title: Tissue-specific expression and post-translational modification of histone H3 variants.
abstract: Analyses of histone H3 from 10 rat tissues using a Middle Down proteomics platform revealed tissue-specific differences in their expression and global PTM abundance. ESI/FTMS with electron capture dissociation showed that, in general, these proteins were hypomodified in heart, liver and testes. H3.3 was hypermodified compared to H3.2 in some, but not all tissues. In addition, a novel rat testes-specific H3 protein was identified with this approach.
authors.affiliation: Institute for Genomic Biology, Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA. bagarcia@princeton.edu.
authors.forename: Benjamin A
authors.initials: BA
authors.lastname: Garcia
authors.forename: C Eric
authors.initials: CE
authors.lastname: Thomas
authors.forename: Neil L
authors.initials: NL
authors.lastname: Kelleher
authors.forename: Craig A
authors.initials: CA
authors.lastname: Mizzen
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D006657:Histones / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008239:Lysine / Q000378:metabolism; D008297:Male; D013058:Mass Spectrometry / Q000379:methods; D008969:Molecular Sequence Data; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D051381:Rats; D017207:Rats, Sprague-Dawley; D013737:Testis / Q000378:metabolism; D014018:Tissue Distribution
chemical_list: D006657:Histones; D020033:Protein Isoforms; D008239:Lysine