메뉴 건너뛰기




Volumn 137, Issue 3, 1997, Pages 649-656

Chlamydomonas inner-arm dynein mutant, ida5, has a mutation in an actin- encoding gene

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; DYNEIN ADENOSINE TRIPHOSPHATASE; PROTEIN SUBUNIT;

EID: 0030983282     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.137.3.649     Document Type: Review
Times cited : (100)

References (40)
  • 1
    • 0021198878 scopus 로고
    • Repeated consensus sequence and pseudopromoters in the four coordinately regulated tubulin genes of Chlamydomonas reinhardtii
    • Brunke, K.J., J.G. Anthony, E.J. Sternberg, and D.P. Weeks. 1984. Repeated consensus sequence and pseudopromoters in the four coordinately regulated tubulin genes of Chlamydomonas reinhardtii. Mol. Cell. Biol. 4:1115-1124.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 1115-1124
    • Brunke, K.J.1    Anthony, J.G.2    Sternberg, E.J.3    Weeks, D.P.4
  • 2
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P., and N. Sacchi. 1987. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 3
    • 0025015357 scopus 로고
    • Structure and expression of a single actin gene in Volvox carteri
    • Cresnar, B., W. Mages, K. Muller, J.M. Salbaum, and R. Schmitt. 1990. Structure and expression of a single actin gene in Volvox carteri. Curr. Genet. 18: 337-346.
    • (1990) Curr. Genet. , vol.18 , pp. 337-346
    • Cresnar, B.1    Mages, W.2    Muller, K.3    Salbaum, J.M.4    Schmitt, R.5
  • 4
    • 0020805282 scopus 로고
    • Elongation of the fertilization tubule in Chlamydomonas: New observations on the core microfilaments and the effect of transient intracellular signals on their structural integrity
    • Detmers, P.A., U.W. Goodenough, and J. Condeelis. 1983. Elongation of the fertilization tubule in Chlamydomonas: new observations on the core microfilaments and the effect of transient intracellular signals on their structural integrity. J. Cell Biol. 97:522-532.
    • (1983) J. Cell Biol. , vol.97 , pp. 522-532
    • Detmers, P.A.1    Goodenough, U.W.2    Condeelis, J.3
  • 5
    • 0022326198 scopus 로고
    • Localization of actin in Chlamydomonas using antiactin and NBD-phallacidin
    • Detmers, P.A., J.M. Carboni, and J. Condeelis. 1985. Localization of actin in Chlamydomonas using antiactin and NBD-phallacidin. Cell Motil. 5:415-430.
    • (1985) Cell Motil. , vol.5 , pp. 415-430
    • Detmers, P.A.1    Carboni, J.M.2    Condeelis, J.3
  • 6
    • 0016715973 scopus 로고
    • Gametic differentiation in Chlamydomonas reinhardtii. III. Cell wall lysis and microfilament-associated mating structure activation in wild-type and mutant strains
    • Goodenough, U.W., and R.L. Weiss. 1975. Gametic differentiation in Chlamydomonas reinhardtii. III. Cell wall lysis and microfilament-associated mating structure activation in wild-type and mutant strains. J. Cell Biol. 67:623-637.
    • (1975) J. Cell Biol. , vol.67 , pp. 623-637
    • Goodenough, U.W.1    Weiss, R.L.2
  • 7
    • 0013832925 scopus 로고
    • Cytochrome f and plastocyanin: Their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardtii
    • Gorman, D.S., and R.P. Levine. 1965. Cytochrome f and plastocyanin: their sequence in the photosynthetic electron transport chain of Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA. 54:1665-1669.
    • (1965) Proc. Natl. Acad. Sci. USA , vol.54 , pp. 1665-1669
    • Gorman, D.S.1    Levine, R.P.2
  • 12
    • 0027097082 scopus 로고
    • Translocation and rotation of microtubules caused by multiple species of Chlamydomonas inner-arm dynein
    • Kagami, O., and R. Kamiya. 1992. Translocation and rotation of microtubules caused by multiple species of Chlamydomonas inner-arm dynein. J. Cell Sci. 103:653-664.
    • (1992) J. Cell Sci. , vol.103 , pp. 653-664
    • Kagami, O.1    Kamiya, R.2
  • 13
    • 0027851766 scopus 로고
    • Isolation of two species of Chlamydomonas reinhardtii flagellar mutants, ida5 and ida6, that lack a newly identified heavy chain of the inner dynein arm
    • Kato, T., O. Kagami, T. Yagi, and R. Kamiya. 1993. Isolation of two species of Chlamydomonas reinhardtii flagellar mutants, ida5 and ida6, that lack a newly identified heavy chain of the inner dynein arm. Cell Struct. Funct. 18: 371-377.
    • (1993) Cell Struct. Funct. , vol.18 , pp. 371-377
    • Kato, T.1    Kagami, O.2    Yagi, T.3    Kamiya, R.4
  • 14
    • 0025117612 scopus 로고
    • High-frequency nuclear transformation of Chlamydomonas reinhardtii
    • Kindle, K.L. 1990. High-frequency nuclear transformation of Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. USA. 87:1228-1232.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1228-1232
    • Kindle, K.L.1
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0029047003 scopus 로고
    • Ida4-1, ida4-2, and ida4-3 are intron splicing mutations affecting the locus encoding p28, a light chain of Chlamydomonas axonemal inner dynein arms
    • LeDizet, M., and G. Piperno. 1995. ida4-1, ida4-2, and ida4-3 are intron splicing mutations affecting the locus encoding p28, a light chain of Chlamydomonas axonemal inner dynein arms. Mol. Biol. Cell. 6:713-723.
    • (1995) Mol. Biol. Cell. , vol.6 , pp. 713-723
    • LeDizet, M.1    Piperno, G.2
  • 17
    • 0026783380 scopus 로고
    • A vertebrate actin-related protein is a component of a multisubunit complex involved in microtubule-based vesicle motility
    • Lees-Miller, J.P., D.M. Helfman, and T.A. Schroer. 1992. A vertebrate actin-related protein is a component of a multisubunit complex involved in microtubule-based vesicle motility. Nature (Lond.). 359:244-246.
    • (1992) Nature (Lond.) , vol.359 , pp. 244-246
    • Lees-Miller, J.P.1    Helfman, D.M.2    Schroer, T.A.3
  • 18
    • 0023803882 scopus 로고
    • Two monoclonal antibodies to actin: One muscle selective and one generally reactive
    • Lessard, J.L. 1988. Two monoclonal antibodies to actin: one muscle selective and one generally reactive. Cell Motil. Cytoskeleton. 10:349-362.
    • (1988) Cell Motil. Cytoskeleton. , vol.10 , pp. 349-362
    • Lessard, J.L.1
  • 19
    • 0011094603 scopus 로고
    • Monoclonal antibodies against myofibrillar components of rat skeletal muscle decorate the intermediate filaments of cultured cells
    • Lin, J.J. 1981. Monoclonal antibodies against myofibrillar components of rat skeletal muscle decorate the intermediate filaments of cultured cells. Proc. Natl. Acad. Sci. USA. 78:2335-2339.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 2335-2339
    • Lin, J.J.1
  • 20
    • 1342296319 scopus 로고
    • Flagellar mutants of Chlamydomonas: Study of radial spoke-defective strains by dikaryon and revertant analysis
    • Luck, D.J.L., G. Piperno, Z. Ramanis, and B. Huang. 1977. Flagellar mutants of Chlamydomonas: study of radial spoke-defective strains by dikaryon and revertant analysis. Proc. Natl. Acad. Sci. USA. 74:3456-3460.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 3456-3460
    • Luck, D.J.L.1    Piperno, G.2    Ramanis, Z.3    Huang, B.4
  • 21
    • 0020517178 scopus 로고
    • Number and organization of actin-related sequences in the mouse genome
    • Minty, A.J., S. Alonso, J.L. Guenet, and M.E. Buckingham. 1983. Number and organization of actin-related sequences in the mouse genome. J. Mol. Biol. 167:77-101.
    • (1983) J. Mol. Biol. , vol.167 , pp. 77-101
    • Minty, A.J.1    Alonso, S.2    Guenet, J.L.3    Buckingham, M.E.4
  • 22
    • 0028347905 scopus 로고
    • Immunological detection of actin in the 14S ciliary dynein of Tetrahymena
    • Muto, E., M. Edamatsu, M, Hirono, and R. Kamiya. 1994. Immunological detection of actin in the 14S ciliary dynein of Tetrahymena. FEBS Lett. 343: 173-177.
    • (1994) FEBS Lett. , vol.343 , pp. 173-177
    • Muto, E.1    Edamatsu, M.2    Hirono, M.3    Kamiya, R.4
  • 23
    • 0024519019 scopus 로고
    • Coordinate accumulation of troponin subunits in chicken breast muscle
    • Nakamura, M., H. Imai, and T. Hirabayashi. 1989. Coordinate accumulation of troponin subunits in chicken breast muscle. Dev. Biol. 132:389-397.
    • (1989) Dev. Biol. , vol.132 , pp. 389-397
    • Nakamura, M.1    Imai, H.2    Hirabayashi, T.3
  • 25
    • 0023554250 scopus 로고
    • Cyclic AMP functions as a primary sexual signal in gametes of Chlamydomonas reinhardtii
    • Pasquale, S.M., and U.W. Goodenough. 1987. Cyclic AMP functions as a primary sexual signal in gametes of Chlamydomonas reinhardtii. J. Cell Biol. 105:2279-2292.
    • (1987) J. Cell Biol. , vol.105 , pp. 2279-2292
    • Pasquale, S.M.1    Goodenough, U.W.2
  • 26
    • 0029164398 scopus 로고
    • Regulation of dynein activity within Chlamydomonas flagella
    • Piperno, G., 1995. Regulation of dynein activity within Chlamydomonas flagella. Cell Motil. Cytoskeleton. 32: 103-105.
    • (1995) Cell Motil. Cytoskeleton. , vol.32 , pp. 103-105
    • Piperno, G.1
  • 27
    • 0018786478 scopus 로고
    • An actin-like protein is a component of axonemes from Chlamydomonas flagella
    • Piperno, G. and D.J.L. Luck. 1979. An actin-like protein is a component of axonemes from Chlamydomonas flagella. J. Biol. Chem. 254:2187-2190.
    • (1979) J. Biol. Chem. , vol.254 , pp. 2187-2190
    • Piperno, G.1    Luck, D.J.L.2
  • 28
    • 0025019981 scopus 로고
    • Three distinct inner dynein arms in Chlamydomonas flagella: Molecular composition and location in the axoneme
    • Piperno, G., Z. Ramanis, E.F. Smith, and W.S. Sale. 1990. Three distinct inner dynein arms in Chlamydomonas flagella: molecular composition and location in the axoneme. J. Cell Biol. 110:379-389.
    • (1990) J. Cell Biol. , vol.110 , pp. 379-389
    • Piperno, G.1    Ramanis, Z.2    Smith, E.F.3    Sale, W.S.4
  • 29
    • 0022571599 scopus 로고
    • Homology of egg and flagellar dynein. Comparison of ATP-binding sites and primary structure
    • Pratt, M.M. 1986. Homology of egg and flagellar dynein. Comparison of ATP-binding sites and primary structure. J. Biol. Chem. 261:956-964.
    • (1986) J. Biol. Chem. , vol.261 , pp. 956-964
    • Pratt, M.M.1
  • 30
    • 0022361156 scopus 로고
    • Organization of the actin multigene family of Dictyostelium discoideum and analysis of variability in the protein coding regions
    • Romans, P., and R.A. Firtel. 1985. Organization of the actin multigene family of Dictyostelium discoideum and analysis of variability in the protein coding regions. J. Mol. Biol. 186:321-335.
    • (1985) J. Mol. Biol. , vol.186 , pp. 321-335
    • Romans, P.1    Firtel, R.A.2
  • 31
    • 1842320380 scopus 로고
    • Nutritional studies with Chlamydomonas reinhardtii
    • Sager, R., and S. Granick. 1953. Nutritional studies with Chlamydomonas reinhardtii. Ann. NY Acad. Sci. 466:18-30.
    • (1953) Ann. NY Acad. Sci. , vol.466 , pp. 18-30
    • Sager, R.1    Granick, S.2
  • 32
    • 0028304474 scopus 로고
    • Ultrastructural analysis of the dynactin complex: An actin-related protein is a component of a filament that resembles F-actin
    • Schafer, D.A., S.R. Gill, J.A. Cooper, J.E. Heuser, and T.A. Schroer. 1994. Ultrastructural analysis of the dynactin complex: an actin-related protein is a component of a filament that resembles F-actin. J. Cell Biol. 126:403-412.
    • (1994) J. Cell Biol. , vol.126 , pp. 403-412
    • Schafer, D.A.1    Gill, S.R.2    Cooper, J.A.3    Heuser, J.E.4    Schroer, T.A.5
  • 33
    • 0028146484 scopus 로고
    • New insights into the interaction of cytoplasmic dynein with the actin-related protein. Arp1
    • Schroer, T.A. 1994. New insights into the interaction of cytoplasmic dynein with the actin-related protein. Arp1. J. Cell Biol. 127:1-4.
    • (1994) J. Cell Biol. , vol.127 , pp. 1-4
    • Schroer, T.A.1
  • 35
    • 0019984409 scopus 로고
    • Lethal disruption of the yeast actin gene by integrative DNA transformation
    • Shortle, D., J.E. Haber, and D. Botstein. 1982. Lethal disruption of the yeast actin gene by integrative DNA transformation. Science (Wash. DC). 217:371-373.
    • (1982) Science (Wash. DC) , vol.217 , pp. 371-373
    • Shortle, D.1    Haber, J.E.2    Botstein, D.3
  • 36
    • 0030053332 scopus 로고    scopus 로고
    • Cloning and characterization of actin-encoding gene of Chlamydomonas reinhardtii
    • Sugase, Y., M. Hirono, K.L. Kindle, and R. Kamiya. 1996. Cloning and characterization of actin-encoding gene of Chlamydomonas reinhardtii. Gene (Amst.). 168:117-121.
    • (1996) Gene (Amst.) , vol.168 , pp. 117-121
    • Sugase, Y.1    Hirono, M.2    Kindle, K.L.3    Kamiya, R.4
  • 37
    • 0027451262 scopus 로고
    • Cloning of flagellar genes in Chlamydomonas reinhardtii by DNA insertional mutagenesis
    • Tam, L.W., and P.A. Lefebvre. 1993. Cloning of flagellar genes in Chlamydomonas reinhardtii by DNA insertional mutagenesis. Genetics. 135:375-384.
    • (1993) Genetics , vol.135 , pp. 375-384
    • Tam, L.W.1    Lefebvre, P.A.2
  • 38
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 39
    • 0022650756 scopus 로고
    • A small-scale five-hour procedure for isolating multiple samples of CsCl-purified DNA: Application to isolations from mammalian, insect, higher plant, algal, yeast, and bacterial sources
    • Weeks, D.P., N. Beerman, and O.M. Griffith. 1986. A small-scale five-hour procedure for isolating multiple samples of CsCl-purified DNA: application to isolations from mammalian, insect, higher plant, algal, yeast, and bacterial sources. Anal. Biochem. 152:376-385.
    • (1986) Anal. Biochem. , vol.152 , pp. 376-385
    • Weeks, D.P.1    Beerman, N.2    Griffith, O.M.3
  • 40
    • 0022962478 scopus 로고
    • Isolation of Chlamydomonas flagella and flagellar axonemes
    • Witman, G.B. 1986. Isolation of Chlamydomonas flagella and flagellar axonemes. Methods Enzymol. 134:280-290.
    • (1986) Methods Enzymol. , vol.134 , pp. 280-290
    • Witman, G.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.