Autor: |
A Simaan, Hayat Hage, Fred Beisson, Sacha Grisel, Harry Brumer, Marie-Noëlle Rosso, Bastien Bissaro, David Ribeaucourt, Jean-Guy Berrin, Stephanie M. Forget, Richard J. O'Connell, Mickael Lafond, Mireille Haon, Yasuyuki Kubo, Sayo Kodama |
Rok vydání: |
2021 |
Předmět: |
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DOI: |
10.21203/rs.3.rs-493001/v1 |
Popis: |
Copper radical oxidases (CRO) form a class of enzymes with a longstanding history encompassing diverse substrate specificities. While the biological function of most CROs remains unknown, we observed that CROs active on aliphatic alcohols are found only in fungal plant pathogens. Here, we unveil the role of these CROs and the identity of their natural redox partner, a haem-iron peroxidase. Combining multiscale approaches, we report that Colletotrichum and Magnaporthe appressoria (specialized cells that puncture the plant cuticles) co-secrete this pair of metalloenzymes early during penetration. We show in vivo that mutant appressoria lacking either or both enzymes have impaired penetration ability and pathogenicity. We reveal in vitro a finely-tuned enzyme interplay is responsible for the oxidation of plant cuticular long-chain alcohols into aldehyde products, suggested to act as key molecular signals in the fungal infection machinery. Our results open new avenues to design oxidase-specific inhibitors as anti-penetrants for crop protection. |
Databáze: |
OpenAIRE |
Externí odkaz: |
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