Structure-function relationships in yeast tubulins

Molecular Biology of the Cell

Volumn 11, Issue 5, 2000, Pages 1887-1903

  Richards, Kristy L ^a   Anders, Kirk R ^a   Nogales, Eva ^b,c   Schwartz, Katja ^a   Downing, Kenneth H ^c   Botstein, David ^a  

^a STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TUBULIN; BENOMYL; BETA TUBULIN; BINDING PROTEIN;

ALLELE; AMINO ACID SUBSTITUTION; ARTICLE; LETHALITY; MICROTUBULE; NONHUMAN; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; STRUCTURE ACTIVITY RELATION; SUPERSENSITIVITY; TEMPERATURE SENSITIVE MUTANT; YEAST;

SACCHAROMYCES CEREVISIAE;

EID: 0034078729     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.11.5.1887     Document Type: Article

References (59)

1. Amberg, D.C., Basart, E., and Botstein, D. (1995). Defining protein interactions with yeast actin in vivo. Nat. Struct. Biol. 2, 28-35.
2. Arce, C.A., Hallak, M.E., Rodriguez, J.A., Barra, H.S., and Caputto, R. (1978). Capability of tubulin and microtubules to incorporate and to release tyrosine and phenylalanine and the effect of the incorporation of these amino acids on tubulin assembly. J. Neurochem. 31, 205-210.
3. Argarana, C.E., Barra, H.S., and Caputto, R. (1978). Release of [14C]tyrosine from tubulinyl-[14C]tyrosine by brain extract. Separation of a carboxypeptidase from rubulin-tyrosine ligase. Mol. Cell. Biochem. 19, 17-21.
4. Bai. C., and Elledge, S.J. (1996). Gene identification using the yeast two-hybrid system. Methods Enzymol. 273, 331-347.
5. Bairoch, A. (1991). PROSITE: a dictionary of sites and patterns in proteins. Nucleic Acids Res. 19, 2241-2246.
6. Barra, H.S., Arce, C.A., and Argarana, C.E. (1988). Posttranslational tyrosination/detyrosination of tubulin. Mol. Neurobiol. 2, 133-153.
7. Bass, S.H., Mulkerrin, M.G., and Wells, J.A. (1991). A systematic mutational analysis of hormone-binding determinants in the human growth hormone receptor. Proc. Natl. Acad. Sci. USA 88, 4498-4502.
8. Becker, D.M., and Guarente, L. (1991). High-efficiency transformation of yeast by electroporation. In: Methods in Enzymology, Guide to Yeast Genetics and Molecular Biology, vol. 194, ed. C. Guthrie and G.R. Fink, San Diego: Academic Press, 182-187.
9. Bennett, W.F., Paoni, N.F., Keyt, B.A., Botstein, D., Jones, A.J.S., Presta, L., Wurm, F.M., and Zoller, M.J. (1991). High resolution analysis of functional determinants on human tissue-type plasminogen activator. J. Biol. Chem 266, 5191-5201.
10. Bowman, S., et al. (1997). The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII. Nature 387, 90-93.
11. Buhr, T.L., and Dickman, M.B. (1994). Isolation, characterization, and expression of a second beta-tubulin-encoding gene from Colletotrichum gloeosporioides f. sp. aeschynomene. Appl. Environ. Microbiol. 60, 4155-4159.
12. Burke, D., Gasdaska, P., and Hartwell, L. (1989). Dominant effects of tubulin overexpression in Saccharomyces cerevisiae. Mol. Cell. Biol. 9, 1049-1059.
13. Burns, R.G. (1991). Alpha-, beta-, and gamma-tubulins: sequence comparisons and structural constraints. Cell Motil. Cytoskeleton 20, 181-189.
14. Cali, B.M., Doyle, T.C., Botstein, D., and Fink, G.R. (1998). Multiple functions for actin during filamentous growth of Saccharomyces cerevisiae. Mol. Biol. Cell 9, 1873-1889.
15. Cleveland, D.W., Joshi, H.C., and Murphy, D.B. (1990). Tubulin site interpretation. Nature 344, 389.
16. Cottingham, F.R., and Hoyt, M.A. (1997). Mitotic spindle positioning in Saccharomyces cerevisiae is accomplished by antagonistically acting microtubule motor proteins. J. Cell Biol. 138, 1041-1053.
17. Feierbach, B., Nogales, E., Downing, K.H., and Stearns, T. (1999). Alf1p, a CLIP-170 domain-containing protein, is functionally and physically associated with alpha-tubulin. J. Cell Biol. 144, 113-124.
18. Ferrin, T.E., Huang, C.C., Jarvis, L.E., and Langridge, R. (1988). The MIDAS Display System. J. Mol. Graph 6, 13-37.
19. Fujimura, M., Oeda, K., Inoue, H., and Kato, T. (1992). A single amino-acid substitution in the beta-tubulin gene of Neurospora confers both carbendazim resistance and diethofencarb sensitivity. Curr. Genet. 21, 399-404.
20. Gibbs, C.S., and Zoller, M.J. (1991). Rational scanning mutagenesis of a protein kinase identifies functional regions involved in catalysis and substrate interactions. J. Biol. Chem 266, 8923-8931.
21. Goldsmith, M., Yarbrough, L., and van der Kooy, D. (1995). Mechanics of motility: distinct dynein binding domains on alpha- and beta-tubulin. Biochem. Cell Biol. 73, 665-671.
22. Guex, N., and Peitsch, M.C. (1997). SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723.
23. Hirose, K., Lockhart, A., Cross, R.A., and Amos, L.A. (1995). Nucleotide-dependent angular change in kinesin motor domain bound to tubulin. Nature 376, 277-279.
24. Hoenger, A., Sablin, E.P., Vale, R.D., Fletterick, R.J., and Milligan, R.A. (1995). Three-dimensional structure of a tubulin-motor-protein complex. Nature 376, 271-274.
25. Huffaker, T.C., Thomas, J.H., and Botstein, D. (1988). Diverse effects of beta-tubulin mutations on microtubule formation and function. J. Cell Biol. 106, 1997-2010.
26. Huh, W.K., Lee, B.H., Kim, S.T., Kim, Y.R., Rhie, G.E., Baek, Y.W., Hwang, C.S., Lee, J.S., and Kang, S.O. (1998). D-Erythroascorbic acid is an important antioxidant molecule in Saccharomyces cerevisiae. Mol. Microbiol. 30, 895-903.
27. Hyams, J.S., and Lloyd, C.W. (1994). Microtubules. In: Modern Cell Biology, vol. 13, J.B. Harford (ed.), New York: Wiley-Liss.
28. Jacobs, C.W., Adams, A.E., Szaniszlo, P.J., and Pringle, J.R. (1988). Functions of microtubules in the Saccharomyces cerevisiae cell cycle. J. Cell Biol. 107, 1409-1426.
29. Jones, J.S., and Prakash, L. (1990). Yeast Saccharomyces cerevisiae selectable markers in pUC18 polylinkers. Yeast 6, 363-366.
30. Jung, M.K., Wilder, I.B., and Oakley, B.R. (1992). Amino acid alterations in the benA (beta-tubulin) gene of Aspergillus nidulans that confer benomyl resistance. Cell Motil. Cytoskeleton 22, 170-174.
31. Kassir, Y., and Simchen, G. (1991). Monitoring meiosis and sporulation in Saccharomyces cerevisiae. Methods Enzymol. 194, 94-110.
32. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
33. Kunkel, T.A., Roberts, J.D., and Zakour, R.A. (1987). Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154, 367-382.
34. Lappalainen, P., Fedorov, E.V., Fedorov, A.A., Almo, S.C., and Drubin, D.G. (1997). Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis. EMBO J. 16, 5520-5530.
35. Little, M., and Seehaus, T. (1988). Comparative analysis of tubulin sequences. Comp. Biochem. Physiol. 90, 655-670.
36. Machin, N.A., Lee, J.M., and Barnes, G. (1995). Microtubule stability in budding yeast: characterization and dosage suppression of a benomyl-dependent tubulin mutant. Mol. Biol. Cell 6, 1241-1259.
37. Miller, C.J., Doyle, T.C., Bobkova, E., Botstein, D., and Reisler, E. (1996). Mutational analysis of the role of hydrophobic residues in the 338-348 helix on actin in actomyosin interactions. Biochemistry 35, 3670-3676.
38. Neff, N.F., Thomas, J.H., Grisafi, P., and Botstein, D. (1983). Isolation of the beta-tubulin gene from yeast and demonstration of its essential function in vivo. Cell 33, 211-219.
39. Nogales, E., Downing, K.H., Amos, L.A., and Lowe, J. (1998a). Tubulin and FtsZ form a distinct family of GTPases. Nat. Struct. Biol. 5, 451-458.
40. Nogales, E., Whittaker, M., Milligan, R.A., and Downing, K.H. (1999). High-resolution model of the microtubule. Cell 96, 79-88.
41. Nogales, E., Wolf, S.G., and Downing, K.H. (1998b). Structure of the alpha beta tubulin dimer by electron crystallography. Nature 391, 199-203.
42. Park, S.Y., Jung, O.J., Chung, Y.R., and Lee, C.W. (1997). Isolation and characterization of a benomyl-resistant form of beta-tubulin-encoding gene from the phytopathogenic fungus Botryotinia fuckeliana. Mol. Cells 7, 104-109.
43. Pasqualone, D., and Huffaker, T.C. (1994). STU1, a suppressor of a beta-tubulin mutation, encodes a novel and essential component of the yeast mitotic spindle. J. Cell Biol. 127, 1973-1984.
44. Reijo, R.A., Cooper, E.M., Beagle, G.J., and Huffaker, T.C. (1994). Systematic mutational analysis of the yeast beta-tubulin gene. Mol. Biol. Cell 5, 29-43.
45. Rose, M.D., Winston, F., and Hieter, P. (1990). Methods in Yeast Genetics: A Laboratory Course Manual, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
46. Sambrook, J., Fritsch, E.F., and Maniatis, T. (1989). Molecular Cloning: A Laboratory Manual, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
47. Sayle, R.A., and Milner-White, E.J. (1995). RASMOL: biomolecular graphics for all. Trends Biochem. Sci. 20, 374.
48. Schatz, P.J., Pillus, L., Grisafi, P., Solomon, F., and Botstein, D. (1986a). Two functional alpha-tubulin genes of the yeast Saccharomyces cerevisiae encode divergent proteins. Mol. Cell. Biol. 6, 3711-3721.
49. Schatz, P.J., Solomon, F., and Botstein, D. (1986b). Genetically essential and nonessential alpha-rubulin genes specify functionally interchangeable proteins. Mol. Cell. Biol. 6, 3722-3733.
50. Schatz, P.J., Solomon, F., and Botstein, D. (1988). Isolation and characterization of conditional-lethal mutations in the TUB1 alpha-tubulin gene of the yeast Saccharomyces cerevisiae. Genetics 120, 681-695.
51. Schwartz, K., Richards, K., and Botstein, D. (1997). BIM1 encodes a microtubule-binding protein in yeast. Mol. Biol. Cell 8, 2677-2691.
52. Sherman, G., Rosenberry, T.L., and Sternlicht, H. (1983). Identification of lysine residues essential for microtubule assembly. Demonstration of enhanced reactivity during reductive methylation. J. Biol. Chem. 258, 2148-2156.
53. Sikorski, R.S., and Hieter, P. (1989). A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27.
54. Szasz, J., Yaffe, M.B., Elzinga, M., Blank, G.S., and Sternlicht, H. (1986). Microtubule assembly is dependent on a cluster of basic residues in alpha-tubulin. Biochemistry 25, 4572-4582.
55. Thomas, J.H. (1984). Genes Controlling the Mitotic Spindle and Chromosome Segregation in Yeast. Ph.D. Thesis. Cambridge, MA: Massachusetts Institute of Technology.
56. Thomas, J.H., Neff, N.F., and Botstein, D. (1985). Isolation and characterization of mutations in the beta-tubulin gene of Saccharomyces cerevisiae. Genetics 111, 715-734.
57. Vega, L.R., Fleming, J., and Solomon, F. (1998). An alpha-tubulin mutant destabilizes the heterodimer: phenotypic consequences and interactions with tubulin-binding proteins. Mol. Biol. Cell 9, 2349-2360.
58. Weinstein, B., and Solomon, F. (1990). Phenotypic consequences of rubulin overproduction in Saccharomyces cerevisiae: differences between alpha-tubulin and beta-tubulin. Mol. Cell. Biol. 10, 5295-5304.
59. Wertman, K.F., Drubin, D.G., and Botstein, D. (1992). Systematic mutational analysis of the yeast ACT1 gene. Genetics 132, 337-350.