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Volumn 43, Issue 24, 2004, Pages 7766-7775

PL-I of Spisula solidissima, a highly elongated sperm-specific histone H1

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; AMINO ACIDS; DNA; ELECTROPHORESIS; GENES; POLYPEPTIDES; PROTEINS;

EID: 2942733480     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0360455     Document Type: Article
Times cited : (14)

References (56)
  • 1
    • 0001357904 scopus 로고
    • (Jamieson, B. G. M., Ausió, J., and Justine, J. L., Eds.), Memoires du Museum National d'Histoire Naturelle, Paris, France
    • Ausió, J. (1995) in Advances in Spermatozoal Phylogeny and Taxonomy (Jamieson, B. G. M., Ausió, J., and Justine, J. L., Eds.) pp 447-462, Memoires du Museum National d'Histoire Naturelle, Paris, France.
    • (1995) Advances in Spermatozoal Phylogeny and Taxonomy , pp. 447-462
    • Ausió, J.1
  • 2
    • 0020490421 scopus 로고
    • A high molecular weight nuclear basic protein from the bivalve mollusc Spisula solidissima
    • Ausió, J., and Subirana, J. A. (1982) A high molecular weight nuclear basic protein from the bivalve mollusc Spisula solidissima, J. Biol. Chem. 257, 2802-2805.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2802-2805
    • Ausió, J.1    Subirana, J.A.2
  • 3
    • 0023663338 scopus 로고
    • Structural characterization of the trypsin-resistant core in the nuclear sperm-specific protein from Spisula solidissima
    • Ausió, J., Toumadje, A., McParland, R., Becker, R. R., Johnson, W. C., and van Holde, K. E. (1987) Structural characterization of the trypsin-resistant core in the nuclear sperm-specific protein from Spisula solidissima, Biochemistry 26, 975-982.
    • (1987) Biochemistry , vol.26 , pp. 975-982
    • Ausió, J.1    Toumadje, A.2    McParland, R.3    Becker, R.R.4    Johnson, W.C.5    Van Holde, K.E.6
  • 4
    • 0024297037 scopus 로고
    • An unusual cysteine-containing histone H1-like protein and two protamine-like proteins are the major nuclear proteins of the sperm of the bivalve mollusc Macoma nasuta
    • Ausió, J. (1988) An unusual cysteine-containing histone H1-like protein and two protamine-like proteins are the major nuclear proteins of the sperm of the bivalve mollusc Macoma nasuta, J. Biol. Chem. 263, 10141-10150.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10141-10150
    • Ausió, J.1
  • 5
    • 0026452991 scopus 로고
    • Presence of a highly specific histone H1-like protein in the chromatin of the sperm of the bivalve mollusks
    • Ausió, J. (1992) Presence of a highly specific histone H1-like protein in the chromatin of the sperm of the bivalve mollusks, Mol. Cell. Biochem. 115, 163-172.
    • (1992) Mol. Cell. Biochem. , vol.115 , pp. 163-172
    • Ausió, J.1
  • 7
    • 0016442562 scopus 로고
    • Chicken erythrocyte histone H5 II. Amino acid sequence adjacent to the phenylalanine residue
    • Sautiere, P., Kmiecik, D., Loy, O., Briand, G., Biserte, G., Garel, A., and Champagne, M. (1975) Chicken erythrocyte histone H5 II. Amino acid sequence adjacent to the phenylalanine residue, FEBS Lett. 50, 200-203.
    • (1975) FEBS Lett. , vol.50 , pp. 200-203
    • Sautiere, P.1    Kmiecik, D.2    Loy, O.3    Briand, G.4    Biserte, G.5    Garel, A.6    Champagne, M.7
  • 9
    • 0034601695 scopus 로고    scopus 로고
    • Formation of regulator/target gene relationships during evolution
    • Schlake, T., Schorpp, M., and Boehm, T. (2000) Formation of regulator/target gene relationships during evolution, Gene 256, 29-34.
    • (2000) Gene , vol.256 , pp. 29-34
    • Schlake, T.1    Schorpp, M.2    Boehm, T.3
  • 10
    • 0033615555 scopus 로고    scopus 로고
    • Histone H1 and evolution of sperm nuclear basic proteins
    • Ausió, J. (1999) Histone H1 and evolution of sperm nuclear basic proteins, J. Biol. Chem. 274, 31115-31118.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31115-31118
    • Ausió, J.1
  • 11
  • 12
    • 0021949334 scopus 로고
    • On the diversity of sperm histones in the vertebrates: IV. Cytochemical and amino acid analysis in Anura
    • Kasinsky, H. E., Huang, S. Y., Mann, M., Roca, J., and Subirana, J. A. (1985) On the diversity of sperm histones in the vertebrates: IV. Cytochemical and amino acid analysis in Anura, J. Exp. Zool. 234, 33-46.
    • (1985) J. Exp. Zool. , vol.234 , pp. 33-46
    • Kasinsky, H.E.1    Huang, S.Y.2    Mann, M.3    Roca, J.4    Subirana, J.A.5
  • 13
    • 0030953535 scopus 로고    scopus 로고
    • Histone H1 variants as sperm-specific nuclear proteins of Rana catesbeiana, and their role in maintaining a unique condensed state of sperm chromatin
    • Itoh, T., Ausió, J., and Katagiri, C. (1997) Histone H1 variants as sperm-specific nuclear proteins of Rana catesbeiana, and their role in maintaining a unique condensed state of sperm chromatin, Mol. Reprod. Dev. 47, 181-190.
    • (1997) Mol. Reprod. Dev. , vol.47 , pp. 181-190
    • Itoh, T.1    Ausió, J.2    Katagiri, C.3
  • 14
    • 0028027202 scopus 로고
    • On the evolution of protamines in bony fish: Alternatives to the "retroviral horizontal transmission" hypothesis
    • Saperas, N., Ausió, J., Lloris, D., and Chiva, M. (1994) On the evolution of protamines in bony fish: Alternatives to the "retroviral horizontal transmission" hypothesis, J. Mol. Evol. 39, 282-295.
    • (1994) J. Mol. Evol. , vol.39 , pp. 282-295
    • Saperas, N.1    Ausió, J.2    Lloris, D.3    Chiva, M.4
  • 15
    • 0032513220 scopus 로고    scopus 로고
    • The high molecular weight chromatin proteins of winter flounder sperm are related to an extreme histone H1 variant
    • Watson, C. E., and Davies, P. L. (1998) The high molecular weight chromatin proteins of winter flounder sperm are related to an extreme histone H1 variant, J. Biol. Chem. 273, 6157-6162.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6157-6162
    • Watson, C.E.1    Davies, P.L.2
  • 18
    • 0033152591 scopus 로고    scopus 로고
    • Structure and expression of the highly repetitive histone H1-related sperm chromatin proteins from winter flounder
    • Watson, C. E., Gauthier, S. Y., and Davies, P. L. (1999) Structure and expression of the highly repetitive histone H1-related sperm chromatin proteins from winter flounder, Eur. J. Biochem. 262, 258-267.
    • (1999) Eur. J. Biochem. , vol.262 , pp. 258-267
    • Watson, C.E.1    Gauthier, S.Y.2    Davies, P.L.3
  • 19
    • 0027518437 scopus 로고
    • Post-translational cleavage of a histone H1-like protein in the sperm of Mytilus
    • Carlos, S., Hunt, D. F., Rocchini, C., Arnott, D. P., and Ausió, J. (1993) Post-translational cleavage of a histone H1-like protein in the sperm of Mytilus, J. Biol. Chem. 268, 195-199.
    • (1993) J. Biol. Chem. , vol.268 , pp. 195-199
    • Carlos, S.1    Hunt, D.F.2    Rocchini, C.3    Arnott, D.P.4    Ausió, J.5
  • 20
    • 0003350729 scopus 로고
    • Basic chromosomal proteins of marine invertebrates. III. The proteins from the sperm of bivalve molluscs
    • Zalensky, A., and Zalenskaya, I. A. (1980) Basic chromosomal proteins of marine invertebrates. III. The proteins from the sperm of bivalve molluscs, Comp. Biochem. Physiol., B 66, 415-419.
    • (1980) Comp. Biochem. Physiol., B , vol.66 , pp. 415-419
    • Zalensky, A.1    Zalenskaya, I.A.2
  • 21
    • 0028944304 scopus 로고
    • Complete sequence and characterization of the major sperm nuclear basic protein from Mytilus trossulus
    • Rocchini, C., Rice, P., and Ausió, J. (1995) Complete sequence and characterization of the major sperm nuclear basic protein from Mytilus trossulus, FEBS Lett. 363, 37-40.
    • (1995) FEBS Lett. , vol.363 , pp. 37-40
    • Rocchini, C.1    Rice, P.2    Ausió, J.3
  • 22
    • 38249034302 scopus 로고
    • Comparison of protamines from freshwater and marine bivalve molluscs: Evolutionary implications
    • Subirana, J. A., and Colom, J. (1987) Comparison of protamines from freshwater and marine bivalve molluscs: Evolutionary implications, FEBS Lett. 220, 193-196.
    • (1987) FEBS Lett. , vol.220 , pp. 193-196
    • Subirana, J.A.1    Colom, J.2
  • 23
    • 0027463631 scopus 로고
    • Sequence and characterization of a sperm-specific histone H1-like protein of Mytilus californianus
    • Carlos, S., Jutglar, L., Borrell, I., Hunt, D. F., and Ausió, J. (1993) Sequence and characterization of a sperm-specific histone H1-like protein of Mytilus californianus, J. Biol. Chem. 268, 185-194.
    • (1993) J. Biol. Chem. , vol.268 , pp. 185-194
    • Carlos, S.1    Jutglar, L.2    Borrell, I.3    Hunt, D.F.4    Ausió, J.5
  • 24
    • 0025837522 scopus 로고
    • Primary, secondary, and tertiary structure of the core of a histone H1-like protein from the sperm of Mytilus
    • Jutglar, L., Borrell, J. I., and Ausió, J. (1991) Primary, secondary, and tertiary structure of the core of a histone H1-like protein from the sperm of Mytilus, J. Biol. Chem. 266, 8184-8191.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8184-8191
    • Jutglar, L.1    Borrell, J.I.2    Ausió, J.3
  • 26
    • 0034622593 scopus 로고    scopus 로고
    • Walking into the unknown: A "step down" PCR-based technique leading to the direct sequence analysis of flanking genomic DNA
    • Zhang, Z., and Gurr, S. J. (2000) Walking into the unknown: A "step down" PCR-based technique leading to the direct sequence analysis of flanking genomic DNA, Gene 253, 145-150.
    • (2000) Gene , vol.253 , pp. 145-150
    • Zhang, Z.1    Gurr, S.J.2
  • 27
    • 0020478339 scopus 로고
    • Conformational study and determination of the molecular weight of highly charged basic proteins by sedimentation equilibrium and gel electrophoresis
    • Ausió, J., and Subirana, J. A. (1982) Conformational study and determination of the molecular weight of highly charged basic proteins by sedimentation equilibrium and gel electrophoresis, Biochemistry 21, 5910-5918.
    • (1982) Biochemistry , vol.21 , pp. 5910-5918
    • Ausió, J.1    Subirana, J.A.2
  • 28
    • 0032726384 scopus 로고    scopus 로고
    • Cysteine-containing histone H1-like (PL-I) proteins of sperm
    • Zhang, F., Lewis, J. D., and Ausió, J. (1999) Cysteine-containing histone H1-like (PL-I) proteins of sperm, Mol. Reprod. Dev. 54, 402-409.
    • (1999) Mol. Reprod. Dev. , vol.54 , pp. 402-409
    • Zhang, F.1    Lewis, J.D.2    Ausió, J.3
  • 30
    • 0026661397 scopus 로고
    • Packaging and unpackaging the sea urchin sperm genome
    • Poccia, D. L., and Green, G. R. (1992) Packaging and unpackaging the sea urchin sperm genome, Trends Biochem. Sci. 17, 223-227.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 223-227
    • Poccia, D.L.1    Green, G.R.2
  • 31
    • 0025091107 scopus 로고
    • Genomic sequences of human protamines whose genes, PRM1 and PRM2, are clustered
    • Domenjoud, L., Nussbaum, G., Adham, I. M., Greeske, G., and Engel, W. (1990) Genomic sequences of human protamines whose genes, PRM1 and PRM2, are clustered, Genomics 8, 127-133.
    • (1990) Genomics , vol.8 , pp. 127-133
    • Domenjoud, L.1    Nussbaum, G.2    Adham, I.M.3    Greeske, G.4    Engel, W.5
  • 33
    • 0028286596 scopus 로고
    • A serine kinase regulates intracellular localization of splicing factors in the cell cycle
    • Gui, J. F., Lane, W. S., and Fu, X. D. (1994) A serine kinase regulates intracellular localization of splicing factors in the cell cycle, Nature 369, 678-682.
    • (1994) Nature , vol.369 , pp. 678-682
    • Gui, J.F.1    Lane, W.S.2    Fu, X.D.3
  • 35
    • 0030980443 scopus 로고    scopus 로고
    • Analysis of expression and function of topoisomerase I and II during meiosis in male mice
    • Cobb, J., Reddy, R. K., Park, C., and Handel, M. A. (1997) Analysis of expression and function of topoisomerase I and II during meiosis in male mice, Mol. Reprod. Dev. 46, 489-498.
    • (1997) Mol. Reprod. Dev. , vol.46 , pp. 489-498
    • Cobb, J.1    Reddy, R.K.2    Park, C.3    Handel, M.A.4
  • 37
    • 0032919370 scopus 로고    scopus 로고
    • SMART: Identification and annotation of domains from signalling and extracellular protein sequences
    • Ponting, C. P., Schultz, J., Milpetz, F., and Bork, P. (1999) SMART: Identification and annotation of domains from signalling and extracellular protein sequences, Nucleic Acids Res. 27, 229-232.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 229-232
    • Ponting, C.P.1    Schultz, J.2    Milpetz, F.3    Bork, P.4
  • 38
    • 0027402969 scopus 로고
    • Crystal structure of globular domain of histone H5 and its implications for nucleosome binding
    • Ramakrishnan, V., Finch, J. T., Graziano, V., Lee, P. L., and Sweet, R. M. (1993) Crystal structure of globular domain of histone H5 and its implications for nucleosome binding, Nature 362, 219-223.
    • (1993) Nature , vol.362 , pp. 219-223
    • Ramakrishnan, V.1    Finch, J.T.2    Graziano, V.3    Lee, P.L.4    Sweet, R.M.5
  • 39
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede, T., Kopp, J., Guex, N., and Peitsch, M. C. (2003) SWISS-MODEL: An automated protein homology-modeling server, Nucleic Acids Res. 31, 3381-3385.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 40
    • 0032144941 scopus 로고    scopus 로고
    • Mytilus protamine-like sperm-specific protein genes are multicopy, dispersed, and closely associated with hypervariable RFLP regions
    • Heath, D. D., and Hilbish, T. J. (1998) Mytilus protamine-like sperm-specific protein genes are multicopy, dispersed, and closely associated with hypervariable RFLP regions, Genome 41, 587-596.
    • (1998) Genome , vol.41 , pp. 587-596
    • Heath, D.D.1    Hilbish, T.J.2
  • 41
    • 0036678329 scopus 로고    scopus 로고
    • Translational repression by MSY4 inhibits spermatid differentiation in mice
    • Giorgini, F., Davies, H. G., and Braun, R. E. (2002) Translational repression by MSY4 inhibits spermatid differentiation in mice, Development 129, 3669-3679.
    • (2002) Development , vol.129 , pp. 3669-3679
    • Giorgini, F.1    Davies, H.G.2    Braun, R.E.3
  • 42
    • 0033583087 scopus 로고    scopus 로고
    • Recent and rapid amplification of the sperm basic nuclear protein genes in winter flounder
    • Watson, C. E., and Davies, P. L. (1999) Recent and rapid amplification of the sperm basic nuclear protein genes in winter flounder, Biochim. Biophys. Acta 1444, 337-345.
    • (1999) Biochim. Biophys. Acta , vol.1444 , pp. 337-345
    • Watson, C.E.1    Davies, P.L.2
  • 43
    • 0027282643 scopus 로고
    • Can a protein influence the fate of its own coding sequence? The amino- and carboxyl-terminal regions of H1 histone
    • Ohno, S., and Becak, M. L. (1993) Can a protein influence the fate of its own coding sequence?: The amino- and carboxyl-terminal regions of H1 histone, Proc. Natl. Acad. Sci. U.S.A. 90, 7341-7345.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 7341-7345
    • Ohno, S.1    Becak, M.L.2
  • 44
    • 0025274379 scopus 로고
    • Vertebrate protamine gene evolution I. Sequence alignments and gene structure
    • Oliva, R., and Dixon, G. H. (1990) Vertebrate protamine gene evolution I. Sequence alignments and gene structure, J. Mol. Evol. 30, 333-346.
    • (1990) J. Mol. Evol. , vol.30 , pp. 333-346
    • Oliva, R.1    Dixon, G.H.2
  • 45
    • 0030870210 scopus 로고    scopus 로고
    • Novel testis-specific protein-DNA interactions activate transcription of the mouse protamine 2 gene during spermatogenesis
    • Yiu, G. K., and Hecht, N. B. (1997) Novel testis-specific protein-DNA interactions activate transcription of the mouse protamine 2 gene during spermatogenesis, J. Biol. Chem. 272, 26926-26933.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26926-26933
    • Yiu, G.K.1    Hecht, N.B.2
  • 47
    • 0032934529 scopus 로고    scopus 로고
    • Transcriptional and translational regulation of gene expression in haploid spermatids
    • Steger, K. (1999) Transcriptional and translational regulation of gene expression in haploid spermatids, Anat. Embryol. 199, 471-487.
    • (1999) Anat. Embryol. , vol.199 , pp. 471-487
    • Steger, K.1
  • 48
  • 49
    • 0038718585 scopus 로고    scopus 로고
    • A walk through vertebrate and invertebrate protamines
    • Lewis, J. D., Song, Y., De Jong, M. E., Bagha, S. M., and Ausió, J. (2003) A walk through vertebrate and invertebrate protamines, Chromosoma 111, 473-482.
    • (2003) Chromosoma , vol.111 , pp. 473-482
    • Lewis, J.D.1    Song, Y.2    De Jong, M.E.3    Bagha, S.M.4    Ausió, J.5
  • 50
    • 0034806975 scopus 로고    scopus 로고
    • MSY2 and MSY4 bind a conserved sequence in the 3′ untranslated region of protamine 1 mRNA in vitro and in vivo
    • Giorgini, F., Davies, H. G., and Braun, R. E. (2001) MSY2 and MSY4 bind a conserved sequence in the 3′ untranslated region of protamine 1 mRNA in vitro and in vivo, Mol. Cell. Biol. 21, 7010-7019.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7010-7019
    • Giorgini, F.1    Davies, H.G.2    Braun, R.E.3
  • 51
    • 0000602926 scopus 로고
    • Structural variability and compositional homology of the protamine-like components of the sperm from the bivalve mollusks
    • Ausió, J. (1986) Structural variability and compositional homology of the protamine-like components of the sperm from the bivalve mollusks, Comp. Biochem. Physiol., B 85, 439-449.
    • (1986) Comp. Biochem. Physiol., B , vol.85 , pp. 439-449
    • Ausió, J.1
  • 52
    • 1442287481 scopus 로고    scopus 로고
    • The sperm-specific proteins of the edible oyster (European flat oyster (Ostrea edulis)) are products of proteolytic processing
    • Agelopoulou, B., Cary, P. D., Pataryas, T., Aleporou-Marinou, V., and Crane-Robinson, C. (2004) The sperm-specific proteins of the edible oyster (European flat oyster (Ostrea edulis)) are products of proteolytic processing, Biochim. Biophys. Acta 1676, 12-22.
    • (2004) Biochim. Biophys. Acta , vol.1676 , pp. 12-22
    • Agelopoulou, B.1    Cary, P.D.2    Pataryas, T.3    Aleporou-Marinou, V.4    Crane-Robinson, C.5
  • 53
    • 0035986077 scopus 로고    scopus 로고
    • Protamine-like proteins: Evidence for a novel chromatin structure
    • Lewis, J. D., and Ausió, J. (2002) Protamine-like proteins: Evidence for a novel chromatin structure, Biochem. Cell Biol. 80, 353-361.
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 353-361
    • Lewis, J.D.1    Ausió, J.2
  • 54
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F., and Higgins, D. G. (1997) The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools, Nucleic Acids Res. 25, 4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 55
    • 0025730049 scopus 로고
    • Histone and histone gene compilation and alignment update
    • Wells, D., and Brown, D. (1991) Histone and histone gene compilation and alignment update, Nucleic Acids Res. 19 Suppl., 2173-2188.
    • (1991) Nucleic Acids Res. , vol.19 , Issue.SUPPL. , pp. 2173-2188
    • Wells, D.1    Brown, D.2
  • 56
    • 0025008168 scopus 로고
    • Sequence logos: A new way to display consensus sequences
    • Schneider, T. D., and Stephens, R. M. (1990) Sequence logos: A new way to display consensus sequences, Nucleic Acids Res. 18, 6097-6100.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6097-6100
    • Schneider, T.D.1    Stephens, R.M.2


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