A key event in the regulation of eukaryotic gene expression is the posttranslational modification of nucleosomal histones, which converts regions of chromosomes into transcriptionally active or inactive chromatin. The most well studied posttranslational modification of histones is the acetylation of
A shifting paradigm: histone deacetylases and transcriptional activation
✍ Scribed by Catharine L. Smith
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 315 KB
- Volume
- 30
- Category
- Article
- ISSN
- 0265-9247
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✦ Synopsis
Abstract
Transcriptional repression and silencing have been strongly associated with hypoacetylation of histones. Accordingly, histone deacetylases, which remove acetyl groups from histones, have been shown to participate in mechanisms of transcriptional repression. Therefore, current models of the role of acetylation in transcriptional regulation focus on the acetylation status of histones and designate histone acetyltransferases, which add acetyl groups to histones, as transcriptional coactivators and histone deacetylases as corepressors. In recent years, an accumulation of studies have shown that these enzymes also target non‐histone proteins and that histone deacetylases have clear roles as coactivators at a variety of genes, some of which are key regulators of cell growth and survival. This review summarizes the evidence for histone deacetylases as coactivators and provides models of coactivation mechanisms, some of which integrate roles of acetylated histones and non‐histone proteins in transcription. BioEssays 30:15–24, 2008. © 2007 Wiley Periodicals, Inc.
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