| Literature DB >> 17070031 |
Jean-François Couture1, Raymond C Trievel.
Abstract
Histone-modifying enzymes catalyze a diverse array of post-translational modifications of core and linker histones within chromatin. These modifications govern a multitude of genomic functions, particularly gene expression, and are believed to constitute an epigenetic code. Histone-modifying enzymes inscribe this code by catalyzing site-selective modifications, which are subsequently interpreted by effector proteins that recognize specific covalent marks. The substrate specificity of these enzymes is of fundamental biological importance because it underpins this epigenetic code. Recently, the structural basis of this specificity has been examined with regards to recently determined structures of GCN5 acetyltransferases and SET domain methyltransferases in complex with their cognate histone substrates.Entities:
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Year: 2006 PMID: 17070031 DOI: 10.1016/j.sbi.2006.10.002
Source DB: PubMed Journal: Curr Opin Struct Biol ISSN: 0959-440X Impact factor: 6.809