European Journal of Plant Pathology

, Volume 102, Issue 6, pp 511–517 | Cite as

Production ofErwinia chrysanthemi pectinases in potato tubers showing high or low level of resistance to soft-rot

  • Corinne Dorel
  • Nicole Hugouvieux-Cotte-Pattat
  • Janine Robert-Baudouy
  • Ewa Lojkowska
Research Articles


Erwinia chrysanthemi was used for inoculation of two lines of potato tubers with different degrees of resistance to soft-rot: cultivar Katahdin, a very sensitive material, and the somatic hybrid ofSolanum brevidens andSolanum tuberosum as a resistant plant. Infection was performed with theE. chrysanthemi wild-type strain 3937 and various mutants containing a transcriptional fusion of one pectinase gene (pem, pelA orpelE), together with the reporter genegus. Compared with the susceptible tubers, the accumulation of pectate lyase in the resistant tubers is limited. This limitation of the pectate lyase production seems to take place at the transcriptional level, with a striking decrease of the expression of thepelA::gus fusion and a decrease in the first steps of infection of thepelE::gus fusion expression. The pectinase genes appeared to be differentially regulated in the two potato lines. This study also revealed the major role of pectin methyl esterase in the infection process which occurs in potato tubers resistant to soft-rot. Indeed, the maceration of somatic hybrid tubers by thepem mutant was strongly reduced in comparison with the wild-type. We suggest that the resistant tubers have the advantage of a high methylated pectin which is difficult to degrade by theE. chrysanthemi pectinases.

Key words

pectate lyase pectin methyl esterase soft-rot Erwinia somatic hybrids Solanum brevidens 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Austin S, Lojkowska E, Ehlenfeldt MK, Kelman A and Helgeson JP (1988) Fertile interspecific somatic hybrids ofSolanum: a novel source of resistance toEnvinia soft rot. Phytopathology 78: 1216–1220Google Scholar
  2. Barras F, Van Gijsegem F and Chatterjee AK (1994) Extracellular enzymes and pathogenesis of soft-rotErwinia Annual Review of Phytopathology 32: 201–234Google Scholar
  3. Bardonnet N and Blanco C (1992)uidA antibiotic resistance cassettes forinsertion mutagenesis, gene fusion and genetic constructions. FEMS Letters 93: 243–248Google Scholar
  4. Beaulieu C, Boccara M and Vangijsegem F (1993) Pathogenic behavior of pectinase-defectiveErwinia chrysanthemi mutants on different plants. Molecular Plant-Microbe Interactions 6: 197–202Google Scholar
  5. Bertheau Y, Madgidi-Hervan E, Kotoujansky A, Nguyen-The C, Andro T and Coleno A (1984) Detection of depolymerase isoenzymes after electrophoresis or electrofocusing, or in titration curves. Analytical Biochemistry 139: 383–389PubMedGoogle Scholar
  6. Boccara M, Diolez A, Rouve M and Kotoujansky A (1988) The role of individual pectate lyases ofErwinia chrysanthemi strain 3937 in pathogenicity onSaintpaulia plants. Physiological and Molecular Plant Pathology 33: 95–104Google Scholar
  7. Boccara M and Chatain V (1989) Regulation and role in pathogenicity ofErwinia chrysanthemi 3937 pectin methylesterase. Journal of Bacteriology 171: 4085–4087PubMedGoogle Scholar
  8. Boccara M, Vedel R, Lalo D, Lebrun M and Lafay JF (1992) Genetic diversity and host range in strains ofErwinia chrysanthemi. Molecular Plant-Microbe Interactions. 5: 293–298Google Scholar
  9. Bourson C, Favey S, Reverchon S and Robert-Baudouy J (1993) Regulation of the expression of apelA::uidA fusion inErwinia chrysanthemi and demonstration of the synergistic action of plant extract with polygalacturonate on pectate lyase synthesis. Journal of General Microbiology 139: 1–9PubMedGoogle Scholar
  10. Collmer A and Keen NT (1986) The role of pectic enzymes in plant pathogenesis. Annual Review of Phytopathology 24: 383–409Google Scholar
  11. Hugouvieux-Cotte-Pattat N and Robert-Baudouy J (1989) Isolation ofErwinia chrysanthemi mutants altered in pectinolytic enzyme production. Molecular Microbiology 3: 1587–1597PubMedGoogle Scholar
  12. Hugouvieux-Cotte-Pattat N, Dominguez H and Robert-Baudouy J (1992) Environmental conditions affect the transcription of the pectinase genes ofErwinia chrysanthemi 3937. Journal of Bacteriology 174: 7807–7818PubMedGoogle Scholar
  13. Kotoujansky A (1987) Molecular genetics of pathogenesis by soft-rot Envinias. Annual Review of Phytopathology 25: 405–430Google Scholar
  14. Lojkowska E and Kelman A (1989) Screening of seedlings of wildSolanum species for resistance to bacterial stem rot caused by soft rot Erwinias. American Potato Journal 66: 379–390Google Scholar
  15. Lojkowska E, Dorel C, Reignault P, Hugouvieux-Cotte-Pattat N and Robert-Baudouy J (1993) Use of GUS fusion to study the expression ofErwinia chrysanthemi pectinase genes during infection of potato tubers. Molecular Plant-Microbe Interactions 6: 488–494Google Scholar
  16. Lojkowska E and Kelman A (1994) Comparison of the effectiveness of different methods of screening for bacterial soft rot resistance of potato tubers. American Potato Journal 71: 99–113Google Scholar
  17. Maher EA and Kelman A (1983) Oxygen status of potato tuber tissue in relation to maceration by pectic enzymes ofErwinia carotovora. Phytopathology 73: 536–539Google Scholar
  18. Masclaux C, Hugouvieux-Cotte-Pattat N and Expert D (1996) Iron is a triggering factor for differential expression ofErwinia chrysanthemi 3937 pectate lyases in pathogenesis of african violets. Molecular Plant Microbe Interactions (In press)Google Scholar
  19. McMillan GP, Hedley and Perombelon MCM (1993a) Activation of pectate lyase fromErwinia carotovora subsp.atroseptica by potato tuber tissue extract. Physiological and Molecular Plant Pathology 42: 1–8Google Scholar
  20. McMillan GP, Hedley D, Fyffe L and Perombelon MCM (1993b) Potato resistance to soft-rot Erwinias is related to cell wall pectin esterification. Physiological and Molecular Plant Pathology 42: 279–289Google Scholar
  21. Moran F, Nasuno S and Starr MP (1968) Extracellular and intracellular polygalacturonic trans-eliminases ofErwinia carotovora. Archives of Biochemistry and Biophysic 123: 293–306Google Scholar
  22. Nasser W, Reverchon S, Condemine G and Robert-Baudouy J (1994) Specific interactions ofErwinia chrysanthemi KdgR repressor with different operators of genes involved in pectinolysis. Journal of Molecular Biology 236: 427–440PubMedGoogle Scholar
  23. Preston J, Rice J, Ingram L and Keen N (1992) Differential depolymerization mechanisms of Pectate Lyases secreted byE. chrysanthemi EC16. Journal of Bacteriology 174: 2039–2042PubMedGoogle Scholar
  24. Reverchon S, Hugouvieux-Cotte-Pattat N, Condemine G, Bourson C, Arpin C and Robert-Baudouy J (1990) Pectinolysis regulation inErwinia chrysanthemi. In: Klement Z (ed) Plant Pathogenic Bacteria (pp. 739–744) Akademiai Kiado, BudapestGoogle Scholar
  25. Reverchon S, Nasser W and Robert-Baudouy J (1994)pecS: a locus controlling pectinase, cellulase and blue pigment production inErwinia chrysanthemi. Molecular Microbiology 11: 1127–1139PubMedGoogle Scholar
  26. Sauvage C and Expert D (1994) Differential regulation by iron ofErwinia chrysanthemi pectate lyases: pathologenicity of iron transport regulatory (cbr) mutants. Molecular Plant-Microbe Interactions 7: 71–77Google Scholar
  27. Surgey N, Robert-Baudouy J and Condemine G (1996) TheErwinia chrysanthemi pecT gene regulates pectinase gene expression. Journal of Bacteriology 178: 1593–1599PubMedGoogle Scholar
  28. Yang Z, Cramer CL and Lacy GH (1992)Erwinia carotovora subsp.carotovora pectic enzymes:in planta gene activation and roles in soft rot pathogenesis. Molecular Plant-Microbe Interactions 5: 104–112Google Scholar

Copyright information

© Kluwer Academic Publishers 1996

Authors and Affiliations

  • Corinne Dorel
    • 1
  • Nicole Hugouvieux-Cotte-Pattat
    • 1
  • Janine Robert-Baudouy
    • 1
  • Ewa Lojkowska
    • 2
  1. 1.Laboratoire de Génétique Moléculaire des Microorganismes et des Interactions CellulairesCNRS UMR 5577, Institut National des Sciences AppliquéesVilleurbanneFrance
  2. 2.Biochemical LaboratoryInstitute for Potato ResearchBoninPoland

Personalised recommendations