Fungicide resistance toward fludioxonil conferred by overexpression of the phosphatase gene MoPTP2 in Magnaporthe oryzae.
Dioxoles
/ pharmacology
Drug Resistance, Fungal
Fungal Proteins
/ analysis
Fungicides, Industrial
/ pharmacology
Gene Deletion
Gene Expression
Magnaporthe
/ drug effects
Mitogen-Activated Protein Kinases
/ metabolism
Oryza
/ microbiology
Phosphoproteins
/ analysis
Phosphorylation
Plant Diseases
/ microbiology
Protein Processing, Post-Translational
Protein Tyrosine Phosphatases
/ biosynthesis
Proteome
/ analysis
Pyrroles
/ pharmacology
Journal
Molecular microbiology
ISSN: 1365-2958
Titre abrégé: Mol Microbiol
Pays: England
ID NLM: 8712028
Informations de publication
Date de publication:
03 2019
03 2019
Historique:
accepted:
29
11
2018
pubmed:
12
12
2018
medline:
3
8
2019
entrez:
12
12
2018
Statut:
ppublish
Résumé
The fungicide fludioxonil causes hyperactivation of the Hog1p MAPK within the high-osmolarity glycerol signaling pathway essential for osmoregulation in pathogenic fungi. The molecular regulation of MoHog1p phosphorylation is not completely understood in pathogenic fungi. Thus, we identified and characterized the putative MoHog1p-interacting phosphatase gene MoPTP2 in the filamentous rice pathogen Magnaporthe oryzae. We found overexpression of MoPTP2 conferred fludioxonil resistance in M. oryzae, whereas the 'loss of function' mutant ΔMoptp2 was more susceptible toward the fungicide. Additionally, quantitative phosphoproteome profiling of MoHog1p phosphorylation revealed lower phosphorylation levels of MoHog1p in the MoPtp2p overexpression mutant compared to the wild-type strain, whereas MoHog1p phosphorylation increased in the ΔMoptp2 mutant. Furthermore, we identified a set of MoHog1p-dependent genes regulated by the MoPtp2p expression level. Our results indicate that the phosphatase MoPtp2p is involved in the regulation of MoHog1p phosphorylation and that overexpression of the gene MoPTP2 is a novel molecular mechanism of fungicide resistance.
Substances chimiques
Dioxoles
0
Fungal Proteins
0
Fungicides, Industrial
0
Phosphoproteins
0
Proteome
0
Pyrroles
0
Mitogen-Activated Protein Kinases
EC 2.7.11.24
Protein Tyrosine Phosphatases
EC 3.1.3.48
fludioxonil
ENS9J0YM16
Types de publication
Journal Article
Langues
eng
Pagination
662-677Informations de copyright
© 2018 John Wiley & Sons Ltd.