Sto1p, a fission yeast protein similar to tubulin folding Cofactor E, plays an essential role in mitotic microtubule assembly

Journal of Cell Science

Volumn 112, Issue 12, 1999, Pages 1979-1988

  Grishchuk, Ekaterina L ^a   McIntosh, J Richard ^b  

^a INSTITUTE OF GENE BIOLOGY   (Russian Federation)

^b UNIVERSITY OF COLORADO   (United States)

Author keywords

Chaperone; Fission yeast; Leucine rich repeat; Microtubule; Tubulin folding

Indexed keywords

COFACTOR E; DNA; FUNGAL PROTEIN; TUBULIN; UNCLASSIFIED DRUG;

ARTICLE; CHROMOSOME CONDENSATION; CONTROLLED STUDY; CYTOSKELETON; DNA SYNTHESIS; FUNGUS MUTANT; GENE DELETION; MICROTUBULE ASSEMBLY; MITOSIS INHIBITION; MITOSIS SPINDLE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SCHIZOSACCHAROMYCES POMBE;

AMINO ACID SEQUENCE; CELL DIVISION; CELLS, CULTURED; FUNGAL PROTEINS; GENE DELETION; GENE EXPRESSION REGULATION, FUNGAL; MICROTUBULES; MITOSIS; MOLECULAR SEQUENCE DATA; PHENOTYPE; PROTEIN FOLDING; SCHIZOSACCHAROMYCES; SCHIZOSACCHAROMYCES POMBE PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TUBULIN;

FUNGI; SCHIZOSACCHAROMYCES POMBE;

EID: 0032770140     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (39)

1. Adachi, Y., Toda, T., Niwa, O. and Yanagida, M. (1986). Differential expressions of essential and nonessential α-tubulin genes in Schizosaccharomyces pombe. Mol. Cell Biol. 6, 2168-2178.
2. Alfa, C., Fantes, P., Hyams, J., McLeod, M. and Warbrick, E. (1993). Experiments with Fission Yeast. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
3. Alvarez, P., Smith, A., Fleming, J. and Solomon, F. (1998). Modulation of tubulin polypeptide ratios by the yeast protein Pac10p. Genetics 149, 857-864.
4. Archer, J. E., Vega, L. R. and Solomon, F. (1995) Rb12p, a yeast protein that binds to β-tubulin and participates in microtubule function in vivo. Cell 82, 425-434.
5. Archer, J. E., Magendantz, M., Vega, L. R. and Solomon, F. (1998). Formation and function of the Rb12p-β-tubulin complex. Mol. Cell Biol. 18, 1757-1762.
6. Barbet, N., Muriel, W. J. and Carr, A. M. (1992). Versatile shuttle vectors and genomic libraries for use with Schizosaccharomyces pombe. Gene 114, 59-66.
7. Basi, G., Schmid, E. and Maundrell, K. (1993). TATA box mutations in the Schizosaccharomyces pombe nmtl promoter affect transcription efficiency but not the transcription start point or thiamine repressibility. Gene 123, 131-136.
8. Beinhauer, J. D., Hagan, I. M., Hegemann, J. H and Fleig, U. (1997). Mal3, the fission yeast homologue of the human APC-interacting protein EB-1 is required for microtubule integrity and the maintenance of cell form. J. Cell Biol. 139, 717-728.
9. Byers, B. and Goetsch, L. (1975). Behavior of spindles and spindle plaques in the cell cycle and conjugation of Saccharomyces cerevisiae. J. Bacteriol. 124, 511-523.
10. Elble, R. (1992). A simple and efficient procedure for transformation of yeasts. Biotechniques 13, 18-20.
11. Gao, Y., Melki, R., Walden, P. D., Lewis, S. A., Ampe, C., Rommelaere, H., Vandekerckhove, J. and Cowan, N. J. (1994). A novel cochaperonin that modulates the ATPase activity of cytoplasmic chaperonin. J. Cell Biol. 125, 989-996.
12. Geiser, J. R., Schott, E. J., Kingsbury, T. J., Cole, N. B., Totis, L. J., Bhattacharyya, G., He, L. and Hoyt, M. A. (1997). Saccharomyces cerevisiae genes required in the absence of the CIN8-encoded spindle motor act in functionally diverse mitotic pathways. Mol. Biol. Cell. 8, 1035-1050.
13. Geissler, S., Siegers, K. and Schiebel, E. (1998). A novel protein complex promoting formation of functional α-and γ-tubulin. EMBO. J. 17, 952-966.
14. +, a novel Schizosaccharomyces pombe gene important for microtubule integrity. Genetics 149, 1251-1264.
15. Hagan, I. M. (1998). The fission yeast microtubule cytoskeleton. J. Cell Sci. 111, 1603-1612.
16. Hagan, I. M. and Hyams, J. S. (1988). The use of cell division cycle mutants to investigate the control of microtubule distribution in the fission yeast Schizosaccharomyces pombe. J. Cell Sci. 89, 343-357.
17. Hiraoka, Y., Toda, T. and Yanagida, M. (1984). The NDA3 gene of fission yeast encodes β-tubulin: a cold-sensitive nda3 mutation reversibly blocks spindle formation and chromosome movement in mitosis. Cell 39, 349-358.
18. Hirata, D., Masuda, H., Eddison, M. and Toda, T. (1998). Essential role of tubulin-folding cotactor D in microtubule assembly and its association with microtubules in fission yeast. EMBO. J. 17, 658-666.
19. Hoheisel, J. D., Maier, E., Mott, R., McCarthy, L., Grigoriev, A. V., Schalkwyk, L. C., Nizetic, D., Francis, F. and Lehrach, H. (1993). High resolution cosmid and Pl maps spanning the 14 Mb genome of the fission yeasts S. pombe. Cell 73, 109-120.
20. Hoyt, M. A., Stearns, T. and Botstein, D. (1990). Chromosome instability mutants of Saccharomyces cerevisiae that are defective in microtubule-mediated processes. Mol. Cell. Biol. 10, 223-234.
21. Hoyt, M. A., Macke, J. P., Roberts, B. T. and Geiser, J. R. (1997). Saccharomyces cerevisiae PAC2 functions with CIN1, 2 and 4 in a pathway leading to normal microtubule stability. Genetics 146, 849-857.
22. Innis, M. A., Gelfand, D. H., Sninsky, J. J. and White, T. J. (1990). PCR protocols: A guide to Methods and Applications. Academic Press Inc., NY.
23. Kobe, B. and Deisenhofer, J. (1994). The leucine-rich repeat: a versatile binding motif. Trends Biochem. Sci. 19, 415-421.
24. Mata, J. and Nurse, P. (1997). teal and the microtubular cytoskeleton are important for generating global spatial order within the fission yeast cell. Cell 89, 939-949.
25. Maundrell, K. (1993). Thiamine-repressible expression vectors pREP and pRIP for fission yeast. Gene 123, 127-130.
26. Melki, R., Rommelaere, H., Leguy, R., Vandekerckhove, J. and Ampe, C. (1996). Cofactor A is a molecular chaperone required for β-tubulin folding: functional and structural characterization. Biochemistry 35, 10422-10435.
27. Moreno, S., Klar, A. and Nurse, P. (1991). Molecular genetic analysis of fission yeast Schizosaccharomyces pombe. In Methods in Enzymology (ed. C. Guthrie and G. Fink), pp. 795-823. Academia Press Inc., NY.
28. + essential for a midmitotic transition encodes a leucine-rich repeat protein that positively modulates protein phosphatase-1. Cell 64, 149-157.
29. Pierre, P., Scheel, J., Rickard, J. E. and Kreis, T. E. (1992). CLIP-170 links endocytic vesicles to microtubules. Cell 70, 887-900.
30. Radcliffe, P., Hirata, D., Childs, D., Vardy, L. and Toda, T. (1998). Identification of novel temperature-sensitive lethal alleles in essential β-tubulin and nonessential α2-tubulin genes as fission yeast polarity mutants. Mol. Biol. Cell. 9, 1757-1771.
31. Sambrook, J., Fritsch, E. F. and Maniatis, T. (1989). Molecular Cloning: A Laboratory Manual, edn 2. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
32. Southern, J. A., Young, D. F., Heaney, F., Baumgartner, W. and Randall, R. E. (1991). Identification of an epitope on the P & V proteins of simian virus 5 that distinguishes between two isolates with different biological characteristics. J. Gen. Virol. 72, 1551-1557.
33. Stearns, T., Hoyt, M. A. and Botstein, D. (1990). Yeast mutants sensitive to antimicrotubule drugs define three genes that affect microtubule function. Genetics 124, 251-262.
34. Tian, G., Huang, Y., Rommelaere, H., Vandekerckhove, J., Ampe, C. and Cowan, N. J. (1996). Pathway leading to correctly folded β-tubulin. Cell 86, 287-296.
35. Tian, G., Lewis, S. A., Feierbach, B., Stearns, T., Rommelaere, H., Ampe, C. and Cowan, N. J. (1997). Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors. J. Cell Biol. 138, 821-832.
36. Toda, T., Umesono, K., Hirata, A. and Yanagida, M. (1983). Cold-sensitive nuclear division arrest mutants of the fission yeast Schizosaccharomyces pombe. J. Mol. Biol. 168, 251-270.
37. Vainberg, I. E., Lewis, S. A., Rommelaere, H., Ampe, C., Vandekerckhove, J., Klein, H. L. and Cowan, N. J. (1998). Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin. Cell 93, 863-873.
38. Vega, L. R., Fleming J. and Solomon, F. (1998). An a-tubulin mutant destabilizes the heterodimer: phenotypic consequences and interactions with tubulin-binding proteins. Mol. Biol. Cell. 9, 2349-2360.
39. Weinstein, B. and Solomon, F. (1990). Phenotypic consequences of tubulin overproduction in Saccharomyces cerevisiae: differences between α-tubulin and β-tubulin. Mol. Cell Biol. 10, 5295-5304.