title: Application of mass spectrometry to the identification and quantification of histone post-translational modifications.
abstract: The core histones are the primary protein component of chromatin, which is responsible for the packaging of eukaryotic DNA. The NH(2)-terminal tail domains of the core histones are the sites of numerous post-translational modifications that have been shown to play an important role in the regulation of chromatin structure. In this study, we discuss the recent application of modern analytical techniques to the study of histone modifications. Through the use of mass spectrometry, a large number of new sites of histone modification have been identified, many of which reside outside of the NH(2)-terminal tail domains. In addition, techniques have been developed that allow mass spectrometry to be effective for the quantitation of histone post-translational modifications. Hence, the use of mass spectrometry promises to dramatically alter our view of histone post-translational modifications.
authors.affiliation: Department of Chemistry, The Ohio State University, Columbus, Ohio 43210, USA.
authors.forename: Michael A
authors.initials: MA
authors.lastname: Freitas
authors.forename: Amy R
authors.initials: AR
authors.lastname: Sklenar
authors.forename: Mark R
authors.initials: MR
authors.lastname: Parthun
mesh_terms: D000818:Animals; D006657:Histones / Q000737:chemistry*; D006801:Humans; D013058:Mass Spectrometry; D010446:Peptide Fragments / Q000737:chemistry*; D010449:Peptide Mapping; D011499:Protein Processing, Post-Translational
chemical_list: D006657:Histones; D010446:Peptide Fragments