Table of Contents
International Journal of Plant Genomics
Volume 2007, Article ID 17542, 13 pages
http://dx.doi.org/10.1155/2007/17542
Research Article

Temporal Gene Expression Profiling of the Wheat Leaf Rust Pathosystem Using cDNA Microarray Reveals Differences in Compatible and Incompatible Defence Pathways

1Cereal Research Centre, Agriculture and Agri-Food Canada, 195 Dafoe Road, Winnipeg, MB, Canada R3T 2M9
2Department of Agricultural, Food and Nutritional Sciences, University of Alberta, 410 Ag/For Building, Edmonton, AB, Canada T6G 2P5

Received 29 December 2006; Accepted 20 July 2007

Academic Editor: Patrick Gulick

Copyright © 2007 Bourlaye Fofana et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. M. G. Eversmeyer and C. L. Kramer, “Epidemiology of wheat leaf and stem rust in the central great plains of the USA,” Annual Review of Phytopathology, vol. 38, pp. 491–513, 2000. View at Publisher · View at Google Scholar · View at PubMed
  2. J. A. Kolmer, “Genetics of resistance to wheat leaf rust,” Annual Review of Phytopathology, vol. 34, pp. 435–455, 1996. View at Publisher · View at Google Scholar · View at PubMed
  3. M. William, R. P. Singh, J. Huerta-Espino, S. O. Islas, and D. Hoisington, “Molecular marker mapping of leaf rust resistance gene Lr46 and its association with stripe rust resistance gene Yr29 in wheat,” Phytopathology, vol. 93, no. 2, pp. 153–159, 2003. View at Publisher · View at Google Scholar · View at PubMed
  4. L. Zhang, H. Meakin, and M. Dickinson, “Isolation of genes expressed during compatible interactions between leaf rust (Puccinia triticina) and wheat using cDNA-AFLP,” Molecular Plant Pathology, vol. 4, no. 6, pp. 469–477, 2003. View at Publisher · View at Google Scholar
  5. M. A. Ayliffe, M. Steinau, and R. F. Park et al., “Aberrant mRNA processing of the maize Rp1-D rust resistance gene in wheat and barley,” Molecular Plant-Microbe Interactions, vol. 17, no. 8, pp. 853–864, 2004. View at Publisher · View at Google Scholar · View at PubMed
  6. R. Rohringer and R. Heitefuss, “Histology and molecular biology of hostparasite specificity,” in The Cereal Rusts, W. R. Bushnell and A. P. Roelfs, Eds., vol. 1, pp. 193–229, Academic Press, Orlando, Fla, USA, 1984.
  7. G. Hu and F. H. J. Rijkenberg, “Subcellular localization of β-1,3-glucanase in Puccinia recondita f.sp. tritici-infected wheat leaves,” Planta, vol. 204, no. 3, pp. 324–334, 1998. View at Publisher · View at Google Scholar
  8. V. K. Thara, J. P. Fellers, and J.-M. Zhou, “In planta induced genes of Puccinia triticina,” Molecular Plant Pathology, vol. 4, no. 1, pp. 51–56, 2003. View at Publisher · View at Google Scholar
  9. G. Hu and F. H. J. Rijkenberg, “Scanning electron microscopy of early infection structure formation by Puccinia recondita f. sp. tritici on and in susceptible and resistant wheat lines,” Mycological Research, vol. 102, no. 4, pp. 391–399, 1998. View at Publisher · View at Google Scholar
  10. J. D. Faris, W. L. Li, D. J. Liu, P. D. Chen, and B. S. Gill, “Candidate gene analysis of quantitative disease resistance in wheat,” Theoretical and Applied Genetics, vol. 98, no. 2, pp. 219–225, 1999. View at Publisher · View at Google Scholar
  11. V. S. Anguelova-Merhar, A. J. Van Der Westhuizen, and Z. A. Pretorius, “β-1,3-glucanase and chitinase activities and the resistance response of wheat to leaf rust,” Journal of Phytopathology, vol. 149, no. 7-8, pp. 381–384, 2001. View at Publisher · View at Google Scholar
  12. K. C. Lin, W. R. Bushnell, A. G. Smith, and L. J. Szabo, “Temporal accumulation patterns of defence response gene transcripts in relation to resistant reactions in oat inoculated with Puccinia graminis,” Physiological and Molecular Plant Pathology, vol. 52, no. 2, pp. 95–114, 1998. View at Publisher · View at Google Scholar
  13. S. G. Southerton and B. J. Deverall, “Changes in phenylalanine ammonia-lyase and peroxidase activities in wheat cultivars expressing resistance to the leaf-rust fungus,” Plant Pathology, vol. 39, no. 2, pp. 223–230, 1990. View at Publisher · View at Google Scholar
  14. L. E. Browder, “A compendium of information about named genes for low reaction to Puccinia recondita in wheat,” Crop Science, vol. 20, no. 6, pp. 775–779, 1980.
  15. D. J. Duggan, M. Bittner, Y. Chen, P. Meltzer, and J. M. Trent, “Expression profiling using cDNA microarrays,” Nature Genetics, vol. 21, supplement 1, pp. 10–14, 1999. View at Publisher · View at Google Scholar · View at PubMed
  16. T. Richmond and S. Somerville, “Chasing the dream: plant EST microarrays,” Current Opinion in Plant Biology, vol. 3, no. 2, pp. 108–116, 2000. View at Publisher · View at Google Scholar
  17. P. Reymond, “DNA microarrays and plant defence,” Plant Physiology and Biochemistry, vol. 39, no. 3-4, pp. 313–321, 2001. View at Publisher · View at Google Scholar
  18. R. A. Caldo, D. Nettleton, and R. P. Wise, “Interaction-dependent gene expression in Mla-specified response to barley powdery mildew,” The Plant Cell, vol. 16, no. 9, pp. 2514–2528, 2004. View at Publisher · View at Google Scholar · View at PubMed
  19. Y. Tao, Z. Xie, and W. Chen et al., “Quantitative nature of Arabidopsis responses during compatible and incompatible interactions with the bacterial pathogen Pseudomonas syringae,” The Plant Cell, vol. 15, no. 2, pp. 317–330, 2003. View at Publisher · View at Google Scholar
  20. T. Eulgem, “Regulation of the Arabidopsis defense transcriptome,” Trends in Plant Science, vol. 10, no. 2, pp. 71–78, 2005. View at Publisher · View at Google Scholar · View at PubMed
  21. P. M. Schenk, K. Kazan, and I. Wilson et al., “Coordinated plant defense responses in Arabidopsis revealed by microarray analysis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no. 21, pp. 11655–11660, 2000. View at Publisher · View at Google Scholar · View at PubMed
  22. K. Maleck, A. Levine, and T. Eulgem et al., “The transcriptome of Arabidopsis thaliana during systemic acquired resistance,” Nature Genetics, vol. 26, no. 4, pp. 403–410, 2000. View at Publisher · View at Google Scholar · View at PubMed
  23. D. Baldwin, V. Crane, and D. Rice, “A comparison of gel-based, nylon filter and microarray techniques to detect differential RNA expression in plants,” Current Opinion in Plant Biology, vol. 2, no. 2, pp. 96–103, 1999. View at Publisher · View at Google Scholar
  24. J. Boddu, S. Cho, W. M. Kruger, and G. J. Muehlbauer, “Transcriptome analysis of the barley-Fusarium graminearum interaction,” Molecular Plant-Microbe Interactions, vol. 19, no. 4, pp. 407–417, 2006. View at Publisher · View at Google Scholar · View at PubMed
  25. D. L. Long and J. A. Kolmer, “A North American system of nomenclature for Puccinia triticina,” Phytopathology, vol. 79, pp. 525–529, 1989. View at Publisher · View at Google Scholar
  26. B. Ewing, L. Hillier, M. C. Wendl, and P. Green, “Base-calling of automated sequencer traces using PhredI>. Accuracy assessment,” Genome Research, vol. 8, no. 3, pp. 175–185, 1998.
  27. X. Huang and A. Madan, “CAP3: a DNA sequence assembly program,” Genome Research, vol. 9, no. 9, pp. 868–877, 1999. View at Publisher · View at Google Scholar
  28. N. N. Iscove, M. Barbara, M. Gu, M. Gibson, C. Modi, and N. Winegarden, “Representation is faithfully preserved in global cDNA amplified exponentially from sub-picogram quantities of mRNA,” Nature Biotechnology, vol. 20, no. 9, pp. 940–943, 2002. View at Publisher · View at Google Scholar · View at PubMed
  29. S. F. Altschul, T. L. Madden, and A. A. Schäffer et al., “Gapped BLAST and PSI-BLAST: a new generation of protein database search programs,” Nucleic Acids Research, vol. 25, no. 17, pp. 3389–3402, 1997. View at Publisher · View at Google Scholar
  30. A. R. Portis Jr., “Rubisco activase—Rubisco's catalytic chaperone,” Photosynthesis Research, vol. 75, no. 1, pp. 11–27, 2003. View at Publisher · View at Google Scholar · View at PubMed
  31. C. Lamb and R. A. Dixon, “The oxidative burst in plant disease resistance,” Annual Review of Plant Physiology and Plant Molecular Biology, vol. 48, pp. 251–275, 1997. View at Publisher · View at Google Scholar · View at PubMed
  32. K. Apel and H. Hirt, “Reactive oxygen species: metabolism, oxidative stress, and signal transduction,” Annual Review of Plant Biology, vol. 55, pp. 373–399, 2004. View at Publisher · View at Google Scholar · View at PubMed
  33. J. L. Dangl and J. D. G. Jones, “Plant pathogens and integrated defence responses to infection,” Nature, vol. 411, no. 6839, pp. 826–833, 2001. View at Publisher · View at Google Scholar · View at PubMed
  34. K. Shirasu and P. Schulze-Lefert, “Complex formation, promiscuity and multi-functionality: protein interactions in disease-resistance pathways,” Trends in Plant Science, vol. 8, no. 6, pp. 252–258, 2003. View at Publisher · View at Google Scholar
  35. P. Schulze-Lefert and S. Bieri, “Recognition at a distance,” Science, vol. 308, no. 5721, pp. 506–508, 2005. View at Publisher · View at Google Scholar · View at PubMed
  36. G. Coaker, A. Falick, and B. Staskawicz, “Activation of a phytopathogenic bacterial effector protein by a eukaryotic cyclophilin,” Science, vol. 308, no. 5721, pp. 548–550, 2005. View at Publisher · View at Google Scholar · View at PubMed
  37. M. H. Glickman and A. Ciechanover, “The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction,” Physiological Reviews, vol. 82, no. 2, pp. 373–428, 2002.
  38. M. C. Heath, “Signalling between pathogenic rust fungi and resistant or susceptible host plants,” Annals of Botany, vol. 80, no. 6, pp. 713–720, 1997. View at Publisher · View at Google Scholar
  39. G. G. Hu and F. H. J. Rijkenberg, “Development of early infection structures of Puccinia recondita f.sp. tritici in non-host cereal species,” Journal of Phytopathology, vol. 146, no. 1, pp. 1–10, 1998. View at Publisher · View at Google Scholar
  40. C. Jantasuriyarat, M. Gowda, and K. Haller et al., “Large-scale identification of expressed sequence tags involved in rice and rice blast fungus interaction,” Plant Physiology, vol. 138, no. 1, pp. 105–115, 2005. View at Publisher · View at Google Scholar · View at PubMed
  41. J. Zou, S. Rodriguez-Zas, and M. Aldea et al., “Expression profiling soybean response to Pseudomonas syringae reveals new defense-related genes and rapid HR-specific downregulation of photosynthesis,” Molecular Plant-Microbe Interactions, vol. 18, no. 11, pp. 1161–1174, 2005. View at Publisher · View at Google Scholar · View at PubMed
  42. M. C. Heath, “Hypersensitive response-related death,” Plant Molecular Biology, vol. 44, no. 3, pp. 321–334, 2000. View at Publisher · View at Google Scholar
  43. M. Trujillo, K.-H. Kogel, and R. Hückelhoven, “Superoxide and hydrogen peroxide play different roles in the nonhost interaction of barley and wheat with inappropriate formae speciales of Blumeria graminis,” Molecular Plant-Microbe Interactions, vol. 17, no. 3, pp. 304–312, 2004. View at Publisher · View at Google Scholar · View at PubMed
  44. H. Vanacker, T. L. W. Carver, and C. H. Foyer, “Pathogen-induced changes in the antioxidant status of the apoplast in barley leaves,” Plant Physiology, vol. 117, no. 3, pp. 1103–1114, 1998. View at Publisher · View at Google Scholar
  45. S. Davletova, L. Rizhsky, and H. Liang et al., “Cytosolic ascorbate peroxidase 1 is a central component of the reactive oxygen gene network of Arabidopsis,” The Plant Cell, vol. 17, no. 1, pp. 268–281, 2005. View at Publisher · View at Google Scholar · View at PubMed
  46. L. J. Allen, K. B. Macgregor, R. S. Koop, D. H. Bruce, J. Karner, and A. W. Bown, “The relationship between photosynthesis and a mastoparan-induced hypersensitive response in isolated mesophyll cells,” Plant Physiology, vol. 119, no. 4, pp. 1233–1241, 1999. View at Publisher · View at Google Scholar
  47. S. Seo, M. Okamoto, and T. Iwai et al., “Reduced levels of chloroplast FtsH protein in tobacco mosaic virus-infected tobacco leaves accelerate the hypersensitive reaction,” The Plant Cell, vol. 12, no. 6, pp. 917–932, 2000. View at Publisher · View at Google Scholar
  48. R. Mittler, X. Feng, and M. Cohen, “Post-transcriptional suppression of cytosolic ascorbate peroxidase expression during pathogen-induced programmed cell death in tobacco,” The Plant Cell, vol. 10, no. 3, pp. 461–473, 1998. View at Publisher · View at Google Scholar
  49. M. Yoshioka, S. Uchida, and H. Mori et al., “Quality control of photosystem—II: cleavage of reaction center D1 protein in spinach thylakoids by FtsH protease under moderate heat stress,” Journal of Biological Chemistry, vol. 281, no. 31, pp. 21660–21669, 2006. View at Publisher · View at Google Scholar · View at PubMed
  50. C. Spetea, T. Hundal, F. Lohmann, and B. Andersson, “GTP bound to chloroplast thylakoid membranes is required for light-induced, multienzyme degradation of the photosystem II D1 protein,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 11, pp. 6547–6552, 1999. View at Publisher · View at Google Scholar
  51. A. Devoto, P. R. Muskett, and K. Shirasu, “Role of ubiquitination in the regulation of plant defence against pathogens,” Current Opinion in Plant Biology, vol. 6, no. 4, pp. 307–311, 2003. View at Publisher · View at Google Scholar
  52. J. P. Rathjen and P. Moffett, “Early signal transduction events in specific plant disease resistance,” Current Opinion in Plant Biology, vol. 6, no. 4, pp. 300–306, 2003. View at Publisher · View at Google Scholar
  53. R. A. Dixon and N. L. Paiva, “Stress-induced phenylpropanoid metabolism,” The Plant Cell, vol. 7, no. 7, pp. 1085–1097, 1995. View at Publisher · View at Google Scholar · View at PubMed
  54. F. Daayf, A. Schmitt, and R. R. Bélanger, “Evidence of phytoalexins in cucumber leaves infected with powdery mildew following treatment with leaf extracts of Reynoutria sachalinensis,” Plant Physiology, vol. 113, no. 3, pp. 719–727, 1997.
  55. E. Nakane, K. Kawakita, N. Doke, and H. Yoshioka, “Elicitation of primary and secondary metabolism during defense in the potato,” Journal of General Plant Pathology, vol. 69, no. 6, pp. 378–384, 2003. View at Publisher · View at Google Scholar
  56. B. Fofana, N. Benhamou, D. J. McNally, C. Labbé, A. Séguin, and R. R. Bélanger, “Suppression of induced resistance in cucumber through disruption of the flavonoid pathway,” Phytopathology, vol. 95, no. 1, pp. 114–123, 2005. View at Publisher · View at Google Scholar · View at PubMed
  57. S. Yoshimura, U. Yamanouchi, and Y. Katayose et al., “Expression of Xa1, a bacterial blight-resistance gene in rice, is induced by bacterial inoculation,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 4, pp. 1663–1668, 1998. View at Publisher · View at Google Scholar
  58. S. Zhang and D. F. Klessig, “MAPK cascades in plant defense signaling,” Trends in Plant Science, vol. 6, no. 11, pp. 520–527, 2001. View at Publisher · View at Google Scholar
  59. J. Dong, C. Chen, and Z. Chen, “Expression profiles of the Arabidopsis WRKY gene superfamily during plant defense response,” Plant Molecular Biology, vol. 51, no. 1, pp. 21–37, 2003. View at Publisher · View at Google Scholar
  60. C. Azevedo, A. Sadanandom, K. Kitagawa, A. Freialdenhoven, K. Shirasu, and P. Schulze-Lefert, “The RAR1 interactor SGT1, an essential component of R gene-triggered disease resistance,” Science, vol. 295, no. 5562, pp. 2073–2076, 2002. View at Publisher · View at Google Scholar · View at PubMed
  61. K. Kitagawa, D. Skowyra, S. J. Elledge, J. W. Harper, and P. Hieter, “SGT1 encodes an essential component of the yeast kinetochore assembly pathway and a novel subunit of the SCF ubiquitin ligase complex,” Molecular Cell, vol. 4, no. 1, pp. 21–33, 1999. View at Publisher · View at Google Scholar
  62. S. Shigeoka, T. Ishikawa, and M. Tamoi et al., “Regulation and function of ascorbate peroxidase isoenzymes,” Journal of Experimental Botany, vol. 53, no. 372, pp. 1305–1319, 2002. View at Publisher · View at Google Scholar
  63. S. Barak, A. Nejidat, Y. Heimer, and M. Volokita, “Transcriptional and posttranscriptional regulation of the glycolate oxidase gene in tobacco seedlings,” Plant Molecular Biology, vol. 45, no. 4, pp. 399–407, 2001. View at Publisher · View at Google Scholar
  64. N. Zhang and A. R. Portis Jr., “Mechanism of light regulation of Rubisco: a specific role for the larger Rubisco activase isoform involving reductive activation by thioredoxin-f,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 16, pp. 9438–9443, 1999. View at Publisher · View at Google Scholar
  65. I. Cohen, J. A. Knopf, V. Irihimovitch, and M. Shapira, “A proposed mechanism for the inhibitory effects of oxidative stress on Rubisco assembly and its subunit expression,” Plant Physiology, vol. 137, no. 2, pp. 738–746, 2005. View at Publisher · View at Google Scholar · View at PubMed
  66. R. Hauschild and A. von Schaewen, “Differential regulation of glucose-6-phosphate dehydrogenase isoenzyme activities in potato,” Plant Physiology, vol. 133, no. 1, pp. 47–62, 2003. View at Publisher · View at Google Scholar
  67. R. Entus, M. Poling, and K. M. Herrmann, “Redox regulation of Arabidopsis 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase,” Plant Physiology, vol. 129, no. 4, pp. 1866–1871, 2002. View at Publisher · View at Google Scholar · View at PubMed