Tissue-specific expression and post-translational modification of histone H3 variants.
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.
Garcia
Benjamin A
BA
Institute for Genomic Biology, Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA. bagarcia@princeton.edu.
Thomas
C Eric
CE
Kelleher
Neil L
NL
Mizzen
Craig A
CA
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
D006657:Histones; D020033:Protein Isoforms; D008239:Lysine