1887

Abstract

Pectin methylesterase (PME) was purified from the supernatant of strain Bd90. SDS-PAGE showed a single band at 42 kDa, but this band corresponded to two distinct isoforms observed by IEF-PAGE at pl values of 7.0 and 7.4. PME was produced during the exponential phase of fungal growth and independently of the carbon source. Unlike other pectinases of , which are polymorphic, no differences were observed between the PME profiles of 25 strains of different origins. Polyclonal antibodies were raised against purified PME from , and immunochemical comparisons with PMEs from and showed the presence of common epitopes between these different enzymes.

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1994-12-01
2021-10-21
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References

  1. Albani D., Altosaar I., Arnisson P.G., Fabijansky S.F. A gene showing sequence similarity to pectin esterase is specifically expressed in developing pollen of Brassica napus. Sequences in its 5' flanking region are conserved in other pollen-specific promoters. Plant Mol Biol 1991; 16:501–513
    [Google Scholar]
  2. Beaulieu C., Boccara M., Van Gijsegem F. Pathogenic behavior of pectinase-defective Erwinia chrysanthemi mutants on different plants. Mol Plant-Microbe Interact 1993; 6:197–202
    [Google Scholar]
  3. Bertheau Y., Madgidi-Hervan E., Kotoujansky A., Nguyen-The C., Andro T., Coleno A. Detection of depolymerase isoenzymes after electrophoresis or electrofocusing, or in titration curves. Anal Biochem 1984; 139:383–389
    [Google Scholar]
  4. Blake M.S., Johnston K.H., Russell-Jones G.J., Gotschiich E.C. A rapid, sensitive method for detection of alkaline-phosphatase-conjugated anti-antibody on Western blots. Anal Biochem 1984; 136:175–179
    [Google Scholar]
  5. Boccara M., Châtain V. Regulation and role in pathogenicity of Erwinia chrysanthemi 3937 pectinmethylesterase. J Bacteriol 1989; 171:4085–4087
    [Google Scholar]
  6. Boccara M., Diolez A., Rouve M., Kotoujansky A. The role of individual pectate lyases of Erwinia chrysanthemi 3937 in pathogenicity on saintpaulia plants. Physiol Mol Plant Pathol 1988; 33:95–104
    [Google Scholar]
  7. Bordenave M., Goldberg R. Purification and characterization of pectin methylesterases from Mung Bean hypocotyl cell walls. Phytochemistry 1993; 33:999–1003
    [Google Scholar]
  8. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 1976; 72:248–254
    [Google Scholar]
  9. Burnette W.N. ‘ Western blotting’: electrophoretic transfer of proteins from sodium-dodecyl-sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodonated protein A. Anal Biochem 1981; 112:195–203
    [Google Scholar]
  10. Collmer A., Keen N. The role of pectic enzymes in plant pathogenesis. Annu Rev Phytopathol 1986; 24:383–409
    [Google Scholar]
  11. Dow J.M., Milligan D.E., Jamieson L., Barber C.E., Daniels M.J. Molecular cloning of a polygalacturonate lyase gene from Xanthomonas pv. campestris and role of the gene product in pathogenicity. Physiol Mol Plant Pathol 1989; 35:113–120
    [Google Scholar]
  12. Drawert F., Krefft M. Charakterisierung extrazellularer Proteine und Enzyme aus Pectinkulturfiltraten von Botrytis cinerea. Phytochemistry 1978; 17:887–890
    [Google Scholar]
  13. Dubois M., Gilles K.A., Hamilton J.K., Rebers P.A., Smith F. Colorimetric method for determination of sugars and related substances. Anal Chem 1956; 28:350–356
    [Google Scholar]
  14. Fisher R.L., Bennett A.B. Role of cell wall hydrolases in fruit ripening. Annu Rev Plant Physiol Plant Mol Biol 1991; 42:675–703
    [Google Scholar]
  15. Goldberg R. Changes in the properties of cell wall pectin methyl esterase along the Vigna radiata hypocotyl. Physiol Plant 1984; 61:58–63
    [Google Scholar]
  16. Hagerman A.E., Austin P.J. Continuous spectro-photometric assay for plant pectin methyl esterase. J Agric Food Chem 1986; 34:440–144
    [Google Scholar]
  17. Hagerman A.E., Blau D.M., McClure A.L. Plate assay for determining the time of production of protease, cellulase and pectinases by germinating fungal spores. Anal Biochem 1986; 151:334–342
    [Google Scholar]
  18. Johnston D.J., Williamson B. Purification and characterisation of four polygalacturonases from Botrytis cinerea. Mycol Res 1992a; 96:343–349
    [Google Scholar]
  19. Johnston D.J., Williamson B. An immunological study of the induction of polygalacturonases in Botrytis cinerea. FEMS Microbiol Lett 1992b; 97:19–24
    [Google Scholar]
  20. Johnston D.J., Ramanathan V., Williamson B. A protein from immature raspberry fruit which inhibits endo-polygalacturonases from Botrytis cinerea and other microorganisms. J Exp Bot 1993; 44:971–976
    [Google Scholar]
  21. Khanh N.Q., Ruttkowski E., Leidinger K., Gottschalk M. Characterization and expression of a genomic pectin methyl esterase-encoding gene of Aspergillus niger. Gene 1992; 106:71–77
    [Google Scholar]
  22. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680–685
    [Google Scholar]
  23. Lin T.-P., Liu C.-C., Chen S.W., Wang W.-Y. Purification and characterization of pectinmethylesterase from Ficus awkeotsang makino achenes. Plant Physiol 1989; 91:1445–1453
    [Google Scholar]
  24. Magro P., Dilenne P., Marianno P., Pallavicini C. Variability of polygalacturonase and protein isoelectric focusing pattern in Botrytis cinerea isolates. J Gen Microbiol 1980; 120:105–109
    [Google Scholar]
  25. Marcus L., Schejter A. Single step chromatographic purification and characterization of the endopolygalacturonases and pectinesterases of the fungus Botrytis cinera. Physiol Plant Pathol 1983; 23:1–13
    [Google Scholar]
  26. Martinez M.J., Reyes F., Luhoz R. Cell wall plant polysaccharide-degrading enzymes in autolysis of Botrytis cinerea. Frans Br Mycol Soc 1982; 78:395–403
    [Google Scholar]
  27. Merril C.R., Goldman D., Sedman S.A., Ebert M.H. Ultrasensitive stain for proteins in polyacrylamide gels shows regional variations in cerebrospinal fluid proteins. Science 1981; 27:1437–1438
    [Google Scholar]
  28. Movahedi S., Heale J.B. The role of aspartic proteinase and endo-pectin lyase enzymes in the primary stages of infection and pathogenesis of various host tissues by different isolates of Botrytis cinerea Pers ex Pers. Physiol Mol Plant Pathol 1990; 36:303–324
    [Google Scholar]
  29. Pitkanen K., Heikinheimo R., Pakkanen R. Purification and characterization of Erwinia chrysanthemi B374 pectin methylesterase produced by Bacillus subtilis. Enzyme Microb Technol 1992; 14:832–836
    [Google Scholar]
  30. Ried J.L., Collmer A. Construction and characterization of an Erwinia chrysanthemi mutant with directed deletions in all the pectate lyase structural genes. Mol Plant-Microbe Interact 1988; 1:32–38
    [Google Scholar]
  31. Rombouts F.M., Wissenburg A.K., Pilnick W. Chromatographic separation of orange pectinesterase isozymes on pectates with different degrees of cross-linking. J Chromatogr 1979; 168:151–161
    [Google Scholar]
  32. Sajjaanantakul T., Pitifer L.A. Pectinesterase. In The Chemistry of Technology of Pectin 1991 New York: Academic Press; pp 135–164
    [Google Scholar]
  33. Schejter A., Marcus L. Isozymes of pectinesterase and polygalacturonase from Botrytis cinerea Pers. Methods Enzymol 1988; 161:366–373
    [Google Scholar]
  34. Scott-Craig J.S., Panaccione D.G., Cervone F., Walton J.D. Endopolygalacturonase is not required for pathogenicity of Cochliobolus carbonum on maize. Plant Cell 1990; 2:1191–1200
    [Google Scholar]
  35. Tieman D.M., Harriman R.W., Ramamohan G., Handa A.K. An antisense pectin methylesterase gene alters pectin chemistry and soluble solids in tomato fruits. Plant Cell 1992; 4:667–679
    [Google Scholar]
  36. Wasfy E.H., Fargas S.A., Tarabieh M.A., Abd-Elmoiety S.H. Studies on enzymes of different strains of Botrytis cinerea. Phytopathol 1978; Z92:168–179
    [Google Scholar]
  37. Zalewska-Sobczak J., Urbaneck H. Purification of polygalacturonases produced by Botrytis cinerea E-200. Bull Acad Pol Sci 1975; 23:663–668
    [Google Scholar]
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