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The Extracellular Proteases of the Phytopathogenic Bacterium Xanthomonas campestris

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Abstract

The culture liquids of three Xanthomonas campestris pv. campestris strains were found to possess proteolytic activity. The culture liquid of strain B611 with the highest proteolytic activity was fractionated by salting-out with ammonium sulfate, gel filtration, and ion-exchange chromatography. The electrophoretic analysis of active fractions showed the presence of two proteases in the culture liquid of strain B611, the major of which was serine protease. The treatment of cabbage seedlings with the proteases augmented the activity of peroxidase in the cabbage roots by 28%.

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REFERENCES

  1. Williams, P.H., Black Rot: A Continuing Threat to World Crucifer, Plant Diseases, 1980, vol. 64, pp. 736-742.

    Google Scholar 

  2. Daniels, M.J., Barber, C.E., Turner, P.C., Sawczyc, M.K., Byrde, R.J.W., and Fielding, A.H., Cloning of Genes Involved in Pathogenicity of Xanthomonas campestris pv. campestris Using the Broad-Host-Range Cosmid pLAFR1, EMBO J., 1984, vol. 3, pp. 3323-3328.

    Google Scholar 

  3. Dow, J.M., Clarke, B.R., Milligan, D.E., Tang, J.-L., and Daniels, M.J., Extracellular Proteases from Xanthomonas campestris pv. campestris, the Black Rot Pathogen, Appl. Environ. Microbiol., 1990, vol. 56,no. 10, pp. 2994-2998.

    Google Scholar 

  4. Dow, J.M., Fan, M.-J., Newman, M.-A., and Daniels, M.J., Differential Expression of Conserved Protease Genes in Crucifer-Attacking Pathovars of Xanthomonas campestris, Appl. Environ. Microbiol., 1993, vol. 59,no. 12, pp. 3996-4003.

    Google Scholar 

  5. Manual of Methods for General Bacteriology, Gerhardt, P. et al., Eds., Washington: Am. Soc. Microbiol., 1981. Translated under the title Metody obshchei bakteriologii, Moscow: Mir, 1983, vol. 1.

    Google Scholar 

  6. Shchegolev, S.Yu. and Khlebtsov, N.G., Primenenie mikro-i mini-EVM pri opredelenii parametrov dispersionnykh sistem spektroturbidimetricheskim metodom (The Application of Micro-and Minicomputers to Determine the Parameters of Dispersed Systems by the Spectroturbidimetric Method), Saratov: Sarat. Gos. Univ., 1984.

    Google Scholar 

  7. Barbieri, P., Zanelli, T., Galli, E., and Zanetti, G., Wheat Inoculation with Azospirillum brasilense Sp6 and Some Mutants Altered in Nitrogen Fixation and Indole-3-Acetic Acid Production, FEMS Microbiol. Lett., 1986, vol. 36, pp. 87-90.

    Google Scholar 

  8. Stadnik, G.I., Kalashnikova, E.E., Konnova, S.A., and Ignatov, V.V., Role of the Surface and Extracellular Substances of the Phytopathogenic Bacterium Xanthomonas campestris in Its Interactions with Cabbage Plants, Mikrobiologiya, 2001, vol. 70,no. 2, pp. 270-274.

    Google Scholar 

  9. Kelleher, P.I. and Juliano, R.L., Proteolytic Enzymes: A Practical Approach, Anal. Biochem., 1984, vol. 136, p. 470.

    Google Scholar 

  10. Laemmli, U.K., Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4, Nature (London), 1970, vol. 227, pp. 680-685.

    Google Scholar 

  11. 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, vol. 72,no. 1, pp. 248-254.

    Google Scholar 

  12. Rumshinskii, L.Z., Matematicheskaya obrabotka rezul'tatov eksperimenta (Mathematical Processing of Experimental Results), Moscow: Nauka, 1971, p. 15.

    Google Scholar 

  13. Andreeva, V.A., Ferment peroksidaza: uchastie v zashchitnom mekhanizme rastenii (Peroxidase: Involvement in the Plant Defense Mechanism), Moscow: Nauka, 1988.

    Google Scholar 

  14. Ball, A.M., Ashby, A.M., Daniels, M.J., Ingram, D.S., and Johnstone, K., Evidence for the Requirement of Extracellular Protease in the Pathogenic Interaction of Pirenopeziza brassicae with Oilseed Rape, Physiol. Mol. Plant Pathol., 1991, vol. 38, pp. 147-161.

    Google Scholar 

  15. Heilbronn, J., Johnstone, D.J., Dunbar, B., and Lyon, G.D., Purification of a Metalloprotease Produced by Erwinia carotovora subsp. carotovora and the Degradation of Potato Lectin In Vitro, Physiol. Mol. Plant Pathol., 1995, vol. 47, pp. 285-292.

    Google Scholar 

  16. Dow, J.M., Davies, H.A., and Daniels, M.J., A Metalloprotease from Xanthomonas campestris That Specifically Degrades Proline-and Hydroxyproline-Rich Glycoproteins of the Plant Extracellular Matrix, Mol. Plant-Microbe Interact., 1998, vol. 11,no. 11, pp. 1085-1093.

    Google Scholar 

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Authors and Affiliations

  1. Institute of Biochemistry and Physiology of Plants and Microorganisms, Russian Academy of Sciences, pr. Entuziastov 13, Saratov, 410015, Russia

    E. E. Kalashnikova, M. P. Chernyshova & V. V. Ignatov

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  1. E. E. Kalashnikova
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  2. M. P. Chernyshova
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  3. V. V. Ignatov
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Kalashnikova, E.E., Chernyshova, M.P. & Ignatov, V.V. The Extracellular Proteases of the Phytopathogenic Bacterium Xanthomonas campestris . Microbiology 72, 443–447 (2003). https://doi.org/10.1023/A:1025044706964

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