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Updated: Jun 24, 2026
Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
Published on: November 30, 2018
Structural and chemical basis of histone acetylation
1The Wistar Institute, Department of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
Abstract:
Histones are the predominant protein components of chromatin and are subject to a variety of specific post-translational modifications that are correlated with transcriptional competence. Among these modifications are reversible acetylation that is mediated by acetyltransferases that mediate transcriptional activation and deactylases that mediate transcriptional repression and gene silencing. Structural studies have provided important insights into the mechanism of substrate specific binding and catalysis by the enzymes that mediate reversible acetylation. In this paper I will review structural work from my laboratory on histone acetyltransferases (HATs) and the Sir2 family of histone deacetylases (HDACs), with a specific focus on catalysis and substrate-specific binding by these enzymes.
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