title: Nuclear basic protein transition during sperm differentiation. Primary structure of the spermatid-specific protein S2 from the dog-fish Scylliorhinus caniculus.
abstract: The remodeling of nucleoproteins during dog-fish spermiogenesis involves two successive nuclear protein transitions: the first from somatic-type histones to transition proteins during the nuclear elongation of spermatids and the second leading to protamine-DNA association in mature spermatozoa. The chromatin of elongating spermatids contains two transition proteins called S1 and S2. The amino acid sequence of protein S1, a polypeptide of 87 residues was determined previously [Chauvière, M., Martinage, A., Briand, G., Sautière, P. & Chevaillier, Ph. (1987) Eur. J. Biochem. 169, 105-111]. In the present paper, we report the elucidation of the primary structure of the minor transition protein S2 established by automated Edman degradation of the protein and of its fragments generated by cleavage at methionine and aspartate residues. S2 contains 80 residues and has a molecular mass of 9726 Da. S2 is mainly characterized by a high content of basic amino acids mostly represented by lysine, a relatively high level of hydrophobic residues, the presence of six phosphorylatable residues and the lack of cysteine. Its amino acid sequence shows that the N-terminal half is highly basic, while the acidic residues are located in the C-terminal part of the protein where more diversity in amino acids is noticed. The two transition proteins S1 and S2 share striking structural similarities. Few but significative similarities have been detected with the mammalian transition protein TP1 [Kistler, W. S., Noyes, C., Hsu, R. & Heinrikson, R. L. (1975) J. Biol. Chem. 250, 1847-1853], suggesting similar functions for all these proteins in chromatin remodeling during sperm differentiation. By contrast, the two dog-fish spermatid-specific proteins are structurally unrelated to sperm protamines and cannot be considered as their precursors.
authors.affiliation: Laboratoire de Biologie Cellulaire, Université Paris-Val de Marne, Créteil, France.
authors.forename: M
authors.initials: M
authors.lastname: Chauvière
authors.forename: A
authors.initials: A
authors.lastname: Martinage
authors.forename: G
authors.initials: G
authors.lastname: Briand
authors.forename: P
authors.initials: P
authors.lastname: Sautière
authors.forename: P
authors.initials: P
authors.lastname: Chevaillier
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D002868:Chromosomal Proteins, Non-Histone / Q000302:isolation & purification*; D004284:Dogfish; D008297:Male; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D011487:Protein Conformation; D012697:Serine Endopeptidases; D013091:Spermatogenesis
chemical_list: D000596:Amino Acids; D002868:Chromosomal Proteins, Non-Histone; D010446:Peptide Fragments; C053886:spermatid transition proteins; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase