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Endopolygalaturonase PG1 in different formae speciales of Fusarium oxysporum
PGI, the major endopolygalacturonase of the vascular wilt pathogen Fusarium oxysporum, was secreted during growth on pectin by 10 of 12 isolates belonging to seven formae speciales, as determined with isoelectric focusing zymograms and sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels....
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Published in: | Applied and environmental microbiology 1998-05, Vol.64 (5) |
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creator | Di Pietro, A. (Universidad de Cardoba, Cordoba, Spain.) Garcia-Maceira, F.I Huertas-Gonzalez, M.D Ruiz-Roldan, M.C Caracuel, Z Barbieri, A.S Roncero, M.I.G |
description | PGI, the major endopolygalacturonase of the vascular wilt pathogen Fusarium oxysporum, was secreted during growth on pectin by 10 of 12 isolates belonging to seven formae speciales, as determined with isoelectric focusing zymograms and sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels. A Southern analysis of genomic DNA and PCR performed with gene-specific primers revealed that the pg1 locus was highly conserved structurally in most isolates. Two PG1-deficient isolates were identified; one lacked the encoding gene, and the other carried a pg1 allele disrupted by a 3.2-kb insertion with sequence homology to hAT transposases. The virulence for muskmelon of different F. oxysporum f. sp. melonis isolates was not correlated with PG1 production in vitro. We concluded that PG1 is widely distributed in F. oxysporum and that it is not essential for pathogenicity |
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(Universidad de Cardoba, Cordoba, Spain.) ; Garcia-Maceira, F.I ; Huertas-Gonzalez, M.D ; Ruiz-Roldan, M.C ; Caracuel, Z ; Barbieri, A.S ; Roncero, M.I.G</creator><creatorcontrib>Di Pietro, A. (Universidad de Cardoba, Cordoba, Spain.) ; Garcia-Maceira, F.I ; Huertas-Gonzalez, M.D ; Ruiz-Roldan, M.C ; Caracuel, Z ; Barbieri, A.S ; Roncero, M.I.G</creatorcontrib><description>PGI, the major endopolygalacturonase of the vascular wilt pathogen Fusarium oxysporum, was secreted during growth on pectin by 10 of 12 isolates belonging to seven formae speciales, as determined with isoelectric focusing zymograms and sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels. A Southern analysis of genomic DNA and PCR performed with gene-specific primers revealed that the pg1 locus was highly conserved structurally in most isolates. Two PG1-deficient isolates were identified; one lacked the encoding gene, and the other carried a pg1 allele disrupted by a 3.2-kb insertion with sequence homology to hAT transposases. The virulence for muskmelon of different F. oxysporum f. sp. melonis isolates was not correlated with PG1 production in vitro. 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Two PG1-deficient isolates were identified; one lacked the encoding gene, and the other carried a pg1 allele disrupted by a 3.2-kb insertion with sequence homology to hAT transposases. The virulence for muskmelon of different F. oxysporum f. sp. melonis isolates was not correlated with PG1 production in vitro. 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A Southern analysis of genomic DNA and PCR performed with gene-specific primers revealed that the pg1 locus was highly conserved structurally in most isolates. Two PG1-deficient isolates were identified; one lacked the encoding gene, and the other carried a pg1 allele disrupted by a 3.2-kb insertion with sequence homology to hAT transposases. The virulence for muskmelon of different F. oxysporum f. sp. melonis isolates was not correlated with PG1 production in vitro. We concluded that PG1 is widely distributed in F. oxysporum and that it is not essential for pathogenicity</abstract></addata></record> |
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source | American Society for Microbiology Journals; PubMed Central |
subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE CUCUMIS MELO ENZYMIC ACTIVITY FLETRISSEMENT FUSARIUM OXYSPORUM LOCI LOCUS MARCHITEZ PCR POLIGALACTURONASA POLYGALACTURONASE POLYMERASE CHAIN REACTION WILTS |
title | Endopolygalaturonase PG1 in different formae speciales of Fusarium oxysporum |
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