Skip to main content
SpringerLink
Log in

Plant gene expression in response to pathogens

  • Review
  • Published:
Plant Molecular Biology Aims and scope Submit manuscript

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

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

References

  1. Abeles FB, Bosshart RP, Forrence LE, Habig WH: Preparation and purification of glucanase and chitinase from bean leaves. Plant Physiol 47: 129–134 (1970).

    Google Scholar 

  2. Aist JR: Papillae and related wound plugs of plant cells. Annual Review Phytopathol 81: 107–121 (1976).

    Google Scholar 

  3. Anderson AJ: Studies on the structure and elicitor activity of fungal glucans. Can J Bot 58: 2343–2348 (1980).

    Google Scholar 

  4. Anderson AJ: Preformed resistance mechanisms. In: Mount MS, Lacy GH (eds) Phytopathogenic Prokaryotes, Vol. 2. Academic Press, London (1982) pp. 119–136.

    Google Scholar 

  5. Antoniw JF, White RF: Changes with time in the distribution of virus and PR protein around single local lesions of TMV infected tobacco. Plant Molec Biol 6: 145–149 (1986).

    Google Scholar 

  6. Arora YK, Bajaj KL: Peroxidase and polyphenol oxidase associated with induced resistance of mung bean to Rhizoctonia solani Kuhn. Phytopathol Z 114: 325–331 (1985).

    Google Scholar 

  7. Asada Y, Kugoh T: Incorporation of tritiated phenylalanine into lignified cell walls of Japanese radish root infected by Peronospora parasitica. Ann Phytopathol Soc Japan 37: 311–313 (1971).

    Google Scholar 

  8. Asada Y, Matsumoto I: Formation of lignin in the root tissues of Japanese radish affected by Alternaria japonica. Phytopathology 57: 1339–1343 (1967).

    Google Scholar 

  9. Asada Y, Matsumoto I: Formation of lignin-like substance in the root tissues of Japanese radish plant infected by downy mildew fungus. Ann Phytopathol Soc Japan 35: 160–167 (1969).

    Google Scholar 

  10. Asada Y, Matsumoto I: De novo synthesis of L-phenylalanine ammonia-lyase in Japanese radish root infected by downy mildew fungus. Mem Coll Agric Ehime Univ 17: 27–36 (1972).

    Google Scholar 

  11. Asada Y, Matsumoto I: The nature of lignin obtained from downy mildew-infected Japanese radish root. Phytopathol Z 73: 208–214 (1972).

    Google Scholar 

  12. Asada Y, Ohguchi T, Matsumoto I: Induction of lignification in response to fungal infection. In: Daly JM, Uritani I (eds) Recognition and Specificity in Host-Parasite Interactions, Japan Scientific Societies Press, Tokyo and University Park Press, Baltimore, USA (1979) pp. 99–112.

    Google Scholar 

  13. Atkinson MM, Huang J-S, Knopp JA: The hypersensitive reaction of tobacco to Pseudomonas syringae pv. pisi. Activation of a plasmalemma K+/H+ exchange mechanism. Plant Physiol 79: 843–847 (1985).

    Google Scholar 

  14. Azad HR, Kado CI: Relation of tobacco hypersensitivity to pathogenicity of Erwinia rubrifaciens. Phytopathology 74: 61–64 (1984).

    Google Scholar 

  15. Bailey JA: Mechanisms of phytoalexin accumulation. In: Bailey JA, Mansfield JW (eds) Phytoalexins. Blackie and Sons, Glasgow (1982) pp. 289–323.

    Google Scholar 

  16. Bailey JA: Phytoalexins: a genetic view of their significance. In: Day PR, Jellis GJ (eds) Genetics and Plant Pathogenesis. Blackwell Scientific Publications, Oxford (1987) pp. 233–244.

    Google Scholar 

  17. Bailey JA, Mansfield JW (eds) Phytoalexins. Blackie and Sons, Glasgow (1982).

    Google Scholar 

  18. Beardmore J, Ride JP, Granger JW: Cellular lignification as a factor in the hypersensitive resistance of wheat to stem rust. Physiol Plant Pathol 22: 209–220 (1983).

    Google Scholar 

  19. Bell AA: Biochemical mechanisms of disease resistance. Ann Rev Plant Physiol 32: 21–81 (1981).

    Google Scholar 

  20. Bell JN, Dixon RA, Bailey JA, Rowell PM, Lamb CJ: Differential induction of chalcone synthase mRNA activity at the onset of phytoalexin accumulation in compatible and incompatible plant-pathogen interactions Proc Natl Acad Sci USA 81: 3384–3388 (1984).

    Google Scholar 

  21. Bell JN, Ryder TB, Wingate VPM, Bailey JA, Lamb CJ: Differential accumulation of plant defense gene transcripts in a compatible and an incompatible plant-pathogen interaction. Molec Cell Biol 6: 1615–1623 (1986).

    Google Scholar 

  22. Bisseling T, Govers P, Stiekema W: The identification of proteins and their mRNAs involved in the establishment of an effective symbiosis. Oxford Surv Plant Molec Cell Biol 1: 53–83 (1984).

    Google Scholar 

  23. Boll W, Fujisawa J-I, Niemi J, Weissmann C: A new approach to high sensitivity differential hybridisation. Gene 50: 41–53 (1986).

    Google Scholar 

  24. Boller T: Induction of hydrolases as a defence reaction against pathogens. In: Key JL, Kosuge T (eds) Cellular and Molecular Biology of Plant Stress. A.R. Liss, New York, NY (1985) pp. 247–262.

    Google Scholar 

  25. Boller T, Gehri A, Maunch F, Vögeli U: Chitinase in bean leaves: induction by ethylene, purification, properties and possible function. Planta 157: 22–31 (1983).

    Google Scholar 

  26. Bolwell GP, Bell JN, Cramer CL, Schuch W, Lamb CJ, Dixon RA: l-phenylalanine ammonia-lyase from Phaseolus vulgaris. Characterisation and differential induction of multiple forms froms elicitor-treated cell suspension cultures. Eur J Biochem 149: 411–419 (1985).

    Google Scholar 

  27. Bolwell GP, Dixon RA: Membrane-bound hydroxylase in elicitor-treated bean cells. Rapid induction of the synthesis of prolyl hydroxylase and a putative cytochrome P-450. Eur J Biochem 159: 163–169 (1986).

    Google Scholar 

  28. Bolwell GP, Robbins MP, Dixon RA: Metabolic changes in elicitor-treated bean cells. Enzymic responses associated with rapid changes in cell wall components. Eur J Biochem 148: 571–578 (1985).

    Google Scholar 

  29. Bolwell GP, Robbins MP, Dixon RA: Elicitor-induced prolyl hydroxylase from French bean (Phaseolus vulgaris). Localisation, purification and properties. Biochem J 229: 693–699 (1985).

    Google Scholar 

  30. Bonhoff A, Loyal R, Ebel J, Grisebach H: Race:cultivar-specific induction of enzymes related to phytoalexin biosynthesis in soybean roots following infection with Phytophthora megasperma f.sp. glycinea. Arch Bioch Biophys 264: 149–154 (1986).

    Google Scholar 

  31. Bonhoff A, Loyal R, Feller K, Ebel J, Grisebach H: Further investigations of race:cultivar-specific induction of enzymes related to phytoalexin biosynthesis in soybean roots following infection with Phytophthora megasperma f.sp. glycinea. Biol Chem Hoppe-Seyler (in press).

  32. Börner H, Grisebach H: Enzyme induction in soybean infected by Phytophthora megasperma f.sp. glycinea. Arch Bioch Biophys 217: 65–71 (1982).

    Google Scholar 

  33. Brewin NJ, Bradley DJ, Wood EA, Galfre G, Butcher GW: A study of surface interactions between Rhizobium bacteroids and the peribacteroid membrane using monoclonal antibodies. In: Lugtenberg B (ed.) Recognition in Microbe-Plant Symbiotic and Pathogenic Interactions. NATO ASI SeriesH, Vol. 4, Springer-Verlag, Berlin (1986) pp. 153–161.

    Google Scholar 

  34. Broglie KE, Gaynor TJ, Broglie RM: Ethylene-regulated gene expression: molecular cloning of the genes encoding an endochitinase from Phaseolus vulgaris. Proc Natl Acad Sci USA 83: 6820–6824 (1986).

    Google Scholar 

  35. Bruegger BB, Keen NT: Specific elicitors of glyceollin accumulation in the Pseudomonas glycinea-soybean hostparasite system. Physiol Plant Pathol 15: 43–51 (1979).

    Google Scholar 

  36. Camacho-Henriquez A, Lucas J, Sänger HL: Purification and biochemical properties of the “pathogenesis-related” protein P14 from tomato leaves. Neth J Plant Pathol 89: 308 (1983).

    Google Scholar 

  37. Carr JP, Dixon DC, Klessig DF: Synthesis of pathogenesis-related proteins in tobacco is regulated at the level of mRNA accumulation and occurs on membrane-bound polysomes. Proc Natl Acad Sci USA 82: 7999–8003 (1985).

    Google Scholar 

  38. Chappell J, Hahlbrock K: Transcription of plant defense genes in response to UV light or fungal elicitor. Nature 311: 76–78 (1984).

    Google Scholar 

  39. Chen J, Varner JE: Isolation and characterisation of cDNA clones for carrot extensin and a proline-rich 33-kDa protein. Proc Natl Acad Sci USA 82: 4399–4403 (1985).

    Google Scholar 

  40. Chen J, Varner JE: An extracellular matrix protein in plants: characterisation of a genomic clone for carrot extensin. EMBO J 4: 2145–2151 (1985).

    Google Scholar 

  41. Collinge DB, Milligan DE, Dow JM, Scofield G, Daniels MJ: Gene expression in Brassica campestris showing a hypersensitive response to the incompatible pathogen Xanthomonas campestris pv. vitians. Plant Molec Biol 8: 405–411 (1987).

    Google Scholar 

  42. Conn EE: Cyanogenic glucosides. In: Stumpf P, Conn EE (eds) The Biochemistry of Plants, Vol. 7, Academic Press, London (1981) pp. 479–500.

    Google Scholar 

  43. Cooper JI, Jones AT: Responses of plants to viruses: proposals for the use of terms. Phytopathology 73: 127–128 (1983).

    Google Scholar 

  44. Cornelissen BJC, Hooft van Huijsduijnen RAM, Bol JF: A tobacco mosaic virus-induced tobacco protein is homologous to the sweet-tasting protein thaumatin. Nature 321: 531–532 (1986).

    Google Scholar 

  45. Cramer CL, Bell JN, Ryder TB, Bailey JA, Schuch W, Bolwell GP, Robbins MP, Dixon RA, Lamb CJ: Co-ordinated synthesis of phytoalexin biosynthetic enzymes in biologically-stressed cells of bean (Phaseolus vulgaris L.). EMBO J 4: 285–289 (1985).

    Google Scholar 

  46. Cramer CL, Ryder TB, Bell JN, Lamb CJ: Rapid switching of plant gene expression induced by fungal elicitor. Science 227: 1240–1243 (1985).

    Google Scholar 

  47. Crute IR: Genetic studies with Bremia lactucae (lettuce downy mildew). In: Day PR, Jellis GJ (eds) Genetics and Plant Pathogenesis. Blackwell Scientific Publications, Oxford (1987) pp. 207–219.

    Google Scholar 

  48. Daly JM: The role of recognition in plant disease. Ann Rev Phytopathol 22: 273–307 (1984).

    Google Scholar 

  49. Daniels CH, Fristensky B, Wagoner W, Hadwiger LA: Pea genes associated with non-host disease resistance to Fusarium are also active in race-specific disease resistance to Pseudomonas. Plant Molec Biol 8: 309–316 (1987).

    Google Scholar 

  50. Daniels DL, Hadwiger LA: Pisatin-inducing components in filtrates of virulent and avirulent Fusarium solani cultures. Physiol Plant Pathol 8: 9–19 (1976).

    Google Scholar 

  51. Davidson AD, Manners JM, Simpson RS, Scott KJ: cDNA cloning of mRNAs induced in resistant barley during infection by Erysiphe graminis f.sp. hordei. Plant Molec Biol 8: 77–85 (1987).

    Google Scholar 

  52. Davis KR, Darvill AG, Albersheim P: Host-pathogen interations XXXI. Several biotic and abiotic elicitors act synergistically in the induction of phytoalexin accumulation in soybean. Plant Molec Biol 6: 23–32 (1986).

    Google Scholar 

  53. Day PR: Genetics of Host-Parasite Interactions. W. H. Freeman and Co., San Fransisco, USA (1974).

    Google Scholar 

  54. Day PR: Genetics of recognition systems in host-parasite interactions. In: Linskens HF, Heslop-Harrison J (eds) Cellular Interactions. Springer-Verlag, Berlin (1984) pp. 134–147.

    Google Scholar 

  55. Dennis ES, Gerlach WL, Pryor AJ, Bennetzen JL, Inglis A, Llewellyn D, Sachs MM, Ferl RJ, Peacock WJ: Molecular analysis of the alcohol dehydrogenase (Adh I) gene of maize. Nucleic Acids Research 12: 3983–4000 (1984).

    Google Scholar 

  56. deTapia M, Bergmann P, Awade A, Burkard G: Analysis of acid extractible bean leaf proteins induced by mercuric chloride treatment and alfalfa mosaic virus infection. Partial purification and characterisation. Plant Science 45: 167–177 (1986).

    Google Scholar 

  57. de Tapia M, Dietrich A, Burkard G: Bean pathogenesis-related proteins: In vitro translation and processing. International Symposium on Plant Molecular Biology, Strasbourg, France, July 1986.

  58. deWit PJGM: Elicitation of active resistance mechanisms. In: Bailey JA (ed.) Biology and Molecular Biology of Plant-Pathogen Interactions. Springer-Verlag, Berlin (1986) pp. 149–169.

    Google Scholar 

  59. deWit PJGM, Spikman G: Evidence for the occurrence of race and cultivar-specific elicitors of necrosis in intercellular fluids of compatible interactions of Cladosporium fulvum and tomato. Physiol Plant Pathol 21: 1–11 (1982).

    Google Scholar 

  60. deWit PJGM, Van derMeer FE: Accumulation of the pathogenesis related tomato leaf protein P14 as an early indicator of incompatibility in the interaction between Cladosporium fulvum (syn Fulvia fulva) and tomato. Physiol Molec Plant Pathol 28: 203–214 (1986).

    Google Scholar 

  61. Dixon RA: The phytoalexin response: elicitation, signalling and control of host gene expression. Biol Rev 61: 239–291 (1986).

    Google Scholar 

  62. Dixon RA, Bailey JA, Bell JN, Bolwell GP, Cramer CL, Edwards K, Hamdan MAMS, Lamb CJ, Robbins MP, Ryder TB, Schuch W: Rapid changes in gene expression in response to microbial elicitation. Phil Trans R Soc Lond B 314: 411–426 (1986).

    Google Scholar 

  63. Dixon RA, Bolwell GP, Hamdan MAMS, Robbins MP: Molecular biology of induced resistance. In: Day PR, Jellis GJ (eds) Genetics and Pathogenesis. Blackwell Scientific Publications, Oxford (1987) pp. 245–259.

    Google Scholar 

  64. Dixon RA, Dey PM, Lamb CJ: Phytoalexins: enzymology and molecular biology. Adv Enz 55: 1–136 (1983).

    Google Scholar 

  65. Dixon RA, Lamb CJ: Stimulation of de novo synthesis of L-phenylalanine ammonia lyase in relation to phytoalexin accumulation in Colletotrichum lindemuthianum elicitor-treated cell suspension cultures of French bean (Phaseolus vulgaris). Biochim Biophys Acta 586: 453–463 (1979).

    Google Scholar 

  66. Doke N, Garas NA, Kuc J: Partial characterisation and aspects of the mode of action of a hypersensitivity-inhibiting factor (HIF) isolated from Phytophthora infestans. Physiol Plant Pathol 15: 127–140 (1979).

    Google Scholar 

  67. Doke N, Tomiyama K: Suppression of the hypersensitive response of potato tuber protoplasts to hyphal wall components by water soluble glucans isolated from Phytophthora infestans. Physiol Plant Pathol 16: 177–186 (1980).

    Google Scholar 

  68. Douglas C, Hoffman H, Schulz W, Hahlbrock K: Structure and elicitor or u.v.-light stimulated expression of two 4-coumarate:CoA ligase genes in parsley. EMBO J 6: 1189–1195 (1987).

    Google Scholar 

  69. Dudley MW, Dueber MT, West CA: Biosynthesis of the macrocyclic diterpene casbene in castor bean (Ricinus communis L.) seedlings. Changes in enzyme levels induced by fungal infection and intracellular localisation of the pathway. Plant Physiol 81: 335–342 (1986).

    Google Scholar 

  70. Dudley MW, Green TR, West CA: Biosynthesis of the macrocyclic diterpene casbene in castor bean (Ricinus communis L.) seedlings. The purification and properties of farnesyl transferase from elicited seedlings. Plant Physiol 81: 343–348 (1985).

    Google Scholar 

  71. Dueber MT, Adolf W, West CA: Biosynthesis of the diterpene phytoalexin casbene. Partial purification and characterisation of casbene synthetase from Ricinus communis. Plant Physiol 62: 598–603 (1978).

    Google Scholar 

  72. Ebel J: Induction of phytoalexin synthesis in plants following microbial infection or treatment with elicitors. In: Bioregulators: Chemistry and Uses. American Chemical Society, Washington DC, USA (1984) pp. 257–271.

    Google Scholar 

  73. Ebel J, Grisebach H, Bonhoff, Grab D, Hoffman C, Kochs G, Mieth H, Schmidt W, Stäb M: Phytoalexin synthesis in soybean following infection of roots with Phytophthora megasperma or treatment of cell cultures with fungal elicitor. In: Lugtenberg B (ed.) Recognition in Microbe-Plant Symbiotic Interactions. Springer-Verlag, Berlin (1986) pp. 345–361.

    Google Scholar 

  74. Ebel J, Schmidt WE, Loyal R: Phytoalexin synthesis in soybean cells: elicitor induction of phenylalanine ammonialyase and chalcone synthase mRNAs and correlation with phytoalexin accumulation. Arch Biochem Biophys 232: 240–248 (1984).

    Google Scholar 

  75. Edwards K, Cramer CL, Bolwell GP, Dixon RA, Schuch W, Lamb CJ: Rapid transient induction of phenylalanine ammonia-lyase mRNA in elicitor-treated bean cells. Proc Natl Acad Sci USA 82: 6731–6735 (1985).

    Google Scholar 

  76. Esnault R, Chibbar RN, Lee D, VanHuystee RB, Ward EWB: Early differences in production of mRNAs for phenylalanine ammonia-lyase and chalcone synthase in resistant and susceptible cultivars of soybean inoculated with Phytophthora megasperma f.sp. glycinea. Physiol Molec Plant Pathol 30: 293–297 (1987).

    Google Scholar 

  77. Esquerré-Tugayé M-T, Lafitte C, Mazau D, Toppan A, Touzé A: Cell surfaces in plant-microorganism interactions. II. Evidence for the accumulation of hydroxyproline-rich glycoproteins in the cell wall of diseased plants as a defense mechanism. Plant Physiol 64: 320–326 (1979).

    Google Scholar 

  78. Esquerré-Tugayé M-T, Lamport DTA: Cell surfaces in plant-microorganism interactions. I. A structural investigation of cell wall hydroxyproline-rich glycoproteins which accumulate in fungus-infected plants. Plant Physiol 64: 314–319 (1979).

    Google Scholar 

  79. Esquerré-Tugayé M-T, Mazau D, Pelissier B, Roby D, Toppan A: Elicitors and ethylene trigger defense responses in plants. In: Fuchs Y, Chalutz (eds) Ethylene: Biochemical, Physiological and Applied Aspects. Martinus Nijhoff, The Hague (1984) pp. 217–218.

    Google Scholar 

  80. Federation of British Plant Pathologists: A guide to the use of terms in plant pathology. Pathological Papers. no. 17 (1973).

  81. Flor HH: Current status of the gene-for-gene concept. Ann Rev Phytopathol 9: 275–296 (1971).

    Google Scholar 

  82. Fraenkel-Conrat H: RNA-directed polymerases of plants. CRC Critical Reviews Plant Sciences 4: 213–227 (1986).

    Google Scholar 

  83. Freeling M, Birchler JA: Mutant and variants of the alcohol dehydrogenase-12 gene in maize. In: Setlow, Hollaender A (eds) Genetic Engineering 3. Plenum Press, New York and London (1981) pp. 223–263.

    Google Scholar 

  84. Friend J: Phenolic substances and plant disease. Ann Proc Phytochem Soc 25: 367–392 (1985).

    Google Scholar 

  85. Friend J: Plant phenolics, lignification and plant disease. In: Rheinhold L, Harborne JB, Swain T (eds) Progress in Phytochemistry 7. Pergamon Press, Oxford (1981) pp. 197–261.

    Google Scholar 

  86. Friend J: Alterations in secondary metabolism. In: Ayres PG (ed.) Effects of Disease on the Physiology of the Growing Plant. Cambridge University Press, Cambridge (1982) pp. 179–200.

    Google Scholar 

  87. Fristensky B, Riggleman RC, Wagoner W, Hadwiger LA: Gene expression in susceptible and resistant interactions of peas induced with Fusarium solani pathogens and chitosin. Physiol Plant Pathol 27: 15–28 (1985).

    Google Scholar 

  88. Fry SC: Primary cell wall metabolism. Oxford Surv Plant Molec Cell Biol 2: 1–42 (1985).

    Google Scholar 

  89. Gabriel DW, Burges A, Lazo GR: Gene-for-gene interactions of five cloned avirulence genes from Xanthomonas campestris pv. malvacearum with specific resistance genes in cotton. Proc Natl Acad Sci USA 83: 6415–6419 (1986).

    Google Scholar 

  90. Goodman RN, Király Z, Wood KR: The Biochemistry and Physiology of Plant Disease. University of Missouri Press, Columbia, Missouri, USA (1986).

    Google Scholar 

  91. Grab D, Loyal R, Ebel J: Elicitor-induced phytoalexin synthesis in soybean cells. Changes in the activity of chalcone synthase mRNA and the total population of translatable mRNA. Arch Biochem Biophys 243: 523–529 (1985).

    Google Scholar 

  92. Graham JS, Hall G, Pearce G, Ryan CA: Regulation of synthesis of proteinase inhibitors I and II mRNAs in leaves of wounded tomato plants. Planta 169: 399–405 (1986).

    Google Scholar 

  93. Graham JS, Pearce G, Merryweather J, Titani K, Ericsson LH, Ryan CA: Wound-induced proteinase inhibitors from tomato leaves. I. The cDNA-deduced primary structure of pre-inhibitor I and its post-translational processing. J Biol Chem 260: 6555–6560 (1985).

    Google Scholar 

  94. Graham JS, Pearce G, Merrywheather J, Titani K, Ericsson LH, Ryan CA: Wound-induced proteinase inhibitors from tomato leaves. II. The cDNA-deduced primary structure of pre-inhibitor II. J Biol Chem 260: 6561–6564 (1985).

    Google Scholar 

  95. Grand C, Rossignol M: Changes in the lignification process of induced by localised infection of muskmelons with Colletotrichum lagenarium. P1 Sci Lett 28: 103–110 (1982).

    Google Scholar 

  96. Grand C, Walter M, Sarni F, Lamb CJ: Elicitation at the mRNA level of cinnamyl alcohol dehydrogenase, a specific enzyme of lignification in bean cell suspension cultures. International Symposium on Plant Molecular Biology, Strasbourg, July 1986.

  97. Grisebach H: Lignins. In: Stumpf P, Conn EE (eds) The Biochemistry of Plants, Vol. 7. Academic Press, London (1981) pp. 457–478.

    Google Scholar 

  98. Hadwiger LA, Daniels C, Fristensky BW, Kendra DF, Wagoner W: Pea genes associated with the non-host resistance to Fusarium solani are also induced by chitosin and in race-specific resistance by Pseudomonas syringae. In: Bailey J (ed.) Biology and Molecular Biology of Plant-Pathogen Interactions. Springer-Verlag, Berlin (1986) pp. 263–269.

    Google Scholar 

  99. Hadwiger LA, Loschke DC: Molecular communication in host-parasite interactions: hexosamine polymers (chitosin) as regulator compounds in race-specific and other interactions. Phytopathology 71: 756–761 (1981).

    Google Scholar 

  100. Hadwiger LA, Wagoner W: Electrophoretic patterns of pea and Fusarium solani proteins synthesised in vitro or in vivo which characterise the compatible and incompatible interactions. Physiol Plant Pathol 23: 153–162 (1983).

    Google Scholar 

  101. Hadwiger LA, Wagoner W: Effect of heat shock on the mRNA-directed disease resistance response of peas. Plant Physiol 72: 553–556 (1983).

    Google Scholar 

  102. Hahlbrock K, Chappell J, Kuhn DN: Rapid induction of mRNAs involved in defense reactions in plants. In: Lea PJ, Stewart GR (eds) The Genetic Manipulation of Plants and its Application to Agriculture. Clarendon Press, Oxford (1984) pp. 171–182.

    Google Scholar 

  103. Hahlbrock K, Cuypers B, Douglas C, Fritzemeier KH, Hoffman H, Rohwer F, Scheel D, Schulz W: Biochemical interactions of plants with potentially pathogenic fungi. In: Lugtenberg B (ed.) Recognition in Microbe-Plant Symbiotic Interactions. Springer-Verlag, Berlin (1986) pp. 311–323.

    Google Scholar 

  104. Hahlbrock K, Grisebach H: Enzymic controls in the biosynthesis or lignin and flavonoids. Ann Rev Plant Physiol 30: 105–130 (1979).

    Google Scholar 

  105. Hahlbrock K, Lamb CJ, Purwin C, Ebel J, Fautz E, Schäfer E: Rapid response of suspension-cultured parsley cells to the elicitor from Phytophthora megasperma var. sojae. Induction of the enzymes of general phenylpropanoid metabolism. Plant Physiol 67: 768–773 (1981).

    Google Scholar 

  106. Hamdan MAMS, Dixon RA: Differential biochemical effects of elicitor preparations from Colletotrichum lindemuthianum. Physiol Molec Plant Pathol 28: 329–344 (1986).

    Google Scholar 

  107. Hammerschmidt R, Lamport DTA, Muldoon EP: Cell wall hydroxyproline enhancement and lignin deposition as an early event in the resistance of cucumber to Cladosporium cucumerinum. Physiol Plant Pathol 24: 43–47 (1984).

    Google Scholar 

  108. Heath MC: Hypersensitivity, the cause or the consequence of rust resistance? Phytopathology 66: 935–936 (1976).

    Google Scholar 

  109. Heath MC: A generalised concept of host-parasite specificity. Phytopathology 71: 1121–1123 (1981).

    Google Scholar 

  110. Heath MC: The absence of active defence mechanisms in compatible host-pathogen interactions. In: Wood RKS (ed.) Active Defence Mechanisms in Plants. Plenum Press, London (1982) pp. 143–156.

    Google Scholar 

  111. Henderson SJ, Friend J: Increase in PAL and lignin-like compounds as race-specific resistance responses of potato tubers to Phytophthora infestans. Phytopathol Z 94: 323–334 (1979).

    Google Scholar 

  112. Higgins VJ, deWit PJGM: Use of race- and cultivar-specific elicitors from intercellular fluids for characterising races of Cladosporium fulvum and resistant tomato cultivars. Phytopathology 75: 695–699 (1985).

    Google Scholar 

  113. Hille A, Purwin C, Ebel J: Induction of enzymes of phytoalexin synthesis in cultured soybean cells by an elicitor from Phytophthora megasperma f.sp. glycinea. Plant Cell Reports 1: 123–127 (1982).

    Google Scholar 

  114. Holden DW, Rohringer R: Peroxidases and glycosidases in intercellular fluids from noninoculated and rust-affected wheat leaves. Plant Physiol 79: 820–824 (1985).

    Google Scholar 

  115. Hooftvan Huijsduijnen RAM, Cornelissen BJC, VanLoon LC, VanBoom JH, Tromp M, Bol JF: Virus-induced synthesis of messenger RNAs for precursors of pathogenesis-related proteins in tobacco. EMBO J 4: 2167–2171 (1985).

    Google Scholar 

  116. Hooftvan Huijsduijnen RAM, VanLoon LC, Bol JF: cDNA cloning of six mRNAs induced by TMV infection of tobacco and a characterisation of their translation products. EMBO J 5: 2057–2061 (1986).

    Google Scholar 

  117. Jamet E, Kopp M, Fritig B: The pathogenesis-related proteins of tobacco: their labelling from [14C] amino acids in leaves reacting hypersensitively to infection by tobacco mosaic virus. Physiol Plant Pathol 27: 29–41 (1985).

    Google Scholar 

  118. Jensen EØ, Hein J, Paludan K, Marcker KA: The soybean leghaemoglobin family. In: Goldberg R (ed.). Plant Molecular Biology. Alan R. Liss, New York (1983) pp. 367–379.

    Google Scholar 

  119. Kauss H: Callose biosynthesis as a Ca2+-regulated process and possible relations to the induction of other metabolic changes. In: Roberts K, Johnston AWB, Lloyd CW, Shaw P, Woolhouse HW (eds). The Cell Surface in Plant Growth and Development. J Cell Sci Supplement 2. The Company of Biologists Ltd., Cambridge, England (1985) pp. 89–103.

    Google Scholar 

  120. Keen NT: Specific elicitors of plant phytoalexin production: determinants of race specificity in pathogens? Science 187: 74–75 (1975).

    Google Scholar 

  121. Keen NT, Ersek T, Long M, Bruegger B, Holliday M: Inhibition of the hypersensitive reaction of soybean leaves to incompatible Pseudomonas spp. by blastocidin S, streptomycin or elevated temperature. Physiol Plant Pathol 18: 325–337 (1981).

    Google Scholar 

  122. Keen NT, Legrand M: Surface glycoproteins: evidence that they may function as the race specific phytoalexin elicitors of Phytophthora megasperma f.sp. glycinea. Physiol Plant Pathol 17: 175–192 (1980).

    Google Scholar 

  123. Keen NT, Staskawicz BJ: Gene cloning as an approach to understanding specificity in plant-pathogen systems. In: Dugger WM, Bartnicki-Garcia S (eds) Structure, Function and Biosynthesis of Plant Cell Walls. Proc 7th Symp Bot, University of California, Riverside (1984) pp. 344–358.

    Google Scholar 

  124. Keen NT, Yoshikawa M: β-1,3-endoglucanase from soybean releases elicitor-active carbohydrates from fungus cell walls. Plant Physiol 71: 460–465 (1983).

    Google Scholar 

  125. Keen NT, Yoshikawa M, Wang MC: Phytoalexin elicitor activity of carbohydrates from Phytophthora megasperma f.sp. glycinea and other sources. Plant Physiol 71: 466–471 (1983).

    Google Scholar 

  126. Klement Z: Hypersensitivity. In: Mount MS, Lacy GH (eds) Phytopathogenic Prokaryotes, Vol. II. Academic Press, London (1982) pp. 149–177.

    Google Scholar 

  127. Koch S, Grisebach H: Enzymatic synthesis of isoflavones. Eur J Biochem 155: 311–318 (1986).

    Google Scholar 

  128. Köhle H, Jehlick W, Poten F, Blaschek W, Kauss H: Chitosin-elicited callose synthesis in soybean cells as a Ca2+-dependent process. Plant Physiol 77: 544–551 (1985).

    Google Scholar 

  129. Kombrink E, Bollmann J, Hauffe KD, Knogge W, Scheel D, Schmelzer E, Somssich I, Hahlbrock K: Biochemical responses of non-host plant cells to fungi and fungal elicitors. In: Bailey JA (ed.) Biology and Molecular Biology of Plant-Pathogen Interactions. Springer-Verlag, Berlin (1986). pp. 253–262.

    Google Scholar 

  130. Kombrink E, Hahlbrock K: Responses of cultured parsley cells to elicitors from pathogenic fungi. Plant Physiol 81: 216–221 (1986).

    Google Scholar 

  131. Kreuzaler F, Ragg H, Fautz E, Kuhn DN, Hahlbrock K: UV-induction of chalcone synthase mRNA in cell suspension cultures of Petroselinum hortense. Proc Natl Acad Sci USA 80: 2591–2593 (1983).

    Google Scholar 

  132. Kuhn DN, Chappell J, Boudet A, Hahlbrock K: Induction of phenylalanine ammonia-lyase and 4-coumarate:CoA ligase mRNAs in cultured plant cells by UV light or fungal elicitor. Proc Natl Acad Sci USA 81: 1102–1106 (1984).

    Google Scholar 

  133. Lamb CJ, Corbin DR, Lawton MA, Sauer N, Wingate VPM: Recognition and response in plants:pathogen interactions. In: Lugtenberg B (ed.) Recognition in Microbe-Plant Symbiotic Interactions. Springer-Verlag, Berlin (1986) pp. 333–344.

    Google Scholar 

  134. Lawton MA, Dixon RA, Hahlbrock K, Lamb CJ: Rapid induction of the synthesis of phenylalanine ammonia-lyase and of chalcone synthase in elicitor-treated plant cells. Eur J Biochem 129: 593–601 (1983).

    Google Scholar 

  135. Lawton MA, Dixon RA, Hahlbrock K, Lamb CJ: Elicitor induction of mRNA activity. Rapid effects of elicitor on phenylalanine ammonia-lyase and chalcone synthase mRNA activities in bean cells. Eur J Biochem 130: 131–139 (1983).

    Google Scholar 

  136. Lee JS, Brown WE, Graham JS, Pearce G, Fox EA, Dreher TW, Ahern KG, Pearson GD, Ryan CA: Molecular characterisation and phylogenetic studies of a wound-inducible proteinase inhibitor I gene in Lycopersicon species. Proc Natl Acad Sci USA 83: 7277–7281 (1986).

    Google Scholar 

  137. Lee S-C, West CA: Polygalacturonase from Rhizopus stolonifer, an elicitor of casbene synthetase activity in castor bean (Ricinus communis L.) seedlings. Plant Physiol 67: 633–639 (1981).

    Google Scholar 

  138. Legrand M: Phenylpropanoid metabolism and its regulation in disease. In: Callow J (ed.) Biochemical Plant Pathology. Wiley, New York (1983) pp. 367–384.

    Google Scholar 

  139. Loschke DC, Hadwiger LA, Wagoner W: Comparison of mRNA populations coding for phenylalanine ammonia lyase and other peptides from pea tissue treated with biotic and abiotic phytoalexin inducers. Physiol Plant Pathol 23: 163–173 (1983).

    Google Scholar 

  140. Lucas J, Camacho Henriquez A, Lottspeich F, Henschen A, Sänger HL: Amino acid sequence of the “pathogenesis-related” leaf protein p14 from viroid-infected tomato reveals a new type of structurally unfamiliar proteins. EMBO J 4: 2745–2749 (1985).

    Google Scholar 

  141. Lyon F, Wood RKS: The hypersensitive reaction and other responses of bean leaves to bacteria. Ann Bot 40: 479–491 (1976).

    Google Scholar 

  142. Lyon F, Wood RKS: Alteration of response of bean leaves to compatible and incompatible bacteria. Ann Bot 41: 359–367 (1977).

    Google Scholar 

  143. Lyon GD, Albersheim P: The nature of the phytoalexin elicitor of Erwinia carotovora. Plant Physiol 74: 61–64 (1984).

    Google Scholar 

  144. Manners JM, Davidson AD, Scott KJ: Patterns of post-infectional protein synthesis in barley carrying different genes for resistance to the powdery mildew fungus. Plant Molec Biol 4: 275–283 (1985).

    Google Scholar 

  145. Mansfield JW: Recognition, elicitors and the hypersensitive reaction. In: Lugtenberg B (ed.) Recognition in Microbe-Plant Symbiotic and Pathogenic Interactions. Springer-Verlag, Berlin (1986) pp. 433–437.

    Google Scholar 

  146. Mason PJ, Williams JG: Hybridisation in the analysis of recombinant DNA. In: Hames BD, Higgins SJ (eds) Nucleic Acid Hybridisation: A Practical Approach. IRL Press, Oxford (1985) pp. 113–137.

    Google Scholar 

  147. Mauch F, Hadwiger LA, Boller T: Ethylene: symptom, not signal for the induction of chitinase and β-1,3-glucanase in pea pods by pathogens and elicitors. Plant Physiol 76: 607–611 (1984).

    Google Scholar 

  148. Maule AJ, Ride JP: Ammonia-lyase and O-methyl transferase activities related to lignification in wheat leaves infected with Botrytis. Phytochemistry 15: 1661–1664 (1976).

    Google Scholar 

  149. Maule AJ, Ride JP: Cinnamate 4-hydroxylase and hydroxycinnamate: CoA ligase in wheat leaves infected with Botrytis cinerea. Phytochemistry 22: 1113–1116 (1983).

    Google Scholar 

  150. Maunders MJ, Holdworth MJ, Slater A, Knapp JE, Bird CR, Schuch W, Grierson D: Ethylene stimulates the accumulation of ripening-related mRNAs in tomatoes. Plant Cell Env 10: 177–184 (1987).

    Google Scholar 

  151. Mazau D, Esquerré-Tugayé M-T: Hydroxyproline-rich glycoprotein accumulation in the cell walls of plants infected by various pathogens. Physiol Molec Plant Pathol 29: 147–157 (1986).

    Google Scholar 

  152. Moesta P, West CA: Casbene synthetase: regulation of phytoalexin biosynthesis in Ricinus communis L. seedlings. Purification of casbene synthetase and regulation of its biosynthesis during elicitation. Arch Biochem Biophys 238: 325–333 (1985).

    Google Scholar 

  153. Nichols EJ, Beckman JM, Hadwiger LA: Glycosidic enzyme activity in pea tissue and pea-Fusarium solani interactions. Plant Physiol 66: 199–204 (1980).

    Google Scholar 

  154. Olsen Larsen P: Glucosinolates. In: Stumpf P, Conn EE (eds) The Biochemistry of Plants, Vol. 7. Academic Press, London (1981) pp. 501–525.

    Google Scholar 

  155. Pavlovkin J, Novacky A, Ullrich-Eberius CI: Membrane potential changes during bacteria-induced hypersensitive reaction. Physiol Molec Plant Pathol 28: 125–135 (1986).

    Google Scholar 

  156. Pegg GF, Young DH: Purification and characterisation of chitinase enzyme from healthy and Verticilium albo-atrum-infected tomato plants, and V. albo-atrum. Physiol Plant Pathol 21: 389–409 (1982).

    Google Scholar 

  157. Pelissier B, Thibaud JB, Grignon C, Esquerré-Tugayé MT: Cell surfaces in plant-microorganism interactions. VII. Elicitor preparations from two fungal pathogens depolarise plant membranes. Plant Science 46: 103–109 (1986).

    Google Scholar 

  158. Reimold U, Kröger M, Kreuzaler F, Hahlbrock K: Coding and 3′ non-coding nucleotide sequence of chalcone synthase mRNA and assignment of amino acid sequence of the enzyme. EMBO J 2: 1801–1805 (1983).

    Google Scholar 

  159. Riggleman RC, Fristensky B, Hadwiger LA: The disease resistance response in pea is associated with increased levels of specific mRNAs. Plant Molec Biol 4: 81–86 (1985).

    Google Scholar 

  160. Robbins MP, Bolwell GP, Dixon RA: Metabolic changes in elicitor-treated bean cells. Selectivity of enzyme induction in relation to phytoalexin accumulation. Eur J Biochem 148: 563–569 (1985).

    Google Scholar 

  161. Robbins MP, Dixon RA: Induction of chalcone isomerase in elicitor-treated bean cells. Comparison of rates of synthesis and appearance of immunodetectable enzyme. Eur J Biochem 145: 195–202 (1984).

    Google Scholar 

  162. Robertson B: Elicitors of the production of lignin-like compounds in cucumber hypocotyls. Physiol Molec Plant Pathol 28: 137–148 (1986).

    Google Scholar 

  163. Robertson JG, Wells B, Brewin MJ, Williams MA: Immunogold localisation of cellular constituents in the legume-Rhizobium symbiosis. Oxford Surveys Plant Molec Biol 2: 69–89 (1985).

    Google Scholar 

  164. Roby D, Ranty B, Marco Y: Ribulose 1,5-bisphosphate carboxylase expression in melon plants infected with Colletotrichum lagenarium (Abs.). International Symposium Plant Molecular Biology, Strasbourg, July 1986.

  165. Roby D, Toppan A, Esquerré-Tugayé M-T: Cell surfaces in plant-microorganism interactions. V. Elicitors of fungal and of plant origin trigger the synthesis of ethylene and of cell wall hydroxyproline-rich glycoprotein in plants. Plant Physiol 77: 700–704 (1985).

    Google Scholar 

  166. Roby D, Toppan A, Esquerré-Tugayé M-T: Cell surfaces in plant-microorganism interactions. VI. Elicitors of ethylene from Colletotrichum lagenarium trigger chitinase activity in melon plants. Plant Physiol 81: 228–233 (1986).

    Google Scholar 

  167. Ryan CA: Proteinase inhibitors in plant leaves: a biochemical model for pest-induced natural plant protection. TIBS 3: 148–150 (1978).

    Google Scholar 

  168. Ryan CA: Proteinase inhibitors. In: Stumpf PK, Conn EE (eds) Biochemistry of Plants, Vol. 6. Academic Press, London (1981) pp. 351–370.

    Google Scholar 

  169. Ryder TB, Cramer CL, Bell JN, Robbins MP, Dixon RA, Lamb CJ: Elicitor rapidly induces chalcone synthase mRNA in Phaseolus vulgaris cells at the onset of the phytoalexin defense response. Proc Natl Acad Sci USA 81: 5724–5728 (1984).

    Google Scholar 

  170. Sachs MM, Ho T-HD: Alteration of gene expression during environmental stress in plants. Ann Rev Plant Physiol 37: 363–376 (1986).

    Google Scholar 

  171. Sanchez-Serrano J, Schmidt R, Schell J, Willmitzer L: Nucleotide sequence of proteinase inhibitor II encoding cDNA of potato (Solanum tuberosum) and its mode of expression. Molec Gen Genet 203: 15–20 (1986).

    Google Scholar 

  172. Schlumbaum A, Mauch F, Vögeli U, Boller T: Plant chitinases are potent inhibitors of fungal growth. Nature 324: 365–367 (1986).

    Google Scholar 

  173. Schmelzer E, Börner H, Grisebach H, Ebel J, Hahlbrock K: Phytoalexin synthesis in soybean (Glycine max). Similar timecourse of mRNA induction in hypocotyls infected with a fungal pathogen and in cell cultures treated with fungal elicitor. FEBS Lett 172: 59–63 (1984).

    Google Scholar 

  174. Schöffl F, Baumann G, Raschke E, Bevan M: The expression of heat-shock genes in higher plants. Phil Trans Roy Soc Lond B 314: 453–468 (1986).

    Google Scholar 

  175. Schöffl F, Lin C-Y, Key JL: Soybean heat shock proteins: temperature regulated gene expression and the development of thermotolerance. In: Lea PJ, Stewart GR (eds) The Genetic Manipulation of Plants and its Applications to Agriculture. Clarendon Press, Oxford (1984) pp. 129–140.

    Google Scholar 

  176. Sen R, Baltimore D: Multiple nuclear factors interact with the immunoglobulin enhancer sequences. Cell 46: 705–716 (1986).

    Google Scholar 

  177. Shimomura T, Dijkstra J: The occurrence of callose during the progress of local lesion formation. Neth J Plant Pathol 81: 107–121 (1975).

    Google Scholar 

  178. Shirras AD, Northcote DH: Molecular cloning and characterisation of cDNAs complementary to mRNAs from wounded potato (Solanum tuberosum) tuber tissue. Planta 162: 353–360 (1984).

    Google Scholar 

  179. Showalter AM, Bell JN, Cramer CL, Bailey JA, Varner JE, Lamb CJ: Accumulation of hydroxyproline-rich glycoprotein mRNAs in response to fungal elicitor and infection. Proc Natl Acad Sci USA 82: 6551–6555 (1985).

    Google Scholar 

  180. Slater A, Maunders MJ, Edwards K, Schuch W, Grierson D: Isolation and characterisation of cDNA clones for tomato polygalacturonase and other ripening-related proteins. Plant Molec Biol 5: 137–147 (1985).

    Google Scholar 

  181. Slusarenko AJ: Gene expression and resistance of French bean to Pseudomonas phaseolicola. In: Day PR, Jellis GJ (eds) Genetics and Plant Pathogenesis. Blackwell, Oxford (1987) pp. 50–64.

    Google Scholar 

  182. Slusarenko AJ, Longland A: Changes in gene activity during expression of the hypersensitive response in Phaseolus vulgaris cv. “Red Mexican” to an avirulent race 1 isolate of Pseudomonas syringae pv. phaseolicola. Physiol Molec Plant Pathol 29: 79–94 (1986).

    Google Scholar 

  183. Slusarenko AJ, Longland A, Friend J: Expression of plant genes in the hypersensitive reaction of French bean (Phaseolus vulgaris) to the plant pathogenic bacterium Pseudomonas syringae pv. phaseolicola. In: Lugtenberg B (ed.) Recognition in Microbe-Plant Symbiotic and Pathogenic Interactions. Spring-VeVerlag, Berlin (1986) pp. 367–376

    Google Scholar 

  184. Smart TE, Dunigen DD, Zaitlin M: In vitro translation of mRNAs derived from TMV-infected tobacco exhibiting a hypersensitive response. Virology 158 (in press).

  185. Smith DA, Banks SW: Biosynthesis, elicitation and biological activity of isoflavonoid phytoalexins. Phytochemistry 25: 979–995 (1986).

    Google Scholar 

  186. Somssich IE, Schmelzer E, Bollmann J, Hahlbrock K: Rapid activation by fungal elicitor of genes encoding “pathogenesis-related” proteins in cultured parsley cells. Proc Natl Acad Sci USA 83: 2427–2430 (1986).

    Google Scholar 

  187. Staskawicz BJ, Dahlbeck D, Keen NT: Cloned avirulence gene of Pseudomonas syringae pv. glycinea determines race incompatibility on Glycine max (L.) Merr. Proc Natl Acad Sci USA 81: 6024–6028 (1984).

    Google Scholar 

  188. Toppan A, Esquerré-Tugayé M-T: Cell surfaces in plant-microorganism interactions. IV. Fungal glycopeptides which elicit the synthesis of ethylene in plants. Plant Physiol 75: 1133–1138 (1984).

    Google Scholar 

  189. Toppan A, Roby D, Esquerré-Tugayé M-T: Cell surfaces in plant-microorganism interactions. III. In vivo effect on hydroxyproline-rich glycoprotein accumulation in the cell wall of diseased plants. Plant Physiol 70: 82–86 (1982).

    Google Scholar 

  190. Vance CP, Anderson JO, Sherwood RT: Soluble and cell wall peroxidases in reed canary grass in relation to disease resistance and localised lignin formation. Plant Physiol 57: 920–922 (1976).

    Google Scholar 

  191. Vance CP, Kirk TK, Sherwood RT: Lignification as a mechanism of disease resistance. Ann Rev Phytopathol 18: 259–288 (1980).

    Google Scholar 

  192. Vance CP, Sherwood RT: Regulation of lignin formation in reed canary grass in relation to disease resistance. Plant Physiol 57: 915–919 (1976).

    Google Scholar 

  193. VanLoon LC: Pathogenesis-related proteins. Plant Molec Biol 4: 111–116 (1985).

    Google Scholar 

  194. Verma DPS, Fortin MG, Stanley J, Mauro VP, Purohit S, Morrison N: Nodulins and nodulin genes of Glycine max. Plant Molec Biol 7: 51–61 (1986).

    Google Scholar 

  195. Voisey CR, Slusarenko AJ: Endochitinase mRNA and enzyme levels in Phaseolus vulgaris (L.) show faster increase in response to avirulent than to virulent cells of Pseudomonas syringae pv. phaseolicola. Submitted for publication.

  196. vonHippel PH, Bear DG, Morgan MD, McSwiggen JA: Protein-nucleic acid interactions in transcription. Ann Rev Biochem 53: 389–446 (1984).

    Google Scholar 

  197. Wagoner W, Loschke DC, Hadwiger LA: Two-dimensional electrophoretic analysis of in vivo and in vitro synthesis of proteins in peas inoculated with compatible and incompatible Fusarium solani. Physiol Plant Pathol 20: 99–107 (1982).

    Google Scholar 

  198. Walker-Simmons M, Ryan CA: Immunological identification of proteinase inhibitors I and II in isolated tomato leaf vacuoles. Plant Physiol 60: 61–63 (1977).

    Google Scholar 

  199. Wang TL: Immunology in Plant Science. Cambridge University Press, Cambridge, England (1986).

    Google Scholar 

  200. White RF: Acetylsalicylic acid (Aspirin) induces resistance to tobacco mosaic virus in tobacco. Virol 99: 410–412 (1979).

    Google Scholar 

  201. Williams JG: The preparation and screening of a cDNA clone bank. In: Williamson R (ed.) Genetic Engineering 1. Academic Press, London (1981) pp. 1–59.

    Google Scholar 

  202. Wilson LG, Fry JC: Extensin-a major cell wall glycoprotein. Plant Cell Env 9: 239–260 (1986).

    Google Scholar 

  203. Wu C: Activating protein factor binds in vitro to upstream control sequences in heat shock gene chromatin. Nature 311: 81–84 (1984).

    Google Scholar 

Download references

Author information

Author notes

  1. David B. Collinge

    Present address: Den kgl Veterinær- og Landbohøjskole, Institut for Plantefysiologi, Thorvaldsensvej 40, 1871, Frederiksberg, Denmark

Authors and Affiliations

  1. John Innes Institute, Colney Lane, NR4 7UH, Norwich, UK

    David B. Collinge & Alan J. Slusarenko

Authors
  1. David B. Collinge
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Alan J. Slusarenko
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Collinge, D.B., Slusarenko, A.J. Plant gene expression in response to pathogens. Plant Mol Biol 9, 389–410 (1987). https://doi.org/10.1007/BF00014913

Download citation

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00014913

Keywords

Search

Navigation