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The structure of ubiquitinated histone H2B.
Author(s) -
Thorne A.W.,
Sautiere P.,
Briand G.,
CraneRobinson C.
Publication year - 1987
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1987.tb04852.x
Subject(s) - biology , ubiquitin , histone h2b , histone , biochemistry , trypsin , ubiquitins , peptide , ubiquitin ligase , enzyme , gene
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.