Tomatinase from Fusarium oxysporum f. sp. lycopersici Defines a New Class of Saponinases
Plants produce a variety of secondary metabolites, many of which have antifungal activity. Saponins are plant glycosides that may provide a preformed chemical barrier against phytopathogenic fungi. Fusarium oxysporum f. sp. lycopersici and other tomato pathogens produce extracellular enzymes known a...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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The American Phytopathological Society
1999-10-01
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| Series: | Molecular Plant-Microbe Interactions |
| Online Access: | https://apsjournals.apsnet.org/doi/10.1094/MPMI.1999.12.10.852 |
| _version_ | 1811278038208348160 |
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| author | Teresa Roldán-Arjona Alonso Pérez-Espinosa Manuel Ruiz-Rubio |
| author_facet | Teresa Roldán-Arjona Alonso Pérez-Espinosa Manuel Ruiz-Rubio |
| author_sort | Teresa Roldán-Arjona |
| collection | DOAJ |
| description | Plants produce a variety of secondary metabolites, many of which have antifungal activity. Saponins are plant glycosides that may provide a preformed chemical barrier against phytopathogenic fungi. Fusarium oxysporum f. sp. lycopersici and other tomato pathogens produce extracellular enzymes known as tomatinases, which deglycosylate α-tomatine to yield less toxic derivatives. We have cloned and characterized the cDNA and genomic DNA encoding tomatinase from the vascular pathogen of tomato F. oxysporum f. sp. lycopersici. This gene encodes a protein (FoTom1) with no amino acid sequence homology to any previously described saponinase, including tomatinase from Septoria lycopersici. Although FoTom1 is related to family 10 glycosyl hydrolases, which include mainly xylanases, it has no detectable xylanase activity. We have over-expressed and purified the protein with a bacterial heterologous system. The purified enzyme is active and cleaves α-tomatine into the less toxic compounds tomatidine and lycotetraose. Tomatinase from F. oxysporum f. sp. lycopersici is encoded by a single gene whose expression is induced by α-tomatine. This expression is fully repressed in the presence of glucose, which is consistent with the presence of two putative CREA binding sites in the promoter region of the tomatinase gene. The tomatinase gene is expressed in planta in both roots and stems throughout the entire disease cycle of F. oxysporum f. sp. lycopersici. |
| first_indexed | 2024-04-13T00:27:32Z |
| format | Article |
| id | doaj.art-21dc40df1d014fcfa4b6233e783c924b |
| institution | Directory Open Access Journal |
| issn | 0894-0282 1943-7706 |
| language | English |
| last_indexed | 2024-04-13T00:27:32Z |
| publishDate | 1999-10-01 |
| publisher | The American Phytopathological Society |
| record_format | Article |
| series | Molecular Plant-Microbe Interactions |
| spelling | doaj.art-21dc40df1d014fcfa4b6233e783c924b2022-12-22T03:10:33ZengThe American Phytopathological SocietyMolecular Plant-Microbe Interactions0894-02821943-77061999-10-01121085286110.1094/MPMI.1999.12.10.852Tomatinase from Fusarium oxysporum f. sp. lycopersici Defines a New Class of SaponinasesTeresa Roldán-ArjonaAlonso Pérez-EspinosaManuel Ruiz-RubioPlants produce a variety of secondary metabolites, many of which have antifungal activity. Saponins are plant glycosides that may provide a preformed chemical barrier against phytopathogenic fungi. Fusarium oxysporum f. sp. lycopersici and other tomato pathogens produce extracellular enzymes known as tomatinases, which deglycosylate α-tomatine to yield less toxic derivatives. We have cloned and characterized the cDNA and genomic DNA encoding tomatinase from the vascular pathogen of tomato F. oxysporum f. sp. lycopersici. This gene encodes a protein (FoTom1) with no amino acid sequence homology to any previously described saponinase, including tomatinase from Septoria lycopersici. Although FoTom1 is related to family 10 glycosyl hydrolases, which include mainly xylanases, it has no detectable xylanase activity. We have over-expressed and purified the protein with a bacterial heterologous system. The purified enzyme is active and cleaves α-tomatine into the less toxic compounds tomatidine and lycotetraose. Tomatinase from F. oxysporum f. sp. lycopersici is encoded by a single gene whose expression is induced by α-tomatine. This expression is fully repressed in the presence of glucose, which is consistent with the presence of two putative CREA binding sites in the promoter region of the tomatinase gene. The tomatinase gene is expressed in planta in both roots and stems throughout the entire disease cycle of F. oxysporum f. sp. lycopersici.https://apsjournals.apsnet.org/doi/10.1094/MPMI.1999.12.10.852 |
| spellingShingle | Teresa Roldán-Arjona Alonso Pérez-Espinosa Manuel Ruiz-Rubio Tomatinase from Fusarium oxysporum f. sp. lycopersici Defines a New Class of Saponinases Molecular Plant-Microbe Interactions |
| title | Tomatinase from Fusarium oxysporum f. sp. lycopersici Defines a New Class of Saponinases |
| title_full | Tomatinase from Fusarium oxysporum f. sp. lycopersici Defines a New Class of Saponinases |
| title_fullStr | Tomatinase from Fusarium oxysporum f. sp. lycopersici Defines a New Class of Saponinases |
| title_full_unstemmed | Tomatinase from Fusarium oxysporum f. sp. lycopersici Defines a New Class of Saponinases |
| title_short | Tomatinase from Fusarium oxysporum f. sp. lycopersici Defines a New Class of Saponinases |
| title_sort | tomatinase from fusarium oxysporum f sp lycopersici defines a new class of saponinases |
| url | https://apsjournals.apsnet.org/doi/10.1094/MPMI.1999.12.10.852 |
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