Catalase A from Botrytis cinerea is not expressed during infection on tomato leaves

Author： van der Vlugt-Bergmans C.J.B. Wagemakers C.A.M. dees D.C.T. van Kan J.A.L.

ISSN： 0885-5765

Source： Physiological and Molecular Plant Pathology, Vol.50, Iss.1, 1997-01, pp. : 1-15

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Abstract

Catalase mediates the enzymatic breakdown of hydrogen peroxide to water and molecular oxygen. During the infection of broad bean ( Vicia faba ) by Botrytis cinerea the release of hydrogen peroxide by fungal oxidase activity was proposed to facilitate penetration by the pathogen. Catalase activity might play a role in protecting the fungus against the damaging effects of hydrogen peroxide.A cDNA clone encoding catalase was isolated from a library of Botrytis cinerea . Southern blot analysis of genomic DNA indicated the presence of a single copy gene, denoted as catA . The cDNA clone encoded a protein, CAT-A, of 480 amino acids showing 56-65% similarity to fungal catalases. Detailed analysis of sequence homologies between other fungal catalases enabled grouping of catalases according to their cellular location. CAT-A of B. cinerea resembled most closely the peroxisomal catalases. Northern blot analysis showed induction of the gene by H 2 O 2 in vitro. In planta , no catA expression could be detected by northern blot analysis, whereas a constitutively expressed beta-tubulin mRNA of B. cinerea was detectable and symptom development on the inoculated leaves was very clear. However, a catalase gene cat1 of tomato appeared to be induced from the time of fungal penetration onwards, suggesting that H 2 O 2 is produced during the interaction.