Nuclear transition protein 1 from ram elongating spermatids. Mass spectrometric characterization primary culture and phosphorylation sites of two variants
1991
Chirat, F. | Martinage, A. | Briand, Gwenola | Kouach, M. | Van Dorsselaer, Alain | LOIR, M. | Sautière, Pierre
The ram transition protein 1 (TP1) is present in spermatid cell nuclei in the nonphosphorylated, monophosphorylated and diphosphorylated forms. Its primary structure was determined by automated Edman degradation of S-carboxamidomethylated protein and of peptides generated by cleavage with thermolysin and endoproteinase Lys-c. The ram TP1 is a small basic protein of 54 residues and structurally very close to other mammalian TPI. The mass spectrometric data obtained from the protein and its fragments reveal that ram TP1 is indeed a mixture (approximately 5: 1) of two structural variants (M, 6346 and 6300). These variants differ only by the nature of the residue at position 27 (Cys in the major variant and Gly in the minor variant). The study of phosphorylation sites has shown that four different serine residues could be phosphorylated in the monophosphorylated TPI, at positions 8, 35, 36 or 39. From previous physical studies, it has been postulated that the Tyr32 surrounded by two highly conserved basic clusters was responsible for the destabilization of chromatin by intercalation of its phenol ring between the bases of double-stranded DNA. The presence of three phosphorylatable serine residues in the very conserved sequence 29 -42 is another argument for the involvement of this region in the interaction with DNA.
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