Currently browsing: “histone code”

Bromodomains in living cells participate in deciphering the histone code

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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 […]

Loyola A., Almouzni G. Bromodomains in living cells participate in deciphering the histone code. Trends Cell Biol. 14(6): 279-281 (2004)
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Facile synthesis of site-specifically acetylated and methylated histone proteins: Reagents for evaluation of the histone code hypothesis

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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 […]

He S., Bauman D., Davis J. S., Loyola A., Nishioka K., Gronlund J. L., Reinberg D., Meng F., Kelleher N., McCafferty D. G. Facile synthesis of site-specifically acetylated and methylated histone proteins: Reagents for evaluation of the histone code hypothesis. PNAS 100(21): 12033-12038 (2003)
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