Site‐directed mutagenesis of the P225, N230 and H272 residues of succinate dehydrogenase subunit B from Botrytis cinerea highlights different roles in enzyme activity and inhibitor binding

Carboxamide fungicides target succinate dehydrogenase (SDH). Recent field monitoring studies have identified Botrytis cinerea isolates resistant to one or several SDH inhibitors (SDHIs) with amino acid substitutions in the SDH B subunit. We confirmed, by site‐directed mutagenesis of the sdhB gene, t...

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Veröffentlicht in:	Environmental microbiology 2014-07, Vol.16 (7), p.2253-2266
Hauptverfasser:	Lalève, Anaïs, Gamet, Stéphanie, Walker, Anne‐Sophie, Debieu, Danièle, Toquin, Valérie, Fillinger, Sabine
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Substitution Animal, plant and microbial ecology Benzamides Biological and medical sciences Biphenyl Compounds boscalid Botrytis - drug effects Botrytis - enzymology Botrytis - genetics Botrytis cinerea Carboxin Dehydrogenases Drug Resistance, Fungal - genetics enzyme activity enzyme inhibition Enzyme Inhibitors Enzymes Fundamental and applied biological sciences. Psychology Fungal Proteins - chemistry Fungal Proteins - genetics Fungal Proteins - metabolism Fungicides, Industrial General aspects genes growth retardation hypersensitivity Life Sciences Microbial ecology Microbiology Miscellaneous monitoring Mutagenesis Mutagenesis, Site-Directed Mutation Mycology Niacinamide - analogs & derivatives Protein Binding Protein Subunits - chemistry Protein Subunits - genetics Protein Subunits - metabolism Pyridines Structure-Activity Relationship succinate dehydrogenase Succinate Dehydrogenase - chemistry Succinate Dehydrogenase - genetics Succinate Dehydrogenase - metabolism
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