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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Bibliographic Details
Published in:Applied and environmental microbiology 1998-05, Vol.64 (5)
Main Authors: 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
Format: Article
Language:English
Subjects:
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
CUCUMIS MELO
ENZYMIC ACTIVITY
FLETRISSEMENT
FUSARIUM OXYSPORUM
LOCI
LOCUS
MARCHITEZ
PCR
POLIGALACTURONASA
POLYGALACTURONASE
POLYMERASE CHAIN REACTION
WILTS
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Summary: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
ISSN:0099-2240
1098-5336