title: Revealing histone variant induced changes via quantitative proteomics.
abstract: Histone variants are isoforms of linker and core histone proteins that differ in their amino acid sequences. These variants have distinct genomic locations and posttranslational modifications, thus increasing the complexity of the chromatin architecture. Biological studies of histone variants indicate that they play a role in many processes including transcription, DNA damage response, and the cell cycle. The small differences in amino acid sequence and the diverse posttranslational modification states that exist between histone variants make traditional analysis using immunoassay methods challenging. In recent years, a number of mass spectrometric techniques have been developed to identify and quantify histones at the whole protein or peptide levels. In this review, we discuss the biology of histone variants and methods to characterize them using mass spectrometry-based proteomics.
authors.affiliation: Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.
authors.forename: Anna M
authors.initials: AM
authors.lastname: Arnaudo
authors.forename: Rosalynn C
authors.initials: RC
authors.lastname: Molden
authors.forename: Benjamin A
authors.initials: BA
authors.lastname: Garcia
mesh_terms: D000107:Acetylation; D000595:Amino Acid Sequence; D002843:Chromatin / Q000737:chemistry*; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D004261:DNA Replication; D006657:Histones / Q000737:chemistry* / Q000235:genetics; D007553:Isotope Labeling; D008969:Molecular Sequence Data; D010455:Peptides / Q000378:metabolism; D010766:Phosphorylation; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics; D011499:Protein Processing, Post-Translational; D040901:Proteomics / Q000379:methods*; D016415:Sequence Alignment; D015533:Transcriptional Activation
chemical_list: D002843:Chromatin; D006657:Histones; D010455:Peptides; D020033:Protein Isoforms