chromatin structure or chromatin compaction and linking this to gene regulation are poorly understood. Previously, we had shown that the PRC1 Polycomb repressive complex is required to maintain a compact chromatin state at Polycomb target loci in embryonic stem cells (ESCs) of the mouse and that this activity, together with the ability to repress target gene expression, is surprisingly independent of the histone ubiquitination activity of the Ring1B component of PRC1. Here we investigate and discuss the role of another histone modification--histone acetylation--in Polycomb function. We show that inhibition of histone deacetylases leads to some decompaction of Hox loci and suggest that histone deacetylation has a role in the pathway of PRC1-mediated chromatin compaction. We discuss whether PRC1 and histone hypoacetylation function together to establish a chromatin template at which stable nucleosomes act to antagonize transcriptional elongation.