Currently browsing: “histone code”

Bromodomains in living cells participate in deciphering the histone code

KEYWORDS: acetylated histones • Alejandra Loyola • amino acids • Bromodomains • chromatin-associated proteins • deciphering • histone code • Interactions • N-terminal

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 […]

Facile synthesis of site-specifically acetylated and methylated histone proteins: Reagents for evaluation of the histone code hypothesis

KEYWORDS: acetylation • Alejandra Loyola • genetically encoded • H2A • H2B • H3 • H4 • histone code • histone proteins • methylation modifications • peptide synthesis

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 […]