Skip to main content

Part of the book series: Developments in Plant Pathology ((DIPP,volume 13))

Abstract

Victoria blight of oats is caused by the fungus Cochliobolus victoriae which is pathogenic because it produces the host-specific toxin, victorin. Oat genotypes are sensitive to victorin if they contain the dominant Vb allele. A 100 kDa protein that binds victorin only in toxin-sensitive (susceptible) genotypes of oats has been identified as the P-protein component of the nuclear-encoded, mitochondrial, glycine decarboxylase complex (GDC). Results have indicated that the 15 kDa H-protein component of the GDC also binds victorin. The GDC, a key component of the photorespiratory cycle, has been shown to be extremely sensitive to the application of victorin both in vivo and in vitro. Recent results have indicated that the cofactor for the P-protein, pyridoxal phosphate, competes with victorin binding in vivo and in vitro and prevents victorin-induced electrolyte leakage. Further, conditions that eliminate photorespiration, protect against victorin-induced symptom development. Thus, a variety of observations indicate a mitochondrial site of action for victorin that is at, or involves, the GDC. Consequently, genetic analyses are being conducted to determine if any of the genes encoding the components of the GDC map to the Vb locus. Our most recent physiological studies have indicated that victorin induces a senescence-like response in sensitive oats including chlorosis, a specific proteolytic degradation of D-ribulose-1,5-bisphosphate carboxylase/oxygenase, and DNA fragmentation. Current studies are directed at characterizing this response and determining what connection exists between victorin’s inhibition of the GDC and this form of programmed cell death.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 169.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 219.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Alnemri, E.S., D.J. Livingston, D.W. Nicholson, G. Salvesen, N.A. Thornbeny, W.W. Wong, and J. Yuan. (1996). Human ICE/CED-3 protease nomenclature. Cell 87:171.

    Article  PubMed  CAS  Google Scholar 

  2. Artus, N.N., S. Naito, and C.R. Somerville. (1994). A mutant of Arabidopsis thaliana that defines a new locus for glycine decarboxylation. Plant Cell Physiol. 35: 879–885.

    CAS  Google Scholar 

  3. Bernardi, P. (1992). Modulation of the mitochondrial cyclosporin A-sensitive permeability transition pore by the proton electrochemical gradient. J. Biol. Chem. 267:8834.

    PubMed  CAS  Google Scholar 

  4. Blackwell, R.D., A.J.S. Murray, and P.J. Lea. (1990). Photorespiratory mutants of the mitochondrial conversion of glycine to serine. Plant Physiol. 94: 1316.

    Article  PubMed  CAS  Google Scholar 

  5. Constantini, P., B.V. Chemyak, V. Petronilli, and P. Bernardi. (1996). Modulation of the mitochondrial permeability transition pore by pyridine nucleotides and dithiol oxidation at two separate sites. J. Biol. Chem. 271:6746.

    Article  Google Scholar 

  6. Douce, R. (1985). The function of plant mitochondrial matrix: The mechanism of glycine oxidation, in Mitochondria in higher plants, by Roland Douce, American Society of Plant Physiologists Monograph Series, Academic Press Inc. pgs 190–204.

    Google Scholar 

  7. Douce, R. J. Bourguignon, D. Macherel, and M. Neuburger. (1994). The glycine decarboxylase system in higher plant mitochondria: structure, function and biogenesis. Biochem. Soc. Trans. 22:184.

    PubMed  CAS  Google Scholar 

  8. Dewey, R.E., J.N. Siedow, D.H. Timothy, and C.S. Levings III.(1988). A 13-kilodalton maize mitochondrial protein in E.coli confers sensitivity to Bipolaris maydis toxin. Science 239:293.

    Article  PubMed  CAS  Google Scholar 

  9. Eger, R. and D.B. Rifkin. (1977). The preparation and use of pyridoxal [32P] phosphate as a labeling reagent for proteins on the outer surface of membranes. Biochimica et Biophys. Acta 470:70.

    Article  CAS  Google Scholar 

  10. Greenberg, J.T. (1996). Programmed cell death: a way of life for plants. Proc. Natl. Acad. Sci. 93:12094.

    Article  PubMed  CAS  Google Scholar 

  11. Gregori, L., D. Marriott, J.A. Putkey, A.R Means, and V. Chau. (1987). Bacterially synthesized vertebrate calmodulin is a specific substrate for ubiqutination. J. Biol. Chem. 262:2562.

    PubMed  CAS  Google Scholar 

  12. Hawes, M.C. (1983). Sensitivity of isolated oat root cap cells and protoplasts to victorin. Plant Path. 22:65.

    CAS  Google Scholar 

  13. Hensel, L.L., G. Vojislava, D.A. Baumgarten, and A.B. Bleecker. (1993). Developmental and age-related processes that influence the longevity and senescence of photosynthetic tissues in Arabidopsis. Plant Cell 5:553.

    PubMed  CAS  Google Scholar 

  14. Houtz, R.L., L. Poneleit, S.B. Jones, M. Royer, and J.T. Stults. (1992). Posttranslational modifications in the amino-terminal region of ribulose-1, 5-bisphosphate carboxylase-4/oxygenase from several plant species. Plant Physiol. 98:1170.

    Article  PubMed  CAS  Google Scholar 

  15. Johal, G.S. and S.P. Briggs. (1992). Reductase activity encoded by the HM1 disease resistance gene in maize. Science 258:985.

    Article  PubMed  CAS  Google Scholar 

  16. Kono, Y., T. Kinoshita, S. Takeuchi, and J.M. Daly. (1986). Structure of HV-toxin M, a host-specific toxin-related compound produced by Helminthosporium victoriae. Agric. Biol. Chem. 50: 2689.

    Article  CAS  Google Scholar 

  17. Litzenberger, C.S. (1949). Nature of susceptibility to Helminthosporium victoriae and resistance to Puccinia coronata in Victoria oats. Phytopath. 39:.

    Google Scholar 

  18. Lohman, K.N., S. Gan, M.C. John, and R.M. Amasino. (1994). Molecular analysis of natural leaf senescence in Arabidopsis thaliana. Physiol. Plant. 92:322.

    Article  CAS  Google Scholar 

  19. Luke, H.H., H.C. Murphy and F.C. Petr. (1966). Inheritance of spontaneous mutations of the victoria locus in oats. Phytopath. 56:210.

    Google Scholar 

  20. Luke, H.H. and H.E. Wheeler. (1955). Toxin production by Helminthosporium victoriae. Phytopaht. 45:453.

    Google Scholar 

  21. Luke, H.H, H.E. Wheeler and A.T. Wallace. (1960). Victoria-type resistance to crown rust separated from susceptibility to Helminthosporium blight in oats. Phytopath. 50:205.

    Google Scholar 

  22. Macko, V., T.J. Wolpert, W. Acklin, B. Jaun, J. Seibl, J. Meili and D. Arigoni. (1985). Characterization of victorin C, the major host-selective toxin from Cochliobolus victoriae: structure of degradation products. Experientia 41, 1366.

    Article  CAS  Google Scholar 

  23. Mayama, S., A.P.A. Bordin, T. Morikawa, H. Tanpo and H. Kalo. (1995). Association of avaenalumin accumulation with co-segregation of victorin sensitivity and crown rust resistance in oat lines carrying the Pc-2 gene. Physiol. Mol. Plant Pathol. 46:263.

    Article  Google Scholar 

  24. Meehan, F. and Murphy, H.C. (1946). A new Helminthosporium blight of oats. Science 104:413.

    Article  Google Scholar 

  25. Meehan, F. and Murphy, H.C. (1947). Differential phytotoxicity of metabolic by-products of Helminthosporium victoriae. Science 106:270.

    Article  PubMed  CAS  Google Scholar 

  26. Meeley, R.B, G.S. Johal, S.P. Briggs, and J.D. Walton. (1992). A biochemical phenotype for a disease resistance gene of maize. Plant Cell 4:71.

    PubMed  CAS  Google Scholar 

  27. Mondai, R. and M.A. Choudhuri. (1982). Regulation of senescence of excised leaves of some C3 and C4 species by endogenous H2O2. Biochem. Physiol. Pflanzen. 177:403.

    Google Scholar 

  28. Morgan, C.L., S.R. Turner and S. Rawsthome. (1993). Coordination of the cell-specific distribution of the four subunits of glycine decarboxylase and of serine hydroxymethyltransferase in leaves of C3-C4 intermediate species from different genera. Planta 190:468.

    Article  CAS  Google Scholar 

  29. Navarre, D.A. and T.J. Wolpert. 1995. Inhibition of the glycine decarboxylase multienzyme complex by the host-selective toxin, victorin. Plant Cell 7:463.

    PubMed  CAS  Google Scholar 

  30. Oliver, D.J., Neuburger, M., Bourguignon, J., and Douce R. (1990). Glycine metabolism by plant mitochondria. Physiol. Plant. 80:487.

    Article  CAS  Google Scholar 

  31. Oliver, D.J., M. Neuburger, J. Bourguignon, and R. Douce. (1990). Interaction between the component enzymes of the glycine decarboxylase multienzyme complex. Plant Physiol. 94:833.

    Article  PubMed  CAS  Google Scholar 

  32. Petit, P.X., S.A. Susin, N. Zamzami, B. Mignotte, and G. Kroemer. (1996). Mitochondria and programmed cell death: bact to the future. FEBS Lets. 396:7.

    Article  CAS  Google Scholar 

  33. Rines, H.W. and Luke, H.H. (1985). Selection and regeneration of toxin-insensitive plants from tissue cultures of oats (Avena sativa) susceptible to Helminthosporium victoriae. Theor. Appl. Genet. 71:16.

    Article  Google Scholar 

  34. Sarojini, G. and D.J. Oliver. (1983). Extraction and partial characterization of the glycine decarboxylase multienzyme complex from pea leaf mitochondria. Plant Physiol. 72:194.

    Article  PubMed  CAS  Google Scholar 

  35. Satler, S.O. and K.V. Thimann. (1983). Metabolism of oat leaves during senescence. Plant Physiol. 71:67.

    Article  PubMed  CAS  Google Scholar 

  36. Smart, C.M. (1994). Gene expression during leaf senescence. New Phytol. 126:419.

    Article  CAS  Google Scholar 

  37. Somerville, S.C. and W.L. Ogren. (1982). Mutants of the cruciferous plant Arabidopsis thaliana lacking glycine decarboxylase activity. Biochem. J. 202:373.

    PubMed  CAS  Google Scholar 

  38. Stauffer, G.V. (1987). Biosynthesis of serine and glycine, in Escherichia coli and Salmonella typhimurium, Cellular and Molecular Biology. Eds. J.L. Ingraham, K. Brooks Low, B. Magasanik, M. Schaechter, and H.E. Umgarger. pgs. 412–418.

    Google Scholar 

  39. Susin, S.A., N. Zamzami, M. Castedo, T. Hirsch, P. Marchetti, A. Macho, E. Daugas, M. Geuskens, and G. Kroemer (1996). Bcl-2 inhibits the mitochondrial release of an apoptogenic protease. J. Exp. Med. 184:1331.

    Article  PubMed  CAS  Google Scholar 

  40. Skulachev, V.P. (1996). Why are mitochondria involved in apoptosis? FEBS Lets. 397:7.

    Article  CAS  Google Scholar 

  41. Walker, J.L. and D.J. Oliver. (1986a). Glycine decarboxylase multienzyme complex. Purification and partial characterization from pea leaf mitochondria. J.B.C. 261:2214.

    CAS  Google Scholar 

  42. Walker, J.L. and D.J. Oliver. (1986b). Light-induced increases in the glycine decarboxylase multienzyme complex from pea leaf mitochondria. Archiv. Biochem. Biophys. 248:626.

    Article  CAS  Google Scholar 

  43. Walton, J.D. (1996). Host-selective toxins: agents of compatibility. Plant Cell 8:1723.

    PubMed  CAS  Google Scholar 

  44. Wheeler, H. and H.H. Luke. (1954). Studies of a toxic agent produced by Helminthosporium victoriae. Phytopath. 44:334.

    Google Scholar 

  45. Widholm, J.M. and W.L. Ogren. (1969). Photorespiratory-induced senescence of plants under conditions of low carbon dioxide. Proc. Natl. Acad. Sci. 63:668.

    Article  PubMed  CAS  Google Scholar 

  46. Wilson, R.L, L.T. Stauffer, and G.V. Stauffer. (1993). Roles of the GcvA and PurR proteins in negative regulation of the Escherichia coli glycine cleavage system. J. Bacteriol. 175:5129.

    PubMed  CAS  Google Scholar 

  47. Wolpert, T.J., V. Macko, W. Acklin, B. Jaun, J. Seibl, J. Meili and D. Arigoni. (1985). Structure of victorin C, the major host-selective toxin from Cochliobolus victoriae. Experientia 41:1524.

    Google Scholar 

  48. Wolpert, T.J., V. Macko, W. Acklin, B. Jaun and D. Arigoni. (1986). Structure of minor host-selective toxins from Cochliobolus victoriae. Experientia 42:1296.

    Article  CAS  Google Scholar 

  49. Wolpert, T.J. and V. Macko. (1988). Molecular features affecting the biological activity of the host-selective toxins from Cochliobolus victoriae. Plant Physiology 88:37.

    Article  PubMed  CAS  Google Scholar 

  50. Wolpert, T.J. and V. Macko. (1989). Specific binding of Victorin to a 100-kd protein from oats. Proc. Natl. Acad. Sci. 86:4092.

    Article  PubMed  CAS  Google Scholar 

  51. Wolpert, T.J. and V. Macko. (1991). Immunological comparison of the victorin binding protein labelled in vitro and in vivo. Plant Physiol 95:917.

    Article  PubMed  CAS  Google Scholar 

  52. Wolpert T.J., D.A. Navarre, D.L. Moore and V. Macko. (1994). Identification of the 100-kD victorin binding protein from oats. Plant Cell 6:1145.

    PubMed  CAS  Google Scholar 

  53. Yoder, O.C. (1980). Toxins in pamqgenesis. Ann. Rev. Phytopathol. 18:103.

    Article  CAS  Google Scholar 

  54. Yuan, J., S. Shaham, S. Ledoux, H.M. Ellis, and H.R. Horvitz. (1993). The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme. Cell 75:641.

    Article  PubMed  CAS  Google Scholar 

  55. Zoratti, M., I. Szabo. (1995). The mitochondrial permeability transition. Biochim. Biophys. Acta 1241:139.

    Article  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1998 Springer Science+Business Media Dordrecht

About this chapter

Cite this chapter

Wolpert, T.J., Navarre, D.A., Lorang, J.M. (1998). Victorin-induced oat cell death. In: Kohmoto, K., Yoder, O.C. (eds) Molecular Genetics of Host-Specific Toxins in Plant Disease. Developments in Plant Pathology, vol 13. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5218-1_12

Download citation

  • DOI: https://doi.org/10.1007/978-94-011-5218-1_12

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-6197-1

  • Online ISBN: 978-94-011-5218-1

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics