Karlson J R, Mørk E, Holtlund J, Laland S G, Lund T
Department of Biochemistry, University of Oslo, Norway.
Biochem Biophys Res Commun. 1989 Feb 15;158(3):646-51. doi: 10.1016/0006-291x(89)92770-8.
The primary structure of the human high mobility group (HMG) protein HMG-Y has been established except for a few amino acids in the N-terminal and the C-terminal part of the protein. It was found that the sequence was identical to that of HMG-I except for a run of eleven amino acids. Like HMG-I the protein was N-terminally blocked and the palindromic sequence Pro-Arg-Gly-Arg-Pro occurred twice as in HMG-I. The binding of peptides derived from HMG-I (after thermolysin cleavage) to poly (dA-dT).poly(dA-dT) suggested that there are at least two different binding domains in the protein and that binding is not dependent upon an intact protein.
