Currently browsing: “histone code”
Bromodomains in living cells participate in deciphering the histone code
ABSTRACT: The bromodomain, a module of ~110 amino acids, is found in several chromatin-associated proteins, including histone acetyltransferases and chromatin-remodeling factors, and can bind to acetylated lysines. Such post-translational modifications occur mainly in the N-terminal tail of the histone proteins and, in combination with other modifications, are thought to participate in defining a histone code. Recent findings provide a model for how bromodomain-containing […]
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Facile synthesis of site-specifically acetylated and methylated histone proteins: Reagents for evaluation of the histone code hypothesis
ABSTRACT: The functional capacity of genetically encoded histone proteins can be powerfully expanded by posttranslational modification. A growing body of biochemical and genetic evidence clearly links the unique combinatorial patterning of side chain acetylation, methylation, and phosphorylation mainly within the highly conserved N termini of histones H2A, H2B, H3, and H4 with the regulation of gene expression and chromatin assembly […]
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