Abstract
The fungicide fludioxonil is used to control plant-pathogenic fungi by causing improper activation of the Hog1-type MAPK. However, the appearance of fludioxonil resistant mutants, mostly caused by mutations in the group III histidine kinases, poses a serious problem. Moreover, such mutations cause also hyperosmotic sensitivity and the underlying mechanism has been elusive for a long time. Using Saccharomyces cerevisiae as an experimental host, we show that those phenotypes are conferred by a constitutively active form of the group III histidine kinase. Our results explain the different reasons for fludioxonil resistance conferred by its deletion and missense mutation.
Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Antifungal Agents / pharmacology*
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Biochemistry / methods
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Dioxoles / pharmacology*
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Drug Resistance, Fungal
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Gene Deletion
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Gene Expression Regulation, Fungal*
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Genes, Reporter
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Histidine Kinase
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Molecular Sequence Data
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Mutation*
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Mutation, Missense
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Phenotype
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Protein Kinases / metabolism
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Protein Serine-Threonine Kinases / genetics*
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Protein Serine-Threonine Kinases / metabolism
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Pyrroles / pharmacology*
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins / genetics*
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Saccharomyces cerevisiae Proteins / metabolism
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Sequence Homology, Amino Acid
Substances
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Antifungal Agents
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Dioxoles
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Pyrroles
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Saccharomyces cerevisiae Proteins
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Protein Kinases
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HSL1 protein, S cerevisiae
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Protein Serine-Threonine Kinases
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Histidine Kinase
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fludioxonil