메뉴 건너뛰기




Volumn 149, Issue 5, 2000, Pages 1097-1106

Polyglycylation of tubulin is essential and affects cell motility and division in Tetrahymena thermophila

Author keywords

Cilia; Cytoskeleton; Microtubules; Motility; Motor proteins

Indexed keywords

ALPHA TUBULIN; BETA TUBULIN;

EID: 0034729530     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.149.5.1097     Document Type: Article
Times cited : (110)

References (50)
  • 2
    • 0017903434 scopus 로고
    • 14C]-tyrosine by brain extract. Separation of a carboxypeptidase from tubulin tyrosine ligase
    • 14C]-tyrosine by brain extract. Separation of a carboxypeptidase from tubulin tyrosine ligase. Mol. Cell. Biochem. 19:17-22.
    • (1978) Mol. Cell. Biochem. , vol.19 , pp. 17-22
    • Argarana, C.E.1    Barra, H.S.2    Caputto, R.3
  • 3
    • 0026699541 scopus 로고
    • A broad molecular phylogeny of ciliates: Identification of major evolutionary trends and radiations within the phylum
    • Baroin-Tourancheau, A., P. Delgado, R. Perasso, and A. Adoutle. 1992. A broad molecular phylogeny of ciliates: identification of major evolutionary trends and radiations within the phylum. Proc. Natl. Acad. Sci. USA. 89: 9764-9768.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9764-9768
    • Baroin-Tourancheau, A.1    Delgado, P.2    Perasso, R.3    Adoutle, A.4
  • 4
    • 0032517865 scopus 로고    scopus 로고
    • Centriole disassembly in vivo and its effect on centrosome structure and function in vertebrate cells
    • Bobinnec, Y., A. Khodjakov, L.M. Mir. C.L. Rieder, B. Eddé, and M. Bornens. 1998. Centriole disassembly in vivo and its effect on centrosome structure and function in vertebrate cells. J. Cell Biol. 143:1575-1589.
    • (1998) J. Cell Biol. , vol.143 , pp. 1575-1589
    • Bobinnec, Y.1    Khodjakov, A.2    Mir, L.M.3    Rieder, C.L.4    Eddé, B.5    Bornens, M.6
  • 5
    • 0028210453 scopus 로고
    • Glutamylated tubulin probed in ciliates with the monoclonal antibody GT335
    • Bré, M.H., B. de Nechaud, A. Wolff, and A. Fleury, 1994. Glutamylated tubulin probed in ciliates with the monoclonal antibody GT335. Cell Motil. Cytoskelet. 27:337-349.
    • (1994) Cell Motil. Cytoskelet. , vol.27 , pp. 337-349
    • Bré, M.H.1    De Nechaud, B.2    Wolff, A.3    Fleury, A.4
  • 7
    • 0031665835 scopus 로고    scopus 로고
    • Tubulin polyglycylation: Differential posttranslational modification of dynamic cytoplasmic and stable axonemal microtubules in Paramecium
    • Bré. M.H., V. Redeker, J. Vinh, J. Rossier, and N. Levilliers. 1998. Tubulin polyglycylation: differential posttranslational modification of dynamic cytoplasmic and stable axonemal microtubules in Paramecium. Mol. Biol. Cell. 9:2655-2665.
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 2655-2665
    • Bré, M.H.1    Redeker, V.2    Vinh, J.3    Rossier, J.4    Levilliers, N.5
  • 9
    • 0030983113 scopus 로고    scopus 로고
    • Posttranslational modification of tubulin by palmitoylation. I. in vivo and cell-free studies
    • Caron, J.M. 1997. Posttranslational modification of tubulin by palmitoylation. I. In vivo and cell-free studies. Mol. Biol. Cell. 8:621-636.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 621-636
    • Caron, J.M.1
  • 11
    • 0023606681 scopus 로고
    • Nucleotide sequence and expression of two beta-tubulin genes in Stylonychia lemnae
    • Conzelmann, K.K., and E. Helftenbein. 1987. Nucleotide sequence and expression of two beta-tubulin genes in Stylonychia lemnae. J. Mol. Biol. 198:643-653.
    • (1987) J. Mol. Biol. , vol.198 , pp. 643-653
    • Conzelmann, K.K.1    Helftenbein, E.2
  • 12
    • 0032128172 scopus 로고    scopus 로고
    • Tubulin and FtsZ structures: Functional and therapeutic implications
    • Desai, A., and T.I. Mitchison. 1998. Tubulin and FtsZ structures: functional and therapeutic implications. Bioessays 20:523-527.
    • (1998) Bioessays , vol.20 , pp. 523-527
    • Desai, A.1    Mitchison, T.I.2
  • 13
  • 14
    • 0026760616 scopus 로고
    • The β-tubulin genes of Paramecium are interrupted by two 27 bp introns
    • Dupuis, P. 1992. The β-tubulin genes of Paramecium are interrupted by two 27 bp introns. EMBO (Eur. Mol. Biol. Organ.) J. 11:3713-3719.
    • (1992) EMBO (Eur. Mol. Biol. Organ.) J. , vol.11 , pp. 3713-3719
    • Dupuis, P.1
  • 15
    • 0030469075 scopus 로고    scopus 로고
    • The tubulin gene family of Paramecium: Characterization and expression of the alpha PT1 and alpha PT2 genes which code for alpha-tubulins with unusual C-terminal amino acids. GLY and ALA
    • Dupuis-Williams, P., C. Klotz, H. Mazarguil, and J. Beisson. 1996. The tubulin gene family of Paramecium: characterization and expression of the alpha PT1 and alpha PT2 genes which code for alpha-tubulins with unusual C-terminal amino acids. GLY and ALA. Biol. Cell. 87:83-93.
    • (1996) Biol. Cell. , vol.87 , pp. 83-93
    • Dupuis-Williams, P.1    Klotz, C.2    Mazarguil, H.3    Beisson, J.4
  • 17
    • 0015385595 scopus 로고
    • Rat brain microtubule protein: Purification and determination of covalently bound phosphate and carbohydrate
    • Eipper, B.A. 1972. Rat brain microtubule protein: purification and determination of covalently bound phosphate and carbohydrate. Proc. Natl Acad. Sci. USA. 69:2283-2287.
    • (1972) Proc. Natl Acad. Sci. USA , vol.69 , pp. 2283-2287
    • Eipper, B.A.1
  • 18
    • 0027234817 scopus 로고
    • Tissue-specific microtubule functions in Drosophila spermatogenesis require the ß2 isotype-specific carboxy terminus
    • Fackenthal, J.D., F.R. Turner, and E.C. Raff. 1993. Tissue-specific microtubule functions in Drosophila spermatogenesis require the ß2 isotype-specific carboxy terminus. Dev. Biol. 158:213-227.
    • (1993) Dev. Biol. , vol.158 , pp. 213-227
    • Fackenthal, J.D.1    Turner, F.R.2    Raff, E.C.3
  • 19
    • 0026750596 scopus 로고
    • Molecular phylogeny of ciliates: What does it tell us about the evolution of the cytoskeleton and of developmental strategies?
    • Fleury, A., P. Delgado, F. Iftode, and A. Adoutte. 1992. Molecular phylogeny of ciliates: what does it tell us about the evolution of the cytoskeleton and of developmental strategies? Dev. Genet. 13:247-254.
    • (1992) Dev. Genet. , vol.13 , pp. 247-254
    • Fleury, A.1    Delgado, P.2    Iftode, F.3    Adoutte, A.4
  • 20
    • 0027298836 scopus 로고
    • Perspectives on tubulin isotype function and evolution based on the observations that Tetrahymena thermophila microtubules contain a single α- and β-tubulin
    • Gaertig, J., T.H. Thatcher, K.E. McGrath, R.C. Callahan, and M.A. Gorovsky. 1993. Perspectives on tubulin isotype function and evolution based on the observations that Tetrahymena thermophila microtubules contain a single α- and β-tubulin. Cell Motil. Cytokelet. 25:243-253.
    • (1993) Cell Motil. Cytokelet. , vol.25 , pp. 243-253
    • Gaertig, J.1    Thatcher, T.H.2    McGrath, K.E.3    Callahan, R.C.4    Gorovsky, M.A.5
  • 21
    • 0028661172 scopus 로고
    • High frequency vector-mediated transformation and gene replacement in Tetrahymena
    • Gaertig, J., I., Gu, B. Hai, and M.A. Gorovsky, 1994a. High frequency vector-mediated transformation and gene replacement in Tetrahymena. Nucleic Acids Res. 22:5391-5398.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5391-5398
    • Gaertig, J.1    Gu, I.2    Hai, B.3    Gorovsky, M.A.4
  • 22
    • 0028293627 scopus 로고
    • Electroporation-mediated replacement of a positively and negatively selectable ß-tubulin gene in Tetrahymena thermophila
    • Gaertig, J., T.H. Thatcher, L. Gu, and M.A. Gorovsky. 1994b. Electroporation-mediated replacement of a positively and negatively selectable ß-tubulin gene in Tetrahymena thermophila. Proc. Natl. Acad. Sci. USA. 91:4549-4553.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4549-4553
    • Gaertig, J.1    Thatcher, T.H.2    Gu, L.3    Gorovsky, M.A.4
  • 23
    • 0029035184 scopus 로고
    • Acetylation of lysine 40 in α-tubulin is not essential in Tetrahymena thermophil
    • Gaertig, J., M.A. Cruz, J. Bowen, L. Gu, D.G. Pennock, and M.A. Gorovsky, 1995. Acetylation of lysine 40 in α-tubulin is not essential in Tetrahymena thermophil. J. Cell Biol. 129:1301-1310.
    • (1995) J. Cell Biol. , vol.129 , pp. 1301-1310
    • Gaertig, J.1    Cruz, M.A.2    Bowen, J.3    Gu, L.4    Pennock, D.G.5    Gorovsky, M.A.6
  • 24
    • 0031029916 scopus 로고    scopus 로고
    • Germ-line knockout heterokaryons of an essential alphn-tubulin gene enable high-frequency gene replacement and a test of gene transfer from somatic to germ-line nuclei in Tetrahymena thermophila
    • Hai, B., and M.A. Gorovsky. 1997. Germ-line knockout heterokaryons of an essential alphn-tubulin gene enable high-frequency gene replacement and a test of gene transfer from somatic to germ-line nuclei in Tetrahymena thermophila. Proc. Natl. Acad. Sci. USA. 94:1310-1315.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1310-1315
    • Hai, B.1    Gorovsky, M.A.2
  • 25
    • 0029795642 scopus 로고    scopus 로고
    • Three-dimensional cryoelectron microscopy of dimeric kinesins and ned motor domains on microtubules
    • Hirose, K., A. Lockhart, R.A. Cross, and L. Amos. 1996. Three-dimensional cryoelectron microscopy of dimeric kinesins and ned motor domains on microtubules. Proc. Natl. Acad. Sci. USA. 93:539-9544.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 539-9544
    • Hirose, K.1    Lockhart, A.2    Cross, R.A.3    Amos, L.4
  • 26
    • 0027515395 scopus 로고
    • Transformation of Tetrahymena thermophila by microinjection of a foreign gene
    • Kahn, R.W., B.H. Andersen, and C.F. Brunk. 1993. Transformation of Tetrahymena thermophila by microinjection of a foreign gene. Proc. Natl. Acad. Sci. USA. 90:9295-9299.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9295-9299
    • Kahn, R.W.1    Andersen, B.H.2    Brunk, C.F.3
  • 27
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel. T.A. 1985. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA. 82:488-492.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 28
    • 0021993649 scopus 로고
    • Chlamydomonas α-tubulin is posttranslationally modified by acelylation on the E-amino group of a lysine
    • L'Hernault, S.W., and J.L. Rosenbaum. 1985. Chlamydomonas α-tubulin is posttranslationally modified by acelylation on the E-amino group of a lysine. Biochemistry. 24:473-478.
    • (1985) Biochemistry , vol.24 , pp. 473-478
    • L'Hernault, S.W.1    Rosenbaum, J.L.2
  • 29
    • 0029125382 scopus 로고
    • Monoclonal and polyclonal antibodies detect a new type of post-translational modification of axonemal tubulin
    • Levilliers, N., A. Fleury, and A.M. Hill. 1995. Monoclonal and polyclonal antibodies detect a new type of post-translational modification of axonemal tubulin. J. Cell Sci. 108:3013-3028.
    • (1995) J. Cell Sci. , vol.108 , pp. 3013-3028
    • Levilliers, N.1    Fleury, A.2    Hill, A.M.3
  • 30
    • 0030709242 scopus 로고    scopus 로고
    • Multiple forms of tubulin: Different gene products and covalent modifications
    • Luduena, R.F. 1998. Multiple forms of tubulin: different gene products and covalent modifications. Int. Rev. Cytol. 178:207-274.
    • (1998) Int. Rev. Cytol. , vol.178 , pp. 207-274
    • Luduena, R.F.1
  • 31
    • 0031039519 scopus 로고    scopus 로고
    • Tubulin post-translational modifications enzymes and their mechanisms of action
    • MacRae, T.H. 1997. Tubulin post-translational modifications enzymes and their mechanisms of action. Eur. J. Biochem. 244:265-278.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 265-278
    • MacRae, T.H.1
  • 33
    • 0029966076 scopus 로고    scopus 로고
    • Posttranslational modifications in the C-terminal tail of axonemal tubulin from sea urchin sperm
    • Mary, J., V. Redeker, J.-P. Le Caer, J. Rossier, and J.M. Schmitter. 1996. Posttranslational modifications in the C-terminal tail of axonemal tubulin from sea urchin sperm. J. Biol. Chem. 271:9928-9933.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9928-9933
    • Mary, J.1    Redeker, V.2    Le Caer, J.-P.3    Rossier, J.4    Schmitter, J.M.5
  • 34
    • 0028066701 scopus 로고
    • Regulation and evolution of the single alpha-tubulin gene of the ciliate Tetrahymena thermophila
    • McGrath, K.R., S.M. Yu, D.P. Heruth, A.A. Kelly, and M.A. Gorovsky. 1994. Regulation and evolution of the single alpha-tubulin gene of the ciliate Tetrahymena thermophila. Cell Motil. Cytoskelet. 27:272-283.
    • (1994) Cell Motil. Cytoskelet. , vol.27 , pp. 272-283
    • McGrath, K.R.1    Yu, S.M.2    Heruth, D.P.3    Kelly, A.A.4    Gorovsky, M.A.5
  • 35
    • 0029757769 scopus 로고    scopus 로고
    • The a and B tubules of the outer doublets of sea urchin sperm axonemes are composed of different tubulin variants
    • Multigner, L., I. Pignot-Paintrand, Y. Saoudi, D. Job, U. Plessmann, M. Rüdiger, and K. Weber. 1996. The A and B tubules of the outer doublets of sea urchin sperm axonemes are composed of different tubulin variants. Biochemistry, 35:10862-10871.
    • (1996) Biochemistry , vol.35 , pp. 10862-10871
    • Multigner, L.1    Pignot-Paintrand, I.2    Saoudi, Y.3    Job, D.4    Plessmann, U.5    Rüdiger, M.6    Weber, K.7
  • 36
    • 0342872003 scopus 로고    scopus 로고
    • Mutation of a gene for a Drosophila kinesin-like protein. KLP38B. leads to a failure of cytokinesis
    • Ohkura, H., T. Torok, G. Tick, J. Hoheisel, I. Kiss, and D.M. Glover, 1997. Mutation of a gene for a Drosophila kinesin-like protein. KLP38B. leads to a failure of cytokinesis. J. Cell Sci. 110:945-954.
    • (1997) J. Cell Sci. , vol.110 , pp. 945-954
    • Ohkura, H.1    Torok, T.2    Tick, G.3    Hoheisel, J.4    Kiss, I.5    Glover, D.M.6
  • 37
    • 0017101041 scopus 로고
    • Induction and isolation of mutants in Tetrahymena
    • D.M. Prescott, editor Academic Press, New York
    • Orias, L., and P.J. Bruns. 1976. Induction and isolation of mutants in Tetrahymena. In Methods in Cell Biology. Vol. 13, D.M. Prescott, editor Academic Press, New York. 247-282.
    • (1976) Methods in Cell Biology , vol.13 , pp. 247-282
    • Orias, L.1    Bruns, P.J.2
  • 38
    • 0031877351 scopus 로고    scopus 로고
    • Cytokinesis and midzone microtubule organization in Caenorhabditis elegant require the kinesin-like protein ZEN-4
    • Raich, W.B., A.N. Moran, J.H. Rothman, and J. Hardin. 1998. Cytokinesis and midzone microtubule organization in Caenorhabditis elegant require the kinesin-like protein ZEN-4. Mol. Biol. Cell. 9:2037-2049.
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 2037-2049
    • Raich, W.B.1    Moran, A.N.2    Rothman, J.H.3    Hardin, J.4
  • 39
    • 0026447041 scopus 로고
    • Structure ot tubulin C-terminal domain obtained by subtilisin treatment. the major α- and β-tubulin isotypes lrom pig brain are glutamylated
    • Redeker, V., R. Melki, D. Promé, J.-P. Le Caer, and J. Rossier. 1992. Structure ot tubulin C-terminal domain obtained by subtilisin treatment. The major α- and β-tubulin isotypes lrom pig brain are glutamylated. FEBS (Fed. Eur. Biochem. Soc.) Lett. 313:185-192.
    • (1992) FEBS (Fed. Eur. Biochem. Soc.) Lett. , vol.313 , pp. 185-192
    • Redeker, V.1    Melki, R.2    Promé, D.3    Le Caer, J.-P.4    Rossier, J.5
  • 43
    • 0013589899 scopus 로고    scopus 로고
    • Cilia: Structure and molecular biology
    • K. Hausmann and P.C. Bradbury, editors. Gustav Fischer. Stuttgart
    • Satir, P., and K.L. Barkalow, 1996. Cilia: structure and molecular biology. In Ciliates: Cells as Organism. K. Hausmann and P.C. Bradbury, editors. Gustav Fischer. Stuttgart. 355-377.
    • (1996) Ciliates: Cells as Organism , pp. 355-377
    • Satir, P.1    Barkalow, K.L.2
  • 44
    • 0002309878 scopus 로고
    • Why do tubulin gene families lack diversity in flagellate/ciliate protists?
    • Silflow, C.D. 1991. Why do tubulin gene families lack diversity in flagellate/ciliate protists? Protoplasma. 164:9-11.
    • (1991) Protoplasma , vol.164 , pp. 9-11
    • Silflow, C.D.1
  • 45
    • 0027405349 scopus 로고
    • Recombinant kinesin motor domain binds to β-tubulin and decorates microtubules with a B surface lattice
    • Song, Y.-H., and E. Mandelkow. 1993. Recombinant kinesin motor domain binds to β-tubulin and decorates microtubules with a B surface lattice. Proc. Natl. Acad. Sci. USA. 90:1671-1675.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1671-1675
    • Song, Y.-H.1    Mandelkow, E.2
  • 46
    • 0345510489 scopus 로고
    • Multiple forms of tubulin in the cilia and cytoplasm of Tetrahymena thermophila
    • Suprenant, K.A., E. Hays, L. LeCluyse, and W.L. Dentler. 1985. Multiple forms of tubulin in the cilia and cytoplasm of Tetrahymena thermophila. Proc. Natl. Acad. Sci. USA. 82:6908-6912.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6908-6912
    • Suprenant, K.A.1    Hays, E.2    LeCluyse, L.3    Dentler, W.L.4
  • 47
    • 0027217068 scopus 로고
    • A transformation vector for Dictyostelium discoideum with a new selectable marker bsr
    • Sutoh, K. 1993. A transformation vector for Dictyostelium discoideum with a new selectable marker bsr. Plasmid. 30:150-154.
    • (1993) Plasmid. , vol.30 , pp. 150-154
    • Sutoh, K.1
  • 48
    • 0033537641 scopus 로고    scopus 로고
    • Structural characterization by tandem spectroscopy of the posttranslational modifications of tubulin
    • Vinh, J., J.I. Langridge, M.-H. Bré, N. Levilliers, V. Redeker, D. Loyaux, and J. Rossier. 1999. Structural characterization by tandem spectroscopy of the posttranslational modifications of tubulin. Biochemistry. 38:3133-3139.
    • (1999) Biochemistry , vol.38 , pp. 3133-3139
    • Vinh, J.1    Langridge, J.I.2    Bré, M.-H.3    Levilliers, N.4    Redeker, V.5    Loyaux, D.6    Rossier, J.7
  • 49
    • 0030576986 scopus 로고    scopus 로고
    • Polyglyeylation of tubulin in the diplomonad Giardia lamblia, one of the oldest eukaryotes
    • Weber, K., A. Schneider, N. Muller, and U. Plessman. 1996. Polyglyeylation of tubulin in the diplomonad Giardia lamblia, one of the oldest eukaryotes. FEBS (Fed. Eur. Biochem. Soc.) Lett. 393:27-30.
    • (1996) FEBS (Fed. Eur. Biochem. Soc.) Lett. , vol.393 , pp. 27-30
    • Weber, K.1    Schneider, A.2    Muller, N.3    Plessman, U.4
  • 50
    • 0028968891 scopus 로고
    • The Drosophila kinesin-like protein KLP3a is a midbody component required for central spindle assembly and initiation of cytokinesis
    • Williams, B.C., M.F. Riedy, E.V. Williams, M. Gatti, and M.L. Goldberg, 1995. The Drosophila kinesin-like protein KLP3A is a midbody component required for central spindle assembly and initiation of cytokinesis. J. Cell Biol. 129:709-723.
    • (1995) J. Cell Biol. , vol.129 , pp. 709-723
    • Williams, B.C.1    Riedy, M.F.2    Williams, E.V.3    Gatti, M.4    Goldberg, M.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.