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Volumn 7, Issue 12, 1996, Pages 1895-1907

Is outer arm dynein intermediate chain 1 multifunctional?

Author keywords

[No Author keywords available]

Indexed keywords

DYNEIN ADENOSINE TRIPHOSPHATASE;

EID: 0029847074     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.7.12.1895     Document Type: Article
Times cited : (82)

References (48)
  • 2
    • 0025882349 scopus 로고
    • PROSITE: A dictionary of sites and patterns in proteins
    • Bairoch, A. (1991). PROSITE: a dictionary of sites and patterns in proteins. Nucleic Acids Res. 29, 2241-2245.
    • (1991) Nucleic Acids Res. , vol.29 , pp. 2241-2245
    • Bairoch, A.1
  • 3
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou, P.Y., and Fasman, G.D. (1978). Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol. 47, 45-148.
    • (1978) Adv. Enzymol. , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 4
    • 0000929505 scopus 로고
    • The hydrophobic moment detects periodicity in protein hydrophobicity
    • Eisenberg, D., Sweet, R.M., and Terwilliger, T.C. (1984). The hydrophobic moment detects periodicity in protein hydrophobicity. Proc. Natl. Acad. Sci. USA 81, 140-144.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 140-144
    • Eisenberg, D.1    Sweet, R.M.2    Terwilliger, T.C.3
  • 5
    • 0028029306 scopus 로고
    • A monoclonal antibody against the dynein 1C1 peptide of sea urchin spermatozoa inhibits the motility of sea urchin, dinoflagellate, and human flagellar axonemes
    • Gagnon, C., White, A., Huitorel, P., and Cosson, J. (1994). A monoclonal antibody against the dynein 1C1 peptide of sea urchin spermatozoa inhibits the motility of sea urchin, dinoflagellate, and human flagellar axonemes. Mol. Biol. Cell 5, 1051-1063.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1051-1063
    • Gagnon, C.1    White, A.2    Huitorel, P.3    Cosson, J.4
  • 6
    • 0024320189 scopus 로고
    • Outer arm dynein from trout spermatozoa. Purification, polypeptide composition, and enzymatic properties
    • Gatti, J.-L., King, S.M., Moss, A.G., and Witman, G.M. (1989). Outer arm dynein from trout spermatozoa. Purification, polypeptide composition, and enzymatic properties. J. Biol. Chem. 264, 11450-11457.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11450-11457
    • Gatti, J.-L.1    King, S.M.2    Moss, A.G.3    Witman, G.M.4
  • 7
    • 0025914104 scopus 로고
    • Nucleoside diphosphate kinase from human erythrocytes: Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme
    • Gilles, A.-M., Presecan, E., Vonica, A., and Lascu, I. (1991). Nucleoside diphosphate kinase from human erythrocytes: structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J. Biol. Chem. 266, 8784-8789.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8784-8789
    • Gilles, A.-M.1    Presecan, E.2    Vonica, A.3    Lascu, I.4
  • 9
    • 0022544108 scopus 로고
    • Rate of ATP synthesis by dynein
    • Holzbaur, E.L.F., and Johnson, K.A. (1986). Rate of ATP synthesis by dynein. Biochemistry 25, 428-434.
    • (1986) Biochemistry , vol.25 , pp. 428-434
    • Holzbaur, E.L.F.1    Johnson, K.A.2
  • 10
    • 0019401849 scopus 로고
    • Evidence for participation of sperm proteinases in fertilization of the solitary ascidian, Halocynthia roretzi: Effects of protease inhibitors
    • Hoshi, M., Numakunai, T., and Sawada, H. (1981). Evidence for participation of sperm proteinases in fertilization of the solitary ascidian, Halocynthia roretzi: effects of protease inhibitors. Dev. Biol. 86, 117-121.
    • (1981) Dev. Biol. , vol.86 , pp. 117-121
    • Hoshi, M.1    Numakunai, T.2    Sawada, H.3
  • 11
    • 0028342672 scopus 로고
    • Cross-linking of β heavy chain subunit of dynein from sea urchin sperm flagella by dimethyl suberimidate
    • Inaba, K. (1994). Cross-linking of β heavy chain subunit of dynein from sea urchin sperm flagella by dimethyl suberimidate. Biomed. Res. 15, 123-126.
    • (1994) Biomed. Res. , vol.15 , pp. 123-126
    • Inaba, K.1
  • 12
    • 0028987667 scopus 로고
    • ATP-dependent conformational changes of dynein: Evidence for changes in the interaction of dynein heavy chain with the intermediate chain 1
    • Inaba, K. (1995). ATP-dependent conformational changes of dynein: evidence for changes in the interaction of dynein heavy chain with the intermediate chain 1. J. Biochem. 117, 903-907.
    • (1995) J. Biochem. , vol.117 , pp. 903-907
    • Inaba, K.1
  • 13
    • 0024336008 scopus 로고
    • Dynamic conformational changes of 21S dynein ATPase coupled with ATP hydrolysis revealed by proteolytic digestion
    • Inaba, K., and Mohri, H. (1989). Dynamic conformational changes of 21S dynein ATPase coupled with ATP hydrolysis revealed by proteolytic digestion. J. Biol. Chem. 264, 8384-8388.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8384-8388
    • Inaba, K.1    Mohri, H.2
  • 14
    • 0026349092 scopus 로고
    • A chymotrypsin-like protease involved in motility of sperm in salmonid fish
    • Inaba, K., and Morisawa, M. (1991). A chymotrypsin-like protease involved in motility of sperm in salmonid fish. Biomed. Res. 12, 435-437.
    • (1991) Biomed. Res. , vol.12 , pp. 435-437
    • Inaba, K.1    Morisawa, M.2
  • 15
    • 0026992037 scopus 로고
    • Chymotrypsin-like protease activity associated with demembranated sperm of chum salmon
    • Inaba, K., and Morisawa, M. (1992). Chymotrypsin-like protease activity associated with demembranated sperm of chum salmon. Biol. Cell 76, 329-333.
    • (1992) Biol. Cell , vol.76 , pp. 329-333
    • Inaba, K.1    Morisawa, M.2
  • 16
    • 0025203679 scopus 로고
    • Localization of an intermediate chain of outer arm dynein by immunoelectron microscopy
    • King, S.M., and Witman, G.B. (1990). Localization of an intermediate chain of outer arm dynein by immunoelectron microscopy. J. Biol. Chem. 265, 19807-19811.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19807-19811
    • King, S.M.1    Witman, G.B.2
  • 17
    • 0025923808 scopus 로고
    • r 78,000 intermediate chain of Chlamydomonas outer arm dynein interacts with α-tubulin in situ
    • r 78,000 intermediate chain of Chlamydomonas outer arm dynein interacts with α-tubulin in situ. J. Biol. Chem. 266, 8401-8407.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8401-8407
    • King, S.M.1    Wilkerson, C.G.2    Witman, G.B.3
  • 18
    • 0025047039 scopus 로고
    • Outer-arm dynein from trout spermatozoa: Substructural organization
    • King, S.M., Gatti, J.L., Moss, A.G., and Witman, G.B. (1990). Outer-arm dynein from trout spermatozoa: substructural organization. Cell Motil. Cytoskel. 16, 266-278.
    • (1990) Cell Motil. Cytoskel. , vol.16 , pp. 266-278
    • King, S.M.1    Gatti, J.L.2    Moss, A.G.3    Witman, G.B.4
  • 20
    • 0017249158 scopus 로고
    • Nucleoside diphosphate kinase and the flagellar movement of glycerinated spermatozoa
    • Kobayashi, T., Kaji, K., and Sakai, H. (1976). Nucleoside diphosphate kinase and the flagellar movement of glycerinated spermatozoa. J. Biochem. 79, 413-418.
    • (1976) J. Biochem. , vol.79 , pp. 413-418
    • Kobayashi, T.1    Kaji, K.2    Sakai, H.3
  • 21
    • 0022497304 scopus 로고
    • The initial phosphate burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified malachite green method for determination of inorganic phosphate
    • Kodama, T., Fukui, K., and Kometani, K. (1986). The initial phosphate burst in ATP hydrolysis by myosin and subfragment-1 as studied by a modified malachite green method for determination of inorganic phosphate. J. Biochem. 99, 1465-1472.
    • (1986) J. Biochem. , vol.99 , pp. 1465-1472
    • Kodama, T.1    Fukui, K.2    Kometani, K.3
  • 22
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and Doolittle, R.F. (1982). A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 23
    • 0023066865 scopus 로고
    • Gene isolation by screening λgt11 libraries with antibodies
    • Mierendorf, R.C., Percy, C., and Young, R.A. (1989). Gene isolation by screening λgt11 libraries with antibodies. Methods Enzymol. 152, 458-469.
    • (1989) Methods Enzymol. , vol.152 , pp. 458-469
    • Mierendorf, R.C.1    Percy, C.2    Young, R.A.3
  • 24
    • 0025770089 scopus 로고
    • Identification of oda6 as a Chlamydomonas dynein mutant by rescue with the wild-type gene
    • Mitchell, D.R., and Kang, Y. (1991). Identification of oda6 as a Chlamydomonas dynein mutant by rescue with the wild-type gene. J. Cell Biol. 113, 835-842.
    • (1991) J. Cell Biol. , vol.113 , pp. 835-842
    • Mitchell, D.R.1    Kang, Y.2
  • 25
    • 0027170722 scopus 로고
    • Reversion analysis of dynein intermediate chain function
    • Mitchell, D.R., and Kang, Y. (1993). Reversion analysis of dynein intermediate chain function. J. Cell Sci. 105, 1069-1078.
    • (1993) J. Cell Sci. , vol.105 , pp. 1069-1078
    • Mitchell, D.R.1    Kang, Y.2
  • 26
    • 0026660469 scopus 로고
    • The α subunit of sea urchin sperm outer arm dynein mediates structural and rigor binding to microtubules
    • Moss, A.G., Sale, W.S., Fox, L.A., and Witman, G.B. (1992). The α subunit of sea urchin sperm outer arm dynein mediates structural and rigor binding to microtubules. J. Cell Biol. 118, 1189-1200.
    • (1992) J. Cell Biol. , vol.118 , pp. 1189-1200
    • Moss, A.G.1    Sale, W.S.2    Fox, L.A.3    Witman, G.B.4
  • 27
    • 0028076764 scopus 로고
    • The ancient regulatory-protein family of WD-repeat proteins
    • Neer, E.J., Schmidt, C.J., Nambudripad, R., and Smith, T.F. (1994). The ancient regulatory-protein family of WD-repeat proteins. Nature 371, 297-300.
    • (1994) Nature , vol.371 , pp. 297-300
    • Neer, E.J.1    Schmidt, C.J.2    Nambudripad, R.3    Smith, T.F.4
  • 28
    • 0026425498 scopus 로고
    • Four ATP-binding sites in the midregion of the β heavy chain of dynein
    • Ogawa, K. (1991). Four ATP-binding sites in the midregion of the β heavy chain of dynein. Nature 352, 643-645.
    • (1991) Nature , vol.352 , pp. 643-645
    • Ogawa, K.1
  • 29
    • 0026849687 scopus 로고
    • Primary structure and function of a dynein motor molecule
    • Ogawa, K. (1992). Primary structure and function of a dynein motor molecule. Zool. Sci. 9, 265-274.
    • (1992) Zool. Sci. , vol.9 , pp. 265-274
    • Ogawa, K.1
  • 30
    • 0015518047 scopus 로고
    • Studies on flagellar ATPase from sea urchin spermatozoa. I. Purification and some properties of the enzyme
    • Ogawa, K., and Mohri, H. (1972). Studies on flagellar ATPase from sea urchin spermatozoa. I. Purification and some properties of the enzyme. Biochim. Biophys. Acta 256, 142-155.
    • (1972) Biochim. Biophys. Acta , vol.256 , pp. 142-155
    • Ogawa, K.1    Mohri, H.2
  • 31
    • 0024192580 scopus 로고
    • Assembly of a protein sharing epitopes with sperm dynein heavy chains into meiotic spindle in the prometaphase starfish oocyte
    • Ogawa, K., Yokota, E., and Shirai, H. (1988). Assembly of a protein sharing epitopes with sperm dynein heavy chains into meiotic spindle in the prometaphase starfish oocyte. Biol. Cell 64, 57-66.
    • (1988) Biol. Cell , vol.64 , pp. 57-66
    • Ogawa, K.1    Yokota, E.2    Shirai, H.3
  • 32
    • 0029078097 scopus 로고
    • Interspecies conservation of outer arm dynein intermediate chain sequences defines two intermediate chain subclasses
    • Ogawa, K., Kamiya, R., Wilkerson, C.G., and Witman, G. (1995). Interspecies conservation of outer arm dynein intermediate chain sequences defines two intermediate chain subclasses. Mol. Biol. Cell 6, 685-696.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 685-696
    • Ogawa, K.1    Kamiya, R.2    Wilkerson, C.G.3    Witman, G.4
  • 33
    • 0025096488 scopus 로고
    • The outer arm dynein α-heavy chains of sea urchin sperm flagella and embryonic cilia are different
    • Ogawa, K., Yokota, E., Hamada, Y., Wada, S., Okuno, M., and Nakajima, Y. (1990). The outer arm dynein α-heavy chains of sea urchin sperm flagella and embryonic cilia are different. Cell Motil. Cytoskel. 16, 58-67.
    • (1990) Cell Motil. Cytoskel. , vol.16 , pp. 58-67
    • Ogawa, K.1    Yokota, E.2    Hamada, Y.3    Wada, S.4    Okuno, M.5    Nakajima, Y.6
  • 34
    • 0029664996 scopus 로고    scopus 로고
    • Two functional thioredoxins containing redox-sensitive vicinal dithiols from the Chlamydomonas outer dynein arm
    • Patel-King, R.S., Benashski, S.E., Harrison, A., and King, S.M. (1996). Two functional thioredoxins containing redox-sensitive vicinal dithiols from the Chlamydomonas outer dynein arm. J. Biol. Chem. 271, 6283-6291.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6283-6291
    • Patel-King, R.S.1    Benashski, S.E.2    Harrison, A.3    King, S.M.4
  • 35
    • 0021111979 scopus 로고
    • Characterization of the ATP-sensitive binding of Tetrahymena 30 S dynein to bovine brain microtubules
    • Porter, M.E., and Johnson, K.A. (1983). Characterization of the ATP-sensitive binding of Tetrahymena 30 S dynein to bovine brain microtubules. J. Biol. Chem. 258, 6575-6581.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6575-6581
    • Porter, M.E.1    Johnson, K.A.2
  • 37
    • 0024110708 scopus 로고
    • Isolated β-heavy chain subunit of dynein translocates microtubules in vitro
    • Sale, W.S., and Fox, L.A. (1988). Isolated β-heavy chain subunit of dynein translocates microtubules in vitro. J. Cell Biol. 107, 1793-1797.
    • (1988) J. Cell Biol. , vol.107 , pp. 1793-1797
    • Sale, W.S.1    Fox, L.A.2
  • 38
    • 0023446558 scopus 로고
    • The substrate specificity of dynein from Tetrahymena cilia
    • Shimizu, T. (1987). The substrate specificity of dynein from Tetrahymena cilia. J. Biochem. 102, 1159-1165.
    • (1987) J. Biochem. , vol.102 , pp. 1159-1165
    • Shimizu, T.1
  • 39
    • 0343001409 scopus 로고
    • Phosphorothioate analogues of adenosine 5′- Triphosphate as substrates of dynein from Tetrahymena cilia
    • Shimizu, T., and Furusawa, K. (1986). Phosphorothioate analogues of adenosine 5′- triphosphate as substrates of dynein from Tetrahymena cilia. Biochemistry 25, 5787-5792.
    • (1986) Biochemistry , vol.25 , pp. 5787-5792
    • Shimizu, T.1    Furusawa, K.2
  • 40
    • 0016144752 scopus 로고
    • Effects of N-ethylmaleimide on dynein adenosine triphosphatase activity and its recombining ability with outer fibers
    • Shimizu, T., and Kimura, I. (1974). Effects of N-ethylmaleimide on dynein adenosine triphosphatase activity and its recombining ability with outer fibers. J. Biochem. 76, 1001-1008.
    • (1974) J. Biochem. , vol.76 , pp. 1001-1008
    • Shimizu, T.1    Kimura, I.2
  • 41
    • 0027076535 scopus 로고
    • Dynein from serotonin-activated cilia and flagella: Extraction characteristics and distinct sites for cAMP-dependent protein phosphorylation
    • Stephens, R.E., and Prior, G. (1992). Dynein from serotonin-activated cilia and flagella: extraction characteristics and distinct sites for cAMP-dependent protein phosphorylation. J. Cell Sci. 103, 999-1012.
    • (1992) J. Cell Sci. , vol.103 , pp. 999-1012
    • Stephens, R.E.1    Prior, G.2
  • 42
    • 0028934289 scopus 로고
    • Dynein inner arm heavy chain identification in cAMP- Activated flagella using class-specific polyclonal antibodies
    • Stephens, R.E., and Prior, G. (1995). Dynein inner arm heavy chain identification in cAMP- activated flagella using class-specific polyclonal antibodies. Cell Motil. Cytoskel. 30, 261-271.
    • (1995) Cell Motil. Cytoskel. , vol.30 , pp. 261-271
    • Stephens, R.E.1    Prior, G.2
  • 43
    • 0020478468 scopus 로고
    • Structure of the dynein-1 outer arm in sea urchin sperm flagella. I. Analysis by separation of subunits
    • Tang, W.-J.Y., Bell, C.W., Sale, W.S., and Gibbons, I.R. (1982). Structure of the dynein-1 outer arm in sea urchin sperm flagella. I. Analysis by separation of subunits. J. Biol. Chem. 257, 508-515.
    • (1982) J. Biol. Chem. , vol.257 , pp. 508-515
    • Tang, W.-J.Y.1    Bell, C.W.2    Sale, W.S.3    Gibbons, I.R.4
  • 44
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., and Gibson, T.J. (1994). CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 45
    • 0027421083 scopus 로고
    • Molecular analysis of the microtubule motor dynein
    • Vallee, R. (1993). Molecular analysis of the microtubule motor dynein. Proc. Natl. Acad. Sci. USA 90, 8769-8772.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8769-8772
    • Vallee, R.1
  • 46
    • 0026968911 scopus 로고
    • Dynein of sperm flagella of oyster belonging to Protostomia also has a two-headed structure
    • Wada, S., Okuno, M., Nakamura, K.-I., and Mohri, H. (1992). Dynein of sperm flagella of oyster belonging to Protostomia also has a two-headed structure. Biol. Cell 76, 311-317.
    • (1992) Biol. Cell , vol.76 , pp. 311-317
    • Wada, S.1    Okuno, M.2    Nakamura, K.-I.3    Mohri, H.4
  • 47
    • 0002513173 scopus 로고
    • The biochemistry, genetics and molecular biology of flagellar dynein
    • ed. J.S. Hyams and C.W. Lloyd, New York: Wiley-Liss
    • Witman, G.B., Wilkerson, C.G., and King, S.M. (1994). The biochemistry, genetics and molecular biology of flagellar dynein. In: Microtubules, ed. J.S. Hyams and C.W. Lloyd, New York: Wiley-Liss, 229-249.
    • (1994) Microtubules , pp. 229-249
    • Witman, G.B.1    Wilkerson, C.G.2    King, S.M.3
  • 48
    • 0014333552 scopus 로고
    • The bound nucleotides of the isolated microtubules of sea-urchin sperm flagella and their possible role in flagellar movement
    • Yanagisawa, T., Hasegawa, S., and Mohri, H. (1968). The bound nucleotides of the isolated microtubules of sea-urchin sperm flagella and their possible role in flagellar movement Exp. Cell Res. 52, 86-100.
    • (1968) Exp. Cell Res. , vol.52 , pp. 86-100
    • Yanagisawa, T.1    Hasegawa, S.2    Mohri, H.3


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