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  • Scientific Societies  (4)
  • 1
    Online Resource
    Online Resource
    The Activators of Type 2A Phosphatases (PP2A) Regulate Multiple Cellular Processes Via PP2A-Dependent and -Independent Mechanisms in Fusarium graminearum
    Scientific Societies ; 2018
    In:  Molecular Plant-Microbe Interactions® Vol. 31, No. 11 ( 2018-11), p. 1121-1133
    Details
    In: Molecular Plant-Microbe Interactions®, Scientific Societies, Vol. 31, No. 11 ( 2018-11), p. 1121-1133
    Abstract: The type 2A protein phosphatases (PP2As) are holoenzymes in all eukaryotes but their activators remain unknown in filamentous fungi. Fusarium graminearum contains three PP2As (FgPp2A, FgSit4, and FgPpg1), which play critical roles in fungal growth, development, and virulence. Here, we identified two PP2A activators (PTPAs), FgRrd1 and FgRrd2, and found that they control PP2A activity in a PP2A-specific manner. FgRrd1 interacts with FgPpg1, but FgRrd2 interacts with FgPp2A and very weakly with FgSit4. Furthermore, FgRrd2 activates FgPp2A via regulating FgPp2A methylation. Phenotypic assays showed that FgRrd1 and FgRrd2 regulate mycelial growth, conidiation, sexual development, and lipid droplet biogenesis. More importantly, both FgRrd1 and FgRrd2 interact with RNA polymerase II, subsequently modulating its enrichments at the promoters of mycotoxin biosynthesis genes, which is independent on PP2A. In addition, FgRrd2 modulates response to phenylpyrrole fungicide, via regulating the phosphorylation of kinase FgHog1 in the high-osmolarity glycerol pathway, and to caffeine, via modulating FgPp2A methylation. Taken together, results of this study indicate that FgRrd1 and FgRrd2 regulate multiple physiological processes via different regulatory mechanisms in F. graminearum, which provides a novel insight into understanding the biological functions of PTPAs in fungi.
    Type of Medium: Online Resource
    ISSN: 0894-0282 , 1943-7706
    URL: Article
    DOI: 10.1094/MPMI-03-18-0056-R
    Language: English
    Publisher: Scientific Societies
    Publication Date: 2018
    detail.hit.zdb_id: 2037108-1
    SSG: 12
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    Online Resource
  • 2
    Online Resource
    Online Resource
    The Importin FgPse1 Is Required for Vegetative Development, Virulence, and Deoxynivalenol Production by Interacting with the Nuclear Polyadenylated RNA-Binding Protein FgNab2 in Fusarium graminearum
    Scientific Societies ; 2022
    In:  Phytopathology® Vol. 112, No. 5 ( 2022-05), p. 1072-1080
    Details
    In: Phytopathology®, Scientific Societies, Vol. 112, No. 5 ( 2022-05), p. 1072-1080
    Abstract: Karyopherins are involved in transport through nuclear pore complexes. Karyopherins are necessary for nuclear import and export pathways and bind to their cargos. Polyadenylation of messenger RNA (mRNA) is necessary for various biological processes, regulating gene expression in eukaryotes. Until now, the association of karyopherin with mRNA polyadenylation has been less understood in plant pathogenic fungi. In our study, we focused on the biological functions of the karyopherin FgPse1 in Fusarium graminearum. The results showed that FgPse1 is involved in mycelial growth, asexual reproduction, virulence, and deoxynivalenol (DON) production. Co-immunoprecipitation and bimolecular fluorescence complementation showed that FgPse1 interacts with the nuclear polyadenylated RNA-binding protein FgNab2. Moreover, a fluorescence localization assay indicated that FgPse1 is necessary for the nuclear import of FgNab2. The nuclear import of FgNab2 regulates the expression of FgTri4, FgTri5, and FgTri6, which are essential for DON production. Thus, ΔFgPse1 and ΔFgNab2 showed consistent defects in DON production. In summary, our data indicated that FgPse1 is necessary for mycelial growth, virulence, and DON production, interacting with FgNab2 in F. graminearum. These results contribute to our understanding of the functions of importins in phytopathogenic fungi.
    Type of Medium: Online Resource
    ISSN: 0031-949X , 1943-7684
    URL: Article
    DOI: 10.1094/PHYTO-08-21-0357-R
    Language: English
    Publisher: Scientific Societies
    Publication Date: 2022
    detail.hit.zdb_id: 2037027-1
    SSG: 12
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  • 3
    Online Resource
    Online Resource
    Fungicide Resistance: Progress in Understanding Mechanism, Monitoring, and Management
    Scientific Societies ; 2023
    In:  Phytopathology® Vol. 113, No. 4 ( 2023-04), p. 707-718
    Details
    In: Phytopathology®, Scientific Societies, Vol. 113, No. 4 ( 2023-04), p. 707-718
    Abstract: Fungicide treatments are often essential for maintaining healthy crops and to achieve reliable and high-quality yields. However, continued use of fungicides with the same modes of action can lead to development of fungicide resistance, which has emerged in various plant pathogens and is a serious threat to effective crop protection. Exploration of resistance mechanisms is critical for resistance monitoring and management. This brief review summarizes advances during the past five decades in understanding the molecular resistance mechanisms of plant pathogenic fungi and oomycetes to major classes of fungicides, including benzimidazoles, myosin inhibitors, sterol demethylation inhibitors, quinone outside inhibitors, succinate dehydrogenase inhibitors, anilinopyrimidines, carboxylic acid amides, and oxysterol-binding protein homolog inhibitors. Based on known resistance mechanisms, PCR- and loop-mediated isothermal amplification-based approaches have been developed to allow high-throughput monitoring and early/rapid detection of emerging resistance. Classical principles in fungicide resistance management are also summarized, including using different modes of action of fungicides, limiting the number of applications of the chemicals with site-specific modes of action, and avoidance of their eradicant use. Future studies on novel strategies of disease management, including development of epigenetics- and RNA-based fungicides, will provide valuable knowledge for management of fungicide resistance.
    Type of Medium: Online Resource
    ISSN: 0031-949X , 1943-7684
    URL: Article
    DOI: 10.1094/PHYTO-10-22-0370-KD
    Language: English
    Publisher: Scientific Societies
    Publication Date: 2023
    detail.hit.zdb_id: 2037027-1
    SSG: 12
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  • 4
    Online Resource
    Online Resource
    Identification and Characterization of Carbendazim-Resistant Isolates of Gibberella zeae
    Scientific Societies ; 2010
    In:  Plant Disease Vol. 94, No. 9 ( 2010-09), p. 1137-1142
    Details
    In: Plant Disease, Scientific Societies, Vol. 94, No. 9 ( 2010-09), p. 1137-1142
    Abstract: Sensitivity of Gibberella zeae to carbendazim was determined by measuring mycelial growth in fungicide-amended media. Among 1,529 isolates tested, 31 isolates showed a high level of resistance (HR) to carbendazim (fungicide concentration that results in 50% inhibition of mycelial growth [EC 50 ] of 10.35 to 30.26 mg a.i. liter –1 ) and 10 isolates were moderately resistant (MR) (EC 50 of 4.50 to 7.28 mg a.i. liter –1 ). The remaining 1,488 isolates were sensitive to carbendazim and were unable to grow on potato dextrose agar amended with carbendazim at 2 mg a.i. liter –1 . Analysis of DNA sequences of the β2-tubulin (Tub2) gene showed that all 10 MR isolates had a point mutation at codon 198 causing a replacement of glutamic acid by glutamine. At the codon position 167, the amino acid phenylalanine was replaced by tyrosine in 28 of 31 HR isolates. The remaining three HR isolates had a point mutation at codon 200 which converted phenylalanine to tyrosine. Based on these point mutations in the Tub2 gene, allele-specific polymerase chain reaction primers were developed for rapid detection of the point mutations. The rapid molecular method will be a valuable tool for the monitoring of carbendazim resistance in G. zeae. Additionally, deletion of the β1-tubulin gene (Tub1) in the HR isolate GJ33 resulted in increased resistance to carbendazim. These results indicate that Tub1 plays a role in the sensitivity of G. zeae to carbendazim.
    Type of Medium: Online Resource
    ISSN: 0191-2917 , 1943-7692
    URL: Article
    DOI: 10.1094/PDIS-94-9-1137
    Language: English
    Publisher: Scientific Societies
    Publication Date: 2010
    detail.hit.zdb_id: 2042679-3
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