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A major stress-inducible Mr-42000 wall glycoprotein of French bean (Phaseolus vulgaris L.)

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Abstract

A major wall protein of suspension-cultured cells of French bean has been isolated and characterised. It can be prepared from walls or the culture filtrate and in composition it is particularly rich in proline, valine and glutamic acid/glutamine and contains appreciable amounts of hydroxyproline. The N-terminus shows some glycosylation, while following chemical deglycosylation the first 38 residues were found to be identical to those of proline-rich proteins from soybean. However, the composition of the highly purified Mr-42000 bean protein differs considerably from the soybean proteins and must contain its own specific domains. An antibody was raised and used to demonstrate the inducibility of the Mr-42000 bean protein in response to elicitor action. The protein was found to be mainly localised in the intercellular spaces of the cortical cells of bean hypocotyls and at the wall-plasmalemma interface of xylem vessels, another potentially accessible compartment for pathogens. Following wounding, the protein was found to be generally distributed in the wall of epidermal and cortical cells of the hypocotyls. The Mr-42000 protein is cross reactive with antibodies raised to glycoproteins of the Rhizobium infection thread and the chitin-binding hydroxyproline-rich glycoprotein, potato lectin. These common epitopes together with the previously demonstrated chitin-binding properties of the bean protein indicate a role in host-microbial interactions. Furthermore, the Mr-42000 protein itself bound to the growing hyphal tips of the bean pathogen, Colletotrichum lindemuthianum.

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Abbreviations

FITC:

fluorescein isothiocyanate

IgG:

immunoglobulin G

PAL:

phenylalanine ammonia-lyase

References

  • Ashford, D., Allen, A.K., Neuberger, A. (1982) The production and properties of an antiserum to potato (Solanum tuberosum) lectin. Biochem. J. 201, 641–645

    Google Scholar 

  • Beerhues, L., Robnenek, H., Wiermann, R. (1988) Chalcone synthases from spinach (Spinacia oleracea L.). II Immunofluorescence and immunogold localization. Planta 173, 544–553

    Google Scholar 

  • Bolwell, G.P. (1986) Microsomal arabinosylation of polysaccharide and elicitor-induced carbohydrate-binding glycoprotein in French bean. Phytochemistry 25, 1807–1813

    Google Scholar 

  • Bolwell, G.P. (1987) Elicitor induction of the synthesis of a novel lectin-like arabinosylated hydroxyproline-rich glycoprotein in suspension cultures of Phaseolus vulgaris L. Planta 172, 184–191

    Google Scholar 

  • Bolwell, G.P. (1988) Synthesis of cell wall components: aspects of control. Phytochemistry 27, 1235–1253

    Google Scholar 

  • Bolwell, G.P., Dixon, R.A. (1986) Membrane-bound hydroxylases in elicitor-treated bean cells. Eur. J. Biochem. 159, 163–169

    Google Scholar 

  • Bolwell, G.P., Bell, J.N., Cramer, C.L., Schuch, W., Lamb, C.J., Dixon, R.A. (1985a) l-phenylalanine ammonia-lyase from Phaseolus vulgaris.Characterisation and differential induction of multiple forms from elicitor-treated cell suspension cultures. Eur. J. Biochem. 149, 411–419

    Google Scholar 

  • Bolwell, G.P., Robbins, M.P., Dixon, R.A. (1985b) Metabolic changes in elicitor-treated bean cells. Eur. J. Biochem. 148, 571–578

    Google Scholar 

  • Bolwell, G.P., Sap, J., Cramer, C.L., Lamb, C.J., Schuch, W., Dixon, R.A. (1986) l-Phenylalanine ammonia-lyase from Phaseolus vulgaris: Partial degradation of enzyme subunits in vitro and in vivo. Biochim. Biophys. Acta 881, 210–221

    Google Scholar 

  • Brambi, R., Gade, W. (1985) Plant seed lectins disrupt growth of germinating fungal spores. Physiol. Plant. 63, 402–408

    Google Scholar 

  • Chambers, R.E., Clamp, J.R. (1971) An assessment of methanolysis and other factors used in the analysis of carbohydrate-containing materials. Biochem. J. 125, 1009–1018

    Google Scholar 

  • Corbin, D., Sauer, N., Lamb, CJ. (1987) Differential expression of a hydroxyproline-rich glycoprotein gene family in wounded and infected plants. Mol. Cell Biol. 7, 4337–4344

    Google Scholar 

  • Cuypers, B., Schmelzer, E., Hahlbrock, K. (1988) In situ localization of rapidly accumulated phenylalanine ammonia-lyase mRNA around penetration sites of Phytophthora infestans in potato leaves. Mol. Plant-Microbe Interact. 1, 157–160

    Google Scholar 

  • Datta, K., Schmidt, A., Marcus, A. (1989) Characterisation of two repetitive proline-rich proteins and a cognate cDNA from germinated axes. Plant Cell 1, 945–952

    Google Scholar 

  • Dixon, R.A., Lamb, CJ. (1979) 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

    Google Scholar 

  • Edge, A.S.B., Faltynek, C.R., Hof, L., Reichert, L.E., Jr., Weber, P. (1981) Deglycosylation of glycoprotein by trifluoromethane sulphonic acid. Anal. Biochem. 118, 131–137

    Google Scholar 

  • Hames, B.D. (1982) An introduction to polacrylamide gel electrophoresis. In: Gel electrophoresis of proteins; a practical approach, pp. 1–86, Hames, B.D., Rickwood, D., eds. IRL Press, Oxford Washington

    Google Scholar 

  • Hong, J.C., Nagao, R.T., Key, J.L. (1989) Developmentally regulated expression of soybean proline-rich cell wall protein genes. Plant Cell 1, 937–943

    Google Scholar 

  • Jeffree, C.E., Dale, J.E., Fry, S.C. (1986) The genesis of intercellular spaces in developing leaves of Phaseolus vulgaris L. Protoplasma 132, 90–98

    Google Scholar 

  • Keller, B., Templeton, M.D., Lamb, CJ. (1989a) Specific localization of a plant cell wall glycine-rich protein in protoxylem cells of the vascular system. Proc. Natl. Acad. Sci. USA 86, 1529–1533

    Google Scholar 

  • Keller, B., Schmid, J., Lamb, CJ. (1989b) Vascular expression of a bean cell wall glycine-rich protein-B-glucuronidase gene fusion in transgenic tobacco. EMBO J. 8, 1309–1314

    Google Scholar 

  • Kolloffel, C., Linssen, P.W.T. (1984) The formation of intercellular spaces in the cotyledons of developing and germinating pea seeds. Protoplasma 120, 12–19

    Google Scholar 

  • Lamb, C.J., Lawton, M.A., Dron, M., Dixon, R.A. (1989) Signals and transduction mechanisms for activation of plant defences against microbial attack. Cell 56, 215–24

    Google Scholar 

  • Li, X., Kieliszewski, M., Lamport, D.T.A. (1990) A chenopod extensin lacks repetitive tetrahydroxyproline blocks. Plant Physiol. 92, 327–333

    Google Scholar 

  • Marcus, A., Greenberg, J., Averyhart-Fullard, V. (1991) Repetitive proline-rich proteins in the extracellular matrix of the plant cell. Physiol. Plant 81, 273–279

    Google Scholar 

  • Mauch, F., Staehelin, L.A. (1989) Functional implications of the subcellular localisation of ethylene-induced chitinase and β-1–3-glucanase in bean leaves. Plant Cell 1, 447–457

    Article  CAS  PubMed  Google Scholar 

  • O'Connell R., Bailey, J.A. (1986) Cellular interactions between Phaseolus vulgaris and the hemibiotrophic fungus Colletotrichum lindemuthianum. In: Biology and molecular biology of plant pathogen interactions, pp. 40–48, J.A. Bailey, ed. Springer-Verlag, Berlin Heidelberg

    Google Scholar 

  • O'Connell, R., Ride, J.D. (1990) Chemical detection and ultrastructural localization of chitin in cell walls of Colletotrichum lindemuthianum. Physiol. Mol. Plant Pathol. 37, 39–53

    Google Scholar 

  • Pennell, R., Roberts K. (1990) Sexual development in the pea is presaged by altered expression of arabinogalactan protein. Nature 344, 547–549

    Google Scholar 

  • Roberts, K. (1989) The plant extracellular matrix. Curr. Op. Cell Biol. 1, 1020–1027

    Google Scholar 

  • Roland, J.C. (1978) Cell wall differentiation and stages involved with intercellular gas space opening. J. Cell Sci. 32, 325–336

    Google Scholar 

  • Showalter, A.M., Varner, J.E. (1989) The biology and molecular biology of plant hydroxyproline-rich glycoproteins. In: The biochemistry of plants: A comprehensive treatise, vol. 15, pp. 485–520, Marcus, A., ed. Academic Press New York

    Google Scholar 

  • Slabas, A.R., Smith, C.G. (1988) Immunogold localization of acyl carrier protein in plants and Esherichia coli: evidence for membrane association in plants. Planta 175, 145–152

    Google Scholar 

  • Stafstrom, J.P., Staehelin, L.A. (1988) Antibody localisation of extensin in cell walls of carrot storage roots. Planta 174, 321–332

    Google Scholar 

  • Van den Bosch, K.A., Bradley, D.J., Knox, J.P., Perotto, S., Butcher, G.W., Brewin, N.J. (1989) Common components of the infection thread matrix and the intercellular space identified by immunocytochemical analysis of pea nodules and infected roots. EMBO J. 8, 335–342

    Google Scholar 

  • Varner, J.E., Lin, L-S (1989) Plant cell wall architecture. Cell 56, 231–239

    Google Scholar 

  • Wessels, J.G.H. (1986) Cell wall synthesis in apical hyphal growth. Int. Rev. Cytol. 104, 37–79

    Google Scholar 

  • Ye, Z-H., Varner, J.E. (1991) Tissue-specific expression of cell wall proteins in developing soybean tissues. Plant Cell 3, 23–37

    Google Scholar 

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We thank Dr Nick Brewin for advice on interpretation of immunolocalisations and for the gift of MCA 265. We thank Dudley Fernandino for carrying out the confocal microscopy. GPB thanks the Science and Engineering Research Council for funding.

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Millar, D.J., Slabas, A.R., Sidebottom, C. et al. A major stress-inducible Mr-42000 wall glycoprotein of French bean (Phaseolus vulgaris L.). Planta 187, 176–184 (1992). https://doi.org/10.1007/BF00201935

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