Nuclear basic proteins in spermiogenesis

Biochimie

Volumn 80, Issue 2, 1998, Pages 117-128

  Wouters Tyrou, D ^a   Martinage, A ^b   Chevaillier, P ^c   Sautiere P ^d  

^a INSERM   (France)

^b UNIV LILLE   (France)

^c UNIVERSITÉ PARIS EST CRÉTEIL   (France)

^d Inst de Biol et Inst P   (France)

Author keywords

Histones; Pro protamines; Protamines; Spermiogenesis; Transition proteins

Indexed keywords

BASIC PROTEIN; HISTONE; NUCLEAR PROTEIN; PROTAMINE; PROTEIN PRECURSOR;

ARTICLE; PROTEIN PROCESSING; SPERMATOGENESIS; SPERMATOZOON;

ANIMALIA;

EID: 0032007221     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(98)80018-7     Document Type: Article

References (92)

1. 1 Bloch DP (1969) A catalog of sperm histones. Genetics (Suppl) 61, 93-111
2. 2 Poccia D (1986) Remodeling of nucleoprotamines during gametogenesis, fertilization, and early development. Int Rev Cytol 105, 1-65
3. 3 Kasinsky HE (1989) Specificity and distribution of sperm basic proteins. In: Histones and other basic nuclear proteins (Hnilica LS, Stein GS, Stein JL eds) CRC Press, Boca Raton, FL, 73-163
4. 4 Oliva R, Dixon GH (1991) Vertebrate protamine genes and the histone-protamine replacement reaction. Prog Nucleic Acid Res Mol Biol 40, 25-94
5. 5 Wouters-Tyrou D, Sautière P, Biserte G (1976) Covalent structure of the sea urchin histone H4. FEBS Lett 65, 225-228
6. 6 Von Holt C, Strickland WN, Brandt WF, Strickland MS (1979) More histones structures. FEBS Lett 14, 201-218
7. 7 Strickland WN, Strickland M, Brandt WF, Von Holt C, Lehman A, Wittmann-Liebold B (1980) The primary structure of histone H1 from sperm of the sea urchin Parechinus angulosus. II. Sequence of the C-terminal CNBr peptide and the entire primary structure. Eur J Biochem 104, 567-578
8. 8 Kmiecik D, Sellos D, Bélaïche D, Sautière P (1985) Primary structure of the two variants of a sperm-specific histone H1 from the annelid Platynereis dumerilii. Eur J Biochem 150, 359-370
9. 9 Martinage A, Briand G, Van Dorsselaer A, Turner CH, Sautière P (1985) Primary structure of histone H2B from gonads of the starfish Asterias rubens. Identification of an N-dimethylproline residue at the amino-terminal. Eur J Biochem 147, 351-359
10. 10 Gusse M, Sautière P, Bélaïche D, Martinage A, Roux C, Dadoune JP, Chevaillier P (1986) Purification and characterization of nuclear basic proteins of human sperm. Biochim Biophys Acta 884, 124-134
11. 11 Wouters-Tyrou D, Martin-Ponthieu A, Sautière P, Biserte G (1981) Acetylation of histone H4 in chicken erythrocyte and cuttlefish testis chromatin. FEBS Lett 128, 195-200
12. 12 Oliva R, Mezquita C (1982) Histone H4 hyperacetylation and rapid turnover of its acetyl groups in transcriptionally inactive rooster testis spermatids-Nucleic Acids Res 10, 8049-8057
13. 13 Christensen ME, Rattner JB, Dixon GH (1984) Hyperacetylation of histone H4 promotes chromatin decondensation prior to histone replacement by protamines during spermatogenesis in rainbow trout. Nucleic Acids Res 12, 4575-4592
14. 14 Grimes SR, Henderson N (1984) Hyperacetylation of histone H4 in rat testis spermatids. Exp Cell Res 152, 91-97
15. 15 Grimes SR, Smart PG (1985) Changes in structural organization of chromatin during spermatogenesis in the rat. Biochim Biophys Acta 824, 128-139
16. 16 Couppez M, Martin-Ponthieu A, Sautière P (1987) Histone H4 from cuttlefish testis is sequentially acetylated. Comparison with acetylation of calf thymus histone H4. J Biol Chem 262, 2854-2860
17. 17 Loir M, Courtens JL (1979) Nuclear reorganization in ram spermatids. J Ultrastruct Res 67, 309-324
18. 18 Gusse M, Chevaillier P (1978) Etude ultrastructurale et chimique de la chromatine au cours de la spermiogenèse de la roussette Scylliorhinus caniculus (L). Cytobiologie 16, 421-443
19. 19 Gusse M, Chevaillier P (1981) Microelectrophoretic analysis of basic protein changes during spermiogenesis in the dogfish Scylliorhinus caniculus (L). Exp Cell Res 136, 391-397
20. 20 Chauvière M, Laine B, Sautière P, Chevaillier P (1983) Purification and characterization of two basic spermatid-specific proteins isolated from the dog-fish Scylliorhinus caniculus. FEBS Lett 152, 231-235
21. 21 Gusse M, Sautière P, Chauvière M, Chevaillier P (1983) Extraction, purification and characterization of the sperm protamines of the dog-fish Scylliorhinus caniculus. Biochim Biophys Acta 748, 93-98
22. 22 Chauvière M, Martinage A, Briand G, Sautière P, Chevaillier P (1987) Nuclear basic protein transition during sperm differentiation. Amino acid sequence of a spermatid-specific protein from the dog-fish Scylliorhinus caniculus. Eur J Biochem 169, 105-11
23. 23 Chauvière M, Martinage A, Briand G, Sautière P, Chevaillier P (1989) Nuclear basic protein transition during sperm differentiation. Primary structure of the spermatid-specific protein S2 from the dog-fish Scylliorhinus caniculus. Eur J Biochem 180, 329-335
24. 24 Chauvière M, Martinage A, Sautière P, Chevaillier P (1990) Les protéines nucléaires basiques de transition au cours de la spermiogenèse de la roussette Scylliorhinus caniculus. Reprod Nutr Dev 30, 349-354
25. 25 Singh J, Rao MRS (1987) Interaction of rat testis protein, TP, with nucleic acids in vitro. Fluorescence quenching, UV absorption, and thermal denaturation studies. J Biol Chem 262, 734-740
26. 26 Kremling H, Luerssen H, Adham IM, Klemmm U, Tsaousidou S, Engel W (1989) Nucleotide sequences and expression of cDNA clones for boar and bull transition protein 1 and its evolutionary conservation in mammals. Differentiation 40, 184-190
27. 27 Chirat F, Martinage A, Briand G, Kouach M, Van Dorsselaer A, Loir M, Sautière P (1991) Nuclear transition protein 1 from ram elongating spermatids. Mass spectrometry characterization, primary structure and phosphorylation sites of two variants. Eur J Biochem 198, 13-20
28. 28 Luerssen H, Hoyer-Fender S, Engel W (1988) The nucleotide sequence of human transition protein 1 cDNA. Nucleic Acids Res 16, 7723
29. 29 Kleene KC, Borzorgzadeh A, Flynn JF, Yelick PC, Hecht NB (1988) Nucleotide sequence of a cDNA clone encoding mouse transition protein 1. Biochim Biophys Acta 950, 215-220
30. 30 Kistler WS, Noyes C, Hsu R, Heinrikson RL (1975) The amino acid sequence of a testis-specific basic protein that is associated with spermatogenesis. J Biol Chem 250, 1847-1853
31. 31 Kleene KC, Flynn JF (1987) Characterization of a cDNA clone encoding a basic protein, TP2, involved in chromatin condensation during spermiogenesis in the mouse. J Biol Chem 262, 17272-17277
32. 32 Luerrssen H, Maier WM, Hoyer-Fender S, Engel W (1989) The nucleotide sequence of rat transition protein 2 (TP2) cDNA. Nucleic Acids Res 17, 3585
33. 33 Reinhart N, Kremling H, Luerssen H, Adham IM (1991) Characterization of a gene encoding a basic protein of the spermatid nucleus, TNP2, and its close linkage to the protamine genes in the bull. Biol Chem Hoppe-Seyler 372, 431-436
34. 34 Keime S, Heitland K, Kumm S, Schlosser M, Hroch N, Holtz W, Engel W (1992) Characterization of four genes encoding basic proteins of the porcine spermatid nucleus and close linkage of three of them. Biol Chem Hoppe-Seyler 373, 261-270
35. 35 Chirat F (1990) Les protéines nucléaires basiques de la spermiogenèse du bélier Ovis aries. Structure primaire, phosphorylation. PhD Thesis, Lille
36. 36 Baskaran R, Rao MRS (1990) Interaction of spermatid-specific protein TP2 with nucleic acids in vitro. A comparative study with TP1. J Biol Chem 265, 21039-21047
37. 37 Baskaran R, Rao MRS (1991) Mammalian spermatid specific protein, TP2, is a zinc metalloprotein with two finger motifs. Biochem Biophys Res Commun 179, 1491-1499
38. 38 Dupressoir T, Sautière P, Lanneau M, Loir M (1985) Isolation and characterization of the ram spermatidal nuclear proteins P1, 3 and T. Exp Cell Res 161, 63-74
39. 39 Akama K, Oka S, Tobita T, Hayashi H (1994) The amino acid sequence of a boar transition protein 3. J Biochem 115, 58-65
40. 40 Unni E, Zhang Y, Meistrich ML, Balhorn R (1994) Rat spermatid basic nuclear protein TP3 is the precursor of protamine 2. Exp Cell Res 210, 39-45
41. 41 Akama K, Sato H, Furihata-Yamauchi M, Komatsu Y, Tobita T, Nakano M (1996) Interaction of nucleosome core DNA with transition proteins 1 and 3 from boar late spermatid nuclei. J Biochem 119, 448-455
42. 42 Unni E, Meistrich ML (1992) Purification and characterization of the rat spermatid basic nuclear protein TP4. J Biol Chem 267, 25359-25363
43. 43 Akama K, Ichimura H, Sato H, Kojima S, Miura KI, Hayashi H, Komatsu Y, Nakano M (1995) The amino acid sequence and interaction with the nucleosome core DNA of transition protein 4 from boar late spermatid nuclei. Eur J Biochem 233, 179-185
44. 44 Wouters-Tyrou D, Martin-Ponthieu A, Richard A, Sautière P (1988) Characterization of the nuclear basic proteins specific of spermiogenesis in cuttlefish, Sepia officinalis. Biochim Biophys Acta 953, 86-94
45. 45 Rousseaux-Prévost R, Engelhardt RP, Rousseaux J, Wouters-Tyrou D, Sautière P (1988) Nuclear protein transitions in cuttlefish spermiogenesis: Immunocytochemical localization of a protein specific for the spermatid stage. Gamete Res 19, 277-290
46. 46 Wouters-Tyrou D, Chartier-Harlin MC, Martin-Ponthieu A, Boutillon C, Van Dorsselaer A, Sautière P (1991) Cuttlefish spermatid-specific protein T. Molecular characterization of two variants T1 and T2, putative precursors of sperm protamine variants Sp1 and Sp2. J Biol Chem 266, 17388-17395
47. 47 Wouters-Tyrou D, Martin-Ponthieu A, Ledoux-Andula N, Kouach M, Jaquinod M, Subirana JA, Sautière P (1995) Squid spermiogenesis: molecular characterization of testis-specific pro-protamines. Biochem J 309, 529-534
48. 48 Chesneau V, Pierotti A.R, Barré N, Créminon C, Tougard C, Cohen P (1994) Isolation and characterization of a dibasic selective metalloendopeptidase from rat testis that cleaves at the amino terminus of arginine residues. J Biol Chem 269, 2056-2061
49. 49 Pierotti AR, Prat A, Chesneau V, Gaudoux F, Leseney AM, Foulon T, Cohen P (1994) N-arginine dibasic convertase, a metalloendopeptidase as a prototype of a class of processing enzymes. Proc Natl Acad Sci USA 91, 6078-6082
50. 50 Rholam M, Nicolas P, Cohen P (1986) Precursors for peptide hormones share common secondary structures forming features at the proteolytic processing sites. FEBS Lett 207, 1-6
51. 51 Webster A, Russel S, Talbot P, Russel WC, Kemp GD (1989) Characterization of the adenovirus proteinase: substrate specificity. J Gen Virol 70, 3225-3234
52. 52 Ausio J, McParland R (1989) Sequence and characterization of the spenn-specific protein φ3 from Mytilus californianus. Eur J Biochem 182, 569-576
53. 53 Colom J, Subirana JA (1981) Presence of H2B histone in spermatozoa from marine gastropods. Exp Cell Res 131, 462-465
54. 54 Daban M, Martinage A, Kouach M, Chiva M, Subirana JA, Sautière P (1995) Sequence analysis and structural features of the largest known protamine isolated from the sperm of the archaeogastropod Monodonta turbinata. J Mol Evol 40, 663-670
55. 55 Marrin-Ponthieu A, Wouters-Tyrou D, Bélaïche D, Sautière P, Schindler P, Van Dorsselaer A (1991 ) Cuttlefish sperm protamines. I Amino acid sequences of two distinct variants. Eur J Biochem 195, 611-619
56. 56 Schindler P, Bitsch F, Klarskov K, Roepstorff P, Briand G, Wouters-Tyrou D, Sautière P, Van Dorsselaer A (1991) Cuttlefish sperm protamines. II Mass spectrometry of protamines and related peptides. Eur J Biochem 195, 621-629
57. 57 Ammer H, Henschen A (1988) Primary structure of rabbit sperm protamine, the first protamine of its type with an aberrant N-terminal. FEBS Lett 242, 111-116
58. 58 Kouach M, Jaquinod M, Bélaïche D, Sautière P, Van Dorsselaer A, Chevaillier P, Briand G (1993) A corrected primary structure for dog-fish Scylliorhinus caniculus protamine Z3. Biochim Biophys Acta 1162, 99-104
59. 59 Subirana JA, Cozcolluela C, Palau J, Unzeta M (1973) Protamines and other basic proteins from spermatozoa of molluscs. Biochim Biophys Acta 317, 364-379
60. 60 Sautière P, Briand G, Gusse M, Chevaillier P (1981) Primary structure of a protamine isolated from the sperm nuclei of the dog-fish Scylliorhinus caniculus. Eur J Biochem 119, 251-255
61. 61 Sautière P, Gusse M, Briand G, Martinage A, Chevaillier P (1984) Primary structure of scylliorhinine S4, a protamine isolated from sperm nuclei of the dog-fish Scylliorhinus caniculus. Biochim Biophys Acta 791, 82-86
62. 62 Martinage A, Gusse M, Bélaïche D, Sautière P, Chevaillier P (1985) Amino acid sequence of a cysteine-rich, arginine-rich sperm protamine of the dog-fish Scylliorhinus caniculus. Biochim Biophys Acta 831, 172-178
63. 63 Chevaillier P, Martinage A, Gusse M, Sautière P (1987) Amino acid sequence of scylliorhinine Z1 and comparison of the primary structure of the protamines of the dog-fish Scylliorhinus caniculus. Biochim Biophys Acta 914, 19-27
64. 64 Ando T, Suzuki K (1967) The amino acid sequence of the third component of clupeine. Biochim Biophys Acta 140, 375-377
65. 65 Ando T, Watanabe S (1969) A new method for fractionation of protamines and the amino acid sequence of salmine and three components of iridine. InI J Protein Res 1, 221-224
66. 66 Bretzel G (1973) Uber Thynin, das Protamine des Thunfisches. Die Aminosauresequenz von Thynin Z1. XIII. Mittelung über die Struktur der Protamine in der Untersuchungsreike von Waldschmidt-Leitz und Mitaebeitern. Hoppe Seyler's Z Physiol Chem 354, 312-320
67. 67 Yulikova EP, Evseenko LK, Baratova LA, Belyanova LP, Rybin VK, Silaev AB (1976) The primary structure of sturine B, a protamine from Caspian sturgeon. Bioorg Khim 2, 1613-1617
68. 68 Martinage A, Depeiges A, Wouters D, Morel L, Sautière P (1996) Spermatogenesis of the lizard Lacerta vivipara: histological studies and amino acid sequence of a protamine lacertine 1. CR Acad Sci Paris 319, 511-516
69. 69 Oliva R, Goren R, Dixon GH (1989) Quail (Coturnix japonica) protamine, full-length cDNA sequence, and the function and evolution of venebrate protamines. J Biol Chem 264, 17627-17630
70. 70 McKay DJ, Renaux BS, Dixon GH (1985) The amino acid sequence of human sperm protamine P1. Biosci Rep 5, 383-391
71. 71 Ammer H, Henschen A, Lee CH (1986) Isolation and amino acid sequence analysis of human sperm protamines P1 and P2. Biol Chem Hoppe Seyler 367, 515-522
72. 72 Sautière P, Bélaïche D, Martinage A, Loir M (1984) Primary structure of the ram (Ovis aries) protamine. Eur J Biochem 144, 121-125
73. 73 Bélaïche D, Loir M, Kruggle W, Sautière P (1987) Isolation and characterization of two protamines St1 and St2 from stallion spermatozoa and amino acid sequence of the major protamine St1. Biochim Biophys Acta 913, 145-149
74. 74 Queralt R, Adroer R, Oliva R, Winkfein RJ, Retief JD, Dixon GH (1995) Evolution of protamine P1 genes in mammals. J Mol Evol 40, 601-607
75. 75 Adroer R, Queralt R, Ballabriga J, Oliva R (1992) Nucleotide sequence of the protamine P1 gene from the whale Orcinus orca predicts a unique N-terminal amino acid motif. Nucleic Acids Res 20, 609
76. 76 Subirana JA (1983) Nuclear proteins in spermatozoa and their interactions with DNA. In: The sperm cell (André J, ed) Martinus Nijhoff, The Hague, 197-213
77. 77 McKay DJ, Renaux BS, Dixon GH (1986) Human sperm protamines. Amino acid sequences of two forms of protamine P2. Eur J Biochem 156, 5-8
78. 78 Domenjoud L, Fronia C, Uhde F, Engel W (1988) Sequence of human protamine 2 cDNA. Nucleic Acids Res 16, 7733
79. 79 Yelick PC, Balhorn R, Johnson PA, Corzett M, Mazrimas TA, Kleene KC, Hecht NB (1987) Mouse protamine 2 is synthesized as a precursor whereas mouse protamine 1 is not. Mol Cell Biol 7, 2173-2179
80. 80 Bellvé AR (1988) Purification and characterization of mouse protamines P1 and P2. Amino acid sequence of P2. Biochemistry 27, 2890-2897
81. 81 Reinicke K, Chevaillier P (1991) Human protamines are zinc-binding proteins. Mol Andrology 3, 49-65
82. 82 Bianchi F, Rousseaux-Prévost R, Sautière P, Rousseaux J (1992) P2 protamines from human sperm are zinc-finger proteins with one cys2/his2 motif. Biochem. Biophys Res Commun 182, 540-547
83. 83 Marushige Y, Marushige K (3975) Transformation of sperm histone during formation and maturation of rat spermatozoa. J Biol Chem 250, 39-45
84. 84 Bellvé AR, Anderson E, Hanley-Bowdoin L (1975) Synthesis and amino acid composition of basic proteins in mammalian sperm nuclei. Dev Biol. 47, 349-365
85. 85 Chirat F, Arkhis A, Martinage A, Jaquinod M, Chevaillier P, Sautière P (1993) Phosphorylation of human sperm protamines HP1 and HP2: identification of phosphorylation sites. Biochim Biophys Acta 1203, 109-114
86. 86 Pirhonen A, Linnale-Kankkunen A, Mäenfëä PH (1994) Identification of phosphoseryl residues in protamines from mature mammalian spermatozoa. Biol Reprod 50, 981-986
87. 87 Marushige Y, Marushige K (1978) Phosphorylation of sperm histone during spermiogenesis in mammals. Biochim Biophys Acta 518, 440-449
88. 88 Martinage A, Arkhis A, Alimi E, Sautière P, Chevaillier P (1990) Molecular characterization of nuclear basic protein HPI1, a putative precursor of human sperm protamines HP2 and HP3. Eur J Biochem 191, 449-451
89. 89 Alimi E, Martinage A, Arkhis A, Bélaïche D, Sautière P, Chevaillier P (1993) Amino acid sequence of the human intermediate basic protein 2 (HPI2) from sperm nuclei. Structural relationship with protamine P2. Eur J Biochem 214, 445-450
90. 90 Chauvière M, Martinage A, Debarle M, Sautière R, Chevaillier P (1992) Molecular characterization of six intermediate proteins in the processing of mouse protamine P2 precursor. Eur J Biochem 204, 759-765
91. 91 Debarle M, Martinage A, Sautière P, Chevaillier P (1995) Persistence of protamine precursors in mature sperm nuclei of the mouse. Mol Reprod Dev 40, 84-90
92. 92 Rogers S, Wells R, Rechsteiner M (1986) Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234, 364-368