Peptide and protein chemistry have become an integral part of chromatin research. Methods ranging from solid-phase synthesis to recombinant technology are available to construct site-specifically modified histone peptides and chromatin templates with distinct patterns. Several peptide- and mononucleosome based approaches have been developed to biochemically address the enormous combinatorial possibilities of histone PTM combinations. overexpression of a histone-modifying enzyme can result in global accumulation of a desired PTM. Upon targeting enzymes to specific genomic sites, perturbations can be localized to genetic reporters, enabling more defined functional assignments of histone modifying activities. In conjunction with reversible dimerization modules, these targeting strategies can shed light on the kinetics of the formation and interpretation of histone PTMs.
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