Secretion of Proteolytic Enzymes by Three Phytopathogenic Microorganisms
| Autor: | Valueva Tatyana A, E. L. Gvozdeva, A. V. Sofyin, T. A. Revina, Natalia N. Kudryavtseva, Ievleva Ev |
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| Rok vydání: | 2013 |
| Předmět: |
chemistry.chemical_classification
Oomycete biology Phytophthora infestans Microorganism fungi Proteolytic enzymes food and beverages General Medicine biology.organism_classification Trypsin Rhizoctonia Microbiology Fungal Proteins Rhizoctonia solani Enzyme Fusarium chemistry Fusarium culmorum medicine Peptide Hydrolases Plant Diseases medicine.drug |
| Zdroj: | Прикладная биохимия и микробиология. 49:513-521 |
| ISSN: | 0555-1099 |
| Popis: | Serine proteinases from three phytopathogenic microorganisms that belong to different fungal families and cause diseases in potatoes were studied and characterized. The oomycete Phytophthora infestans (Mont.) de Bary and the fungi Rhizoctonia solani and Fusarium culmorum were shown to secrete serine proteinases. An analysis of the substrate specificity of these enzymes and their sensitivity to synthetic and protein inhibitors allowed us to refer them to trypsin- and subtilisin-like proteinases. The correlation between the trypsin- and subtilisin-like proteinases depended on the composition of the culture medium, particularly on the form of the nitrogen source. A phylogenetic analysis was carried out. In contrast to basidiomycetes R. solani, ascomycetes F. culmorum and oomycetes P. infestans produced a similar set of exoproteinases, although they had more distant phylogenetic positions. This indicated that the secretion of serine proteinases by various phytopathogenic microorganisms also depended on their phylogenetic position. These results allowed us to suggest that exoproteinases from phytopathogenic fungi play a different role in pathogenesis. They may promote the adaptation of fungi if the range of hosts is enlarged. On the other hand, they may play an important role in the survival of microorganisms in hostile environements outside their hosts. |
| Databáze: | OpenAIRE |
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