title: The structure of ubiquitinated histone H2B.
abstract: Ubiquitinated histone H2B (uH2B) has been purified from both calf and pig thymus by exclusion chromatography in 7 M urea. Digestion of uH2B with Staphylococcus aureus V8 protease yielded the peptide 114-125 containing the ubiquitin moiety. Further digestion of this peptide with trypsin removed the ubiquitin and three H2B residues from the N-terminus. Edman degradations of both peptides established that ubiquitin is attached to the epsilon-amino group of lysine 120 in both calf and pig uH2B by an iso-peptide bond to the C-terminal glycine 76 of ubiquitin.
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D010450:Endopeptidases; D006657:Histones / Q000302:isolation & purification; D010446:Peptide Fragments / Q000032:analysis; D012697:Serine Endopeptidases; D013045:Species Specificity; D013552:Swine; D013950:Thymus Gland / Q000032:analysis*; D014357:Trypsin; D014452:Ubiquitins / Q000302:isolation & purification
chemical_list: D000596:Amino Acids; D006657:Histones; D010446:Peptide Fragments; D014452:Ubiquitins; D010450:Endopeptidases; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D014357:Trypsin