1. A short guide to histone deacetylases including recent progress on class II enzymes
- Author
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Jeong-Sun Kim and Suk-Youl Park
- Subjects
Clinical Biochemistry ,lcsh:Medicine ,Gene Expression ,Review Article ,Biochemistry ,Histone Deacetylases ,lcsh:Biochemistry ,Histones ,chemistry.chemical_compound ,Transcription (biology) ,Gene expression ,Gene silencing ,Humans ,lcsh:QD415-436 ,Protein folding ,Molecular Biology ,Polymerase ,Histone Acetyltransferases ,biology ,lcsh:R ,Acetylation ,DNA ,DNA-Directed RNA Polymerases ,Chromatin ,Cell biology ,Histone ,chemistry ,biology.protein ,Molecular Medicine - Abstract
The interaction between histones and DNA is important for eukaryotic gene expression. A loose interaction caused, for example, by the neutralization of a positive charge on the histone surface by acetylation, induces a less compact chromatin structure, resulting in feasible accessibility of RNA polymerase and increased gene expression. In contrast, the formation of a tight chromatin structure due to the deacetylation of histone lysine residues on the surface by histone deacetylases enforces the interaction between the histones and DNA, which minimizes the chance of RNA polymerases contacting DNA, resulting in decreased gene expression. Therefore, the balance of the acetylation of histones mediated by histone acetylases (HATs) and histone deacetylases (HDACs) is an issue of transcription that has long been studied in relation to posttranslational modification. In this review, current knowledge of HDACs is briefly described with an emphasis on recent progress in research on HDACs, especially on class IIa HDACs., Cancer: Loosening DNA–Protein interactions Targeting specific structural and functional features of enzymes involved in regulating the interactions between DNA and the histone proteins associated with it could lead to the development of more effective cancer therapeutics. Histone deacetylases (HDACs), enzymes which remove acetyl groups from histones, make the histones wrap more tightly around the DNA so that it becomes inaccessible to the initial steps in gene expression. Drugs that target these enzymes have shown limited efficacy due to lack of specificity and off-target toxicity. Jeong-Sun Kim at Chonnam National University, Gwangju, and Suk-Youl Park at Pohang Accelerator Laboratory, Pohang University of Science and Technology, South Korea, review the latest knowledge about class II HDACs. They suggest that their unique structural features and low enzymatic activity are important features to consider when designing new, more selective HDAC inhibitors.
- Published
- 2020