Chemical approaches for studying histone modifications.
Histones form the protein core around which genomic DNA is wrapped in eukaryotic chromatin. Numerous genetic studies have established that the structure and transcriptional state of chromatin are closely related to histone post-translational modifications. Further elucidation of the precise mechanistic roles for individual histone modifications requires the ability to isolate and study homogeneously modified histones. However, the highly heterogeneous nature of histone modifications in vivo poses a significant challenge for such studies. Chemical tools that have enabled biochemical and biophysical studies of site-specifically modified histones are the focus of this minireview.
Laboratory of Synthetic Protein Chemistry, The Rockefeller University, New York, New York 10065, USA.
Champak
C
Chatterjee
Tom W
TW
Muir
D000595:Amino Acid Sequence; D000818:Animals; D001671:Biochemistry / Q000379:methods; D001703:Biophysics / Q000379:methods; D019921:Biotinylation; D002843:Chromatin / Q000737:chemistry; D006657:Histones / Q000737:chemistry*; D006801:Humans; D008954:Models, Biological; D008956:Models, Chemical; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D009707:Nucleosomes / Q000737:chemistry; D010455:Peptides / Q000737:chemistry; D011499:Protein Processing, Post-Translational
D002843:Chromatin; D006657:Histones; D009707:Nucleosomes; D010455:Peptides