The amino acid sequence of the chromosomal protein HMG-Y, its relation to HMG-I and possible domains for the preferential binding of the proteins to stretches of A-T base pairs.
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.
Karlson
J R
JR
Department of Biochemistry, University of Oslo, Norway.
Mørk
E
E
Holtlund
J
J
Laland
S G
SG
Lund
T
T
D000595:Amino Acid Sequence; D001482:Base Composition; D001665:Binding Sites; D006609:High Mobility Group Proteins / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism; D011067:Poly dA-dT / Q000378:metabolism*; D011089:Polydeoxyribonucleotides / Q000378:metabolism*; D012689:Sequence Homology, Nucleic Acid; D012697:Serine Endopeptidases / Q000378:metabolism; D013820:Thermolysin / Q000378:metabolism
D006609:High Mobility Group Proteins; D010446:Peptide Fragments; D011089:Polydeoxyribonucleotides; D011067:Poly dA-dT; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D013820:Thermolysin