Abstract
A distinctive feature of Pseudomonas syringae pv. syringae is the production of two lipopcptide toxins, syringomycin and syringopeptin, which form pores in plasma membranes and cause passive transmembrane ion fluxes. Syringomycin and syringopeptin are the major virulence determinants of P. s. pv. syringae based on pathogenicity tests of syr and syp biosynthesis mutants. The biosynthesis of both phytotoxins is predicted to occur on multifunctional enzyme complexes by the thiotemplate mechanism. The syringomycin (syr) gene cluster lies adjacent to the syringopeptin (syp) gene cluster on the P. s. pv. syringae chromosome, and together they compose over 1% of the genome. A model for syringomycin biosynthesis and its underlying genetic organization is presented. Most of the ~35 kb syr gene cluster encodes Syr synthetases composed of amino acid-activating domains that catalyze the adenylation of the constituent amino acids and thioester formation. The role of phenolic plant signal molecules in the activation of syrB gene expression and syringomycin production is summarized. This represents the first example of a nonribosomal peptide synthetase gene being activated by specific plant-derived signal molecules.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Ankenbauer, R. G., and Nester, E. W. (1990) ‘Sugar-mediated induction of Agrobacterium tumefaciens virulence genes: Structural specificity and activities of monosaccharides’, J. Bacteriol. 172, 6442–6446.
Ballio, A., Barra, D., Bossa, F., Collina, A., Grgurina, I., Marino, G., Moneti, G., Paci, M., Pucci, P., Segre, A., and Simmaco, M. (1991) ‘Syringopeptins, new phytotoxic lipodepsipeptides of Pseudomonas syringae pv. syringae’, FEBS Lett. 291, 109–112.
De Crécy-Lagard, V., Marlière, P., and Saurin, W. (1995) ‘Multienzymatic non ribosomal peptide biosynthesis: Identification of the functional domains catalysing peptide elongation and epimerisation’, C. R. Acad. Sci. Paris 318, 927–936.
Grgurina, I., Gross, D. C., Deligiovas, I., and Zhang, J.-H. (1997) ‘SyrC, an enzyme involved in syringomycin biosynthesis, shows thioesterasic activity’, in K. Rudolph, T. J. Burr, J. W. Mansfield, D. Stead, A. Vivian, and J. von Kietzell (eds.), Pseudomonas syringae Pathovars and Related Pathogens, Kluwer Academic Publishers, Dordrecht, pp. 192–197.
Grgurina, I., Gross, D. C., Iacobellis, N S., Lavermicocca, P., Takemoto, J. Y., and Benincasa, M. (1996) ‘Phytotoxin production by Pseudomonas syringae pv. syringae: Syringopeptin production by syr mutants defective in biosynthesis or secretion of syringomycin’, FEMS Microbiol. Lett. 138, 35–39.
Grgurina, I., and Mariotti, F. (1997) ‘Biosynthesis of bioactive lipodepsipeptides by Pseudomonas syringae pv. syringae’, in K. Rudolph, T. J. Burr, J. W. Mansfield, D. Stead, A. Vivian, and J. von Kietzell (eds.), Pseudomonas syringae Pathovars and Related Pathogens, Kluwer Academic Publishers, Dordrecht, pp. 182–191.
Hutchison, M. L., and Gross, D. C. (1997) ‘Lipopeptide phytotoxins produced by Pseudomonas syringae pv. syringae: Comparison of the biosurfactant and ion channel-forming activities of syringopeptin and syringomycin’, Mol. Plant-Microbe Interact. 10, 347–354.
Hutchison, M. L., Tester, M. A., and Gross, D. C. (1995) ‘Role of biosurfactant and ion channel-forming activities of syringomycin in transmembrane ion flux: A model for the mechanism of action in the plant-pathogen interaction’, Mol. Plant-Microbe Interact. 8, 610–620.
Iacobellis, N. S., Lavermicocca, P., Grgurina, I., Simmaco, M., and Ballio, A. (1992) ‘Phytotoxic properties of Pseudomonas syringae pv. syringae toxins’, Physiol. Mol. Plant Pathol. 40, 107–116.
Kleinkauf, H. and von Döhren, H. (1996) ‘A nonribosomal system of peptide synthesis’, Eur. J. Biochem. 236, 335–351.
Krätzchmar, J., Krause, M., and Marahiel, M. A. (1989) ‘Gramicidin S biosynthesis operon containing the structural genes grsA and grsB has an open reading frame encoding a protein homologous to fatty acid thioesterases’, J. Bacteriol. 171, 5422–5429.
Lavermicocca, P., Iacobellis, N. S., Simmaco, M., and Graniti, A. (1997) ‘Biological properties and spectrum of activity of Pseudomonas syringae pv. syringae toxins’, Physiol. Mol. Plant Pathol. 50, 129–140.
Mo, Y.-Y., and Gross, D. C. (1991) ‘Plant signal molecules activate the syrB gene, which is required for syringomycin production by Pseudomonas syringae pv. syringae’, J. Bacteriol. 173, 5784–5792.
Mo, Y.-Y., Geibel, M., Bonsall, R. F., and Gross, D. C. (1995) ‘Analysis of sweet cherry (Prunus avium L.) leaves for plant signal molecules that activate the syrB gene required for synthesis of the phytotoxin, syringomycin, by Pseudomonas syringae pv. syringae’, Plant Physiol. 107, 603–612.
Quigley, N. B., and Gross, D. C. (1994) ‘Syringomycin production among strains of Pseudomonas syringae pv. syringae: Conservation of the syrB and syrD genes and activation of phytotoxin production by plant signal molecules’, Mol. Plant-Microbe Interact. 7, 78–90.
Quigley, N. B., Mo, Y.-Y., and Gross, D. C. (1993) ‘SyrD is required for syringomycin production by Pseudomonas syringae pathovar syringae and is related to a family of ATP-binding secretion proteins’, Mol. Microbiol. 9, 787–801.
Rusnak, F., Sakaitani, M., Drueckhammer, D., Reichert, J., and Walsh, C. T. (1991) ‘Biosynthesis of the Escherichia coli siderophore enterobactin: Sequence of the entF gene, expression and purification of EntF, and analysis of covalent phosphopantetheine’, Biochemistry 30, 2916–2927.
Segre, A., Bachmann, R. C., Ballio, A., Bossa, F., Grgurina, I., Iacobellis, N. S., Marino, G., Pucci, P., Simmaco, M., and Takemoto, J. Y. (1989) ‘The structure of syringomycins A1, E and G’, FEBS Lett. 255, 27–31.
Stachelhaus, T., and Marahiel, M. A. (1995) ‘Modular structure of genes encoding multifunctional peptide synthetases required for non-ribosomal peptide synthesis’, FEMS Microbiol. Lett. 125, 3–14.
Stachelhaus, T., and Marahiel, M. A. (1995) ‘Modular structure of peptide synthetases revealed by dissection of the multifunctional enzyme GrsA’, J. Biol. Chem. 270, 6163–6169.
Stein, T., and Vater, J. (1996) ‘Amino acid activation and polymerization at modular multienzymes in nonribosomal peptide biosynthesis’, Amino Acids 10, 201–227.
Zhang, J.-H., Quigley, N. B., and Gross, D. C. (1995) ‘Analysis of the syrB and syrC genes of Pseudomonas syringae pv. syringae indicates that syringomycin is synthesized by a thiotemplate mechanism’, J. Bacteriol. 177, 4009–4020.
Zhang, J.-H., Quigley, N. B., and Gross, D. C. (1997) ‘Analysis of the syrP gene, which regulates syringomycin synthesis by Pseudomonas syringae pv. syringae’, Appl. Environ. Microbiol. 63, 2771–2778.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1998 Springer Science+Business Media Dordrecht
About this chapter
Cite this chapter
Gross, D.C. et al. (1998). Characterization of the Thiotemplate Mechanisms of Syringomycin and Syringopeptin Synthesis by Pseudomonas Syringae pv. syringae . In: Kohmoto, K., Yoder, O.C. (eds) Molecular Genetics of Host-Specific Toxins in Plant Disease. Developments in Plant Pathology, vol 13. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5218-1_10
Download citation
DOI: https://doi.org/10.1007/978-94-011-5218-1_10
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-6197-1
Online ISBN: 978-94-011-5218-1
eBook Packages: Springer Book Archive