Cuttlefish spermatid-specific protein T. Molecular characterization of two variants T1 and T2, putative precursors of sperm protamine variants Sp1 and Sp2
In cuttlefish, as in selachians and mammals, spermiogenesis is characterized by the double nuclear protein transition histones---intermediate protein (protein T)---protamine (protein Sp). The cuttlefish protein T, which consists of two structural variants phosphorylated at different degrees, is the...
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Veröffentlicht in: | The Journal of biological chemistry 1991-09, Vol.266 (26), p.17388-17395 |
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Sprache: | eng |
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Zusammenfassung: | In cuttlefish, as in selachians and mammals, spermiogenesis is characterized by the double nuclear protein transition histones---intermediate
protein (protein T)---protamine (protein Sp). The cuttlefish protein T, which consists of two structural variants phosphorylated
at different degrees, is the first invertebrate spermatid-specific protein to be fully characterized and sequenced. The primary
structures of these two variants were established from sequence analysis and mass spectrometric data of the proteins and their
fragments. T1 and T2 are two highly related proteins of 78 and 77 residues, respectively, which differ only by four conservative
substitutions, two inversions Ser in equilibrium with Arg, and the deletion of 1 residue of arginine in variant T2. The asymmetrical
distribution of the hydrophobic and basic residues determines two well defined domains: an amino-terminal domain (residues
1-21) devoid of arginine and aromatic residues and containing all the aliphatic hydrophobic residues and a highly basic carboxyl-terminal
domain (residues 22-77 or 78) that contains 77% of arginine, all the tyrosine residues, and most of the phosphorylated serine
residues present in the protein. The complete structural identity of the basic carboxyl-terminal domain of spermatidal proteins
T1 and T2 with the protamine variants Sp1 and Sp2 isolated from cuttlefish spermatozoa strongly suggests that T1 and T2 could
be precursors of Sp1 and Sp2, respectively. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(19)47385-7 |