Characterization of histones and their post-translational modifications by mass spectrometry.
Histone proteins and their accompanying post-translational modifications have received much attention for their ability to affect chromatin structure and, hence, regulate gene expression. Recently, mass spectrometry has become an important complementary tool for the analysis of histone variants and modification sites, for determining the degree of occupancy of these modifications and for quantifying differential expression of these modifications from various samples. Additionally, as advancements in mass spectrometry technologies continue, the ability to read entire 'histone codes' across large regions of histone polypeptides or intact protein is possible. As chromatin biology demands, mass spectrometry has adapted and continues as a key technology for the analysis of gene regulation networks involving histone modifications.
Garcia
Benjamin A
BA
Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Shabanowitz
Jeffrey
J
Hunt
Donald F
DF
D000595:Amino Acid Sequence; D002843:Chromatin / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D005786:Gene Expression Regulation / Q000235:genetics / Q000502:physiology; D006657:Histones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D013058:Mass Spectrometry / Q000379:methods; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D010449:Peptide Mapping; D011499:Protein Processing, Post-Translational
D002843:Chromatin; D006657:Histones; D010446:Peptide Fragments