1887

Abstract

Summary: Cells of the dimorphic yeast are easily induced to germinate in synchrony. Using germinating cells of strain FC18, we examined the effects of several drugs that are known to affect the cytoskeleton on growth and cytoskeletal organization. Cytochalasin A (CA), an inhibitor of actin function, inhibited the germination of the yeast cells and changed the cylindrical expansion of the apex of the germ tube to swelling growth. Effects of CA on the organization of actin were examined with rhodamine-phalloidin (Rh-Ph), which specifically stains F-actin. In CA-untreated cells, Rh-Ph staining resulted in condensed dot-like fluorescence at the growing tip, as well as filamentous fluorescence (actin cables) that ran from the apex to the basal region. In CA-treated cells, condensed dot-like fluorescence was still observed at the swelling tip, but actin cables had disappeared completely. This result indicates that CA does not affect the asymmetrical distribution of actin, and suggests that the actin cables are not required for maintenance of the polarized localization of actin. Benomyl, an anti-microtubule drug, inhibited the germination of yeast cells and the apical growth of germinated cells. not only disrupted microtubules (MTs), but also affected the distribution of actin. In benomyl-treated cells, actin dots were randomly dispersed all over the cell. This result indicates that benomyl destroyed the mechanism that maintains the asymmetrical distribution of actin, and suggests that MTs are involved in such a mechanism. The polarized localization of organelles is one of the most important factors associated with dimorphism. Our data suggest that the cytoskeleton, composed of actin and MTs, is involved in the control of polarity in the hyphal growth of , and that actin and MTs are interrelated in the establishment of polarity.

Loading

Article metrics loading...

/content/journal/micro/10.1099/13500872-140-2-271
1994-02-01
2024-04-25
Loading full text...

Full text loading...

/deliver/fulltext/micro/140/2/mic-140-2-271.html?itemId=/content/journal/micro/10.1099/13500872-140-2-271&mimeType=html&fmt=ahah

References

  1. Adams A. E. M., Pringle J. R. Relationship of actin and tubulin distribution to bud growth in wild-type and morpho-genetic-mutant Saccharomyces cerevisiae. J Cell Biol 1984; 98 934 945
    [Google Scholar]
  2. Adams A. E., Botstein D., Drubin D. G. A yeast actin- binding protein is encoded by SAC6, a gene found by suppression of an actin mutation. Science 1989; 243 231 233
    [Google Scholar]
  3. Akashi T., Homma M., Kanbe T., Tanaka K. Ultra-structure of proteinase-secreting cells of Candida albicans studied by alkaline bismuth staining and immunocytochemistry. Gen Microbiol 1993; 139 2185 2195
    [Google Scholar]
  4. Anderson J. M., Soil D. R. Differences in actin localization during bud and hypha formation in the yeast Candida albicans. J Gen Microbiol 1986; 132 2035 2047
    [Google Scholar]
  5. Bartnicki-Garcia S., Hergert F., Gierz G. Computer simulation of fungal morphogenesis and the mathematical basis for hyphal (tip) growth. Protoplasma 1989; 153 46 57
    [Google Scholar]
  6. Barton R., Gull K. Variation in cytoplasmic microtubule organization and spindle length between the two forms of the dimorphic fungus Candida albicans. J Cell Sci 1988; 91 211 220
    [Google Scholar]
  7. Caesar Ton That T. C., Rossier C., Barja F., Turian G., Roos U.P. Induction of multiple germ tubes in Neurospora crassa by antitubulin agents. Fur J Cell Biol 1988; 46 68 79
    [Google Scholar]
  8. Davidse L. C., Flach W. The mechanism of resistance to the antitubulin methyl benzimidazole-2-yl carbamate in the fungus Aspergillus nidulans. J Cell Biol 1977; 72 174 193
    [Google Scholar]
  9. Drubin D. G. Actin and actin-binding proteins in yeast. Cell Motil Cytoskeleton 1990; 15 7 11
    [Google Scholar]
  10. Grove S. N. The cytology of hyphal tip growth. In The Filamentous Fungi 1978 Edited by Smith J. E., Berry D. R. London: Edward Arnold; pp 28 50
    [Google Scholar]
  11. Grove S. N., Sweigard J. A. Cytochalasin A inhibits spore germination and hyphal tip growth in Gibertella persicaria. Exp Mycol 1980; 4 239 250
    [Google Scholar]
  12. Haarer B. K., Lillie S. H., Adams A. E. M., Magdolen V., Bandlow W., Brown S. S. Purification of profilin from Saccharomyces cerevisiae and analysis of profilin-deficient cells. J Cell Biol 1990; 110 105 114
    [Google Scholar]
  13. Heath I. B. The role of actin in tip growth of fungi. Int Rep Cytol 1990; 123 95 127
    [Google Scholar]
  14. Herr F. B., Heath M. C. The effects of antimicrotubule agents on organelle positioning in the cowpea rust fungus, Uromyces phaseoli var vignae. Exp Mycol 1982; 6 15 24
    [Google Scholar]
  15. Hoch H. C., Staples R. C. The microtubule cytoskeleton in hyphae of Uromyces phaseoli germlings: its relationship to the region of nucleation and to the F-actin cytoskeleton. Protoplasma 1985; 124 112 122
    [Google Scholar]
  16. Howard R. J. Ultrastructural analysis of hyphal tip cell growth in fungi: spitzenkorper, cytoskeleton and endomembranes after freeze-substitution. J Cell Sci 1981; 48 89 103
    [Google Scholar]
  17. Howard R. J., Aist J. R. Cytoplasmic microtubules and fungal morphogenesis: ultrastructural effects of methyl benz- imidazole-2-ylcarbamate determined by freeze-substitution of hyphal tip cells. J Cell Biol 1980; 87 55 64
    [Google Scholar]
  18. Huffaker T. C., Thomas J. H., Botstein D. Diverse effects of β-tubulin mutations on microtubule formation and function. J Cell Biol 1988; 106 1997 2010
    [Google Scholar]
  19. Ishigami M., Nagai R. Motile apparatus in Vallisneria leaf cells II. Effects of cytochalasin B and lead acetate on the rate and direction of streaming. Cell Struct Fund 1980; 5 13 20
    [Google Scholar]
  20. Jackson S. L., Heath I. B. Evidence that actin reinforces the extensible hyphal apex of the oomycete Saprolegnia ferax. Protoplasma 1990; 157 144 153
    [Google Scholar]
  21. Jacobs C. W., Adams A. E. M., Szaniszlo P. J. R., Pringle J. R. 1988; Functions of microtubules in the Saccharomyces cerevisiae cell cycle. J Cell Biol 107 1409 1426
    [Google Scholar]
  22. Johnston G. C., Prendergast J. A., Singer R. A. The Saccharomyces cerevisiae MY02 gene encodes an essential myosin for vectorial transport of vesicles. J Cell Biol 1991; 113 539 551
    [Google Scholar]
  23. Kamiya N. Physical and chemical basis of cytoplasmic streaming. Annu Rev Plant Physiol 1981; 32 205 236
    [Google Scholar]
  24. Liu H., Bretscher A. Disruption of the single tropomyosin gene in yeast results in the disappearance of actin cables from the cytoskeleton. Cell 1989; 57 233 242
    [Google Scholar]
  25. Magee B. B., Koltin Y., Gorman J. A., Magee P. T. Assignment of cloned genes to the seven electrophoretically separated Candida albicans chromosomes. Mol Cell Biol 1988; 8 4721 4726
    [Google Scholar]
  26. Marks J., Hagan I. M., Hyams J. S. Growth polarity and cytokinesis in fission veast: the role of the cytoskeleton. J Cell Sci Suppl 1986; 5 229 241
    [Google Scholar]
  27. Novick P., Botstein D. Phenotypic analysis of tem-perature-sensitive yeast actin mutants. Cell 1985; 40 405 416
    [Google Scholar]
  28. Odds F. C. 1988 Candida and Candidosis London: Bailliere Tindall;
    [Google Scholar]
  29. Oliver J. M., Krawiec J. A., Berlin R. D. 1978; A carbamate herbicide causes microtubule and microfilament disruption and nuclear fragmentation in fibroblasts. Exp Cell Res 116 229 237
    [Google Scholar]
  30. Orbach M. J., Porro E. B., Yanofsky C. Cloning and characterization of the gene for /i-tubulin from a benomyl-resistant mutant of Neurospora crassa and its use as a dominant selectable marker. Mol Cell Biol 1986; 6 2452 2461
    [Google Scholar]
  31. Solomon F. Analyses of the cytoskeleton in Saccharomyces cerevisiae. Annu Rev Cell Biol 1991; 7 633 662
    [Google Scholar]
  32. Staples R. C., Hoch H. C. 1982; A possible role for microtubules and microfilaments in the induction of nuclear division in bean rust uredospore germlings. Exp Mycol 6 293 302
    [Google Scholar]
  33. Thomas J. H., Neff N. F., Botstein D. Isolation and characterization of mutations in the β-tubulin gene of Saccharomjces cerevisiae. Genetics 1985; 112 715 734
    [Google Scholar]
  34. Thyberg J., Moskalewski S. Microtubules and the organization of the Golgi complex. Exp Cell Res 1985; 159 1 16
    [Google Scholar]
  35. Tucker B. E., Hoch H. C., Staples R. C. The involvement of F-actin in Uromyces cell differentiation: the effects of cytochalasin E and phalloidin. Protoplasma 1986; 135 88 101
    [Google Scholar]
  36. Vale R. D. Intracellular transport using microtubule-based motors. Annu Rep Cell Biol 1987; 3 347 378
    [Google Scholar]
  37. Yahara I., Harada F., Sekita S., Yoshihira K., Natori S. Correlation between effects of 24 different cytochalasins on cellular structures and cellular events and those on actin in vitro. J Cell Biol 1982; 92 69 78
    [Google Scholar]
  38. Yokoyama K., Kaji H., Nishimura K., Miyaji M. The role of microfilaments and microtubules in apical growth and dimorphism of Candida albicans. J Gen Microbiol 1990; 136 1067 1075
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/13500872-140-2-271
Loading
/content/journal/micro/10.1099/13500872-140-2-271
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error