Functional and Structural Comparison of Pyrrolnitrin- and Iprodione-Induced Modifications in the Class III Histidine-Kinase Bos1 of Botrytis cinerea

Autor: Sakhr Ajouz, Philippe C. Nicot, Sabine Fillinger, Pierre Leroux, Marc Bardin
Přispěvatelé: BIOlogie et GEstion des Risques en agriculture (BIOGER), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Unité de Pathologie Végétale (PV), Institut National de la Recherche Agronomique (INRA), AgroParisTech-Institut National de la Recherche Agronomique (INRA), Station de Pathologie Végétale (AVI-PATHO)
Rok vydání: 2012
Předmět:
[SDV.SA]Life Sciences [q-bio]/Agricultural sciences
Models
Molecular
0106 biological sciences
Antifungal Agents
Histidine Kinase
Mutant
lcsh:Medicine
Plant Science
medicine.disease_cause
01 natural sciences
chemistry.chemical_compound
Fungal Evolution
lcsh:Science
Botrytis cinerea
2. Zero hunger
Genetics
0303 health sciences
Mutation
Multidisciplinary
Iprodione
biology
Agriculture
Pyrrolnitrin
FUNGICIDE RESISTANCE
Biochemistry
Botrytis
HAMP
Agrochemicals
Research Article
Evolutionary Processes
Molecular Sequence Data
Plant Pathogens
SIGNAL-TRANSDUCTION
Mutagenesis (molecular biology technique)
DICARBOXIMIDE-RESISTANCE
Mycology
Microbiology
MECHANISMS
03 medical and health sciences
GENETIC-ANALYSIS
IN-FIELD STRAINS
PHENYLPYRROLE-RESISTANCE
NEUROSPORA-CRASSA
USTILAGO-MAYDIS
HAMP DOMAINS
Drug Resistance
Fungal
Osmotic Pressure
medicine
Amino Acid Sequence
Pesticides
Biology
030304 developmental biology
Evolutionary Biology
Hydantoins
lcsh:R
Histidine kinase
Fungi
Plant Pathology
Aminoimidazole Carboxamide
biology.organism_classification
Protein Structure
Tertiary
chemistry
Mutagenesis
Site-Directed
lcsh:Q
Pest Control
Protein Kinases
Protein Processing
Post-Translational
010606 plant biology & botany
Zdroj: PLoS ONE
PLoS ONE, Public Library of Science, 2012, 7 (8), 14 p. ⟨10.1371/journal.pone.0042520⟩
Plos One 8 (7), 14 p.. (2012)
PLoS ONE, Vol 7, Iss 8, p e42520 (2012)
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0042520
Popis: Dicarboximides and phenylpyrroles are commonly used fungicides against plant pathogenic ascomycetes. Although their effect on fungal osmosensing systems has been shown in many studies, their modes-of-action still remain unclear. Laboratory- or field-mutants of fungi resistant to either or both fungicide categories generally harbour point mutations in the sensor histidine kinase of the osmotic signal transduction cascade. In the present study we compared the mechanisms of resistance to the dicarboximide iprodione and to pyrrolnitrin, a structural analogue of phenylpyrrole fungicides, in Botrytis cinerea. Pyrrolnitrin-induced mutants and iprodione-induced mutants of B. cinerea were produced in vitro. For the pyrrolnitrin-induced mutants, a high level of resistance to pyrrolnitrin was associated with a high level of resistance to iprodione. For the iprodione-induced mutants, the high level of resistance to iprodione generated variable levels of resistance to pyrrolnitrin and phenylpyrroles. All selected mutants showed hypersensitivity to high osmolarity and regardless of their resistance levels to phenylpyrroles, they showed strongly reduced fitness parameters (sporulation, mycelial growth, aggressiveness on plants) compared to the parental phenotypes. Most of the mutants presented modifications in the osmosensing class III histidine kinase affecting the HAMP domains. Site directed mutagenesis of the bos1 gene was applied to validate eight of the identified mutations. Structure modelling of the HAMP domains revealed that the replacements of hydrophobic residues within the HAMP domains generally affected their helical structure, probably abolishing signal transduction. Comparing mutant phenotypes to the HAMP structures, our study suggests that mutations perturbing helical structures of HAMP2-4 abolish signal-transduction leading to loss-of-function phenotype. The mutation of residues E529, M427, and T581, without consequences on HAMP structure, highlighted their involvement in signal transduction. E529 and M427 seem to be principally involved in osmotic signal transduction.
Databáze: OpenAIRE
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