Mass spectrometric analysis of the HMGY protein from Lewis lung carcinoma. Identification of phosphorylation sites.
The primary structure of the Lewis lung carcinoma protein HMGY belonging to the nuclear group of proteins HMGI (high mobility group I) was determined using electrospray and fast atom bombardment mass spectrometry. It was demonstrated that the sequence of the tumor protein corresponds to the amino acid sequence derived from the cDNA from cultured cells and that the N-terminal serine residue is N-acetylated. Moreover, the two high performance liquid chromatography-purified forms Y1 and Y2 of the protein HMGY were shown to differ at the level of serine phosphorylation, since they contain three phosphate and two phosphate groups, respectively, in the C-terminal region. No other modification was detected in the remaining part of the molecule.
Ferranti
P
P
Servizio di Spettrometria di Massa, Consiglio Nazionale delle Ricerche, Naples, Italy.
Malorni
A
A
Marino
G
G
Pucci
P
P
Goodwin
G H
GH
Manfioletti
G
G
Giancotti
V
V
D000595:Amino Acid Sequence; D000818:Animals; D004247:DNA / Q000235:genetics; D006609:High Mobility Group Proteins / Q000737:chemistry*; D008175:Lung Neoplasms / Q000737:chemistry*; D013058:Mass Spectrometry; D051379:Mice; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry; D010750:Phosphoproteins / Q000737:chemistry; D010766:Phosphorylation
D006609:High Mobility Group Proteins; D009363:Neoplasm Proteins; D010446:Peptide Fragments; D010750:Phosphoproteins; D004247:DNA