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SUMOylation is required for fungal development and pathogenicity in the rice blast fungus Magnaporthe oryzae.

ABSTRACT: Amongst the various post-translational modifications (PTMs), SUMOylation is a conserved process of attachment of a small ubiquitin-related modifier (SUMO) to a protein substrate in eukaryotes. This process regulates many important biological mechanisms, including transcriptional regulation, protein stabilization, cell cycle, DNA repair and pathogenesis. However, the functional role of SUMOylation is not well understood in plant-pathogenic fungi, including the model fungal pathogen Magnaporthe oryzae. In this study, we elucidated the roles of four SUMOylation-associated genes that encode one SUMO protein (MoSMT3), two E1 enzymes (MoAOS1 and MoUBA2) and one E2 enzyme (MoUBC9) in fungal development and pathogenicity. Western blot assays showed that SUMO modification was abolished in all deletion mutants. MoAOS1 and MoUBA2 were mainly localized in the nucleus, whereas MoSMT3 and MoUBC9 were localized in both the nucleus and cytoplasm. However, the four SUMOylation-associated proteins were predominantly localized in the nucleus under oxidative stress conditions. Deletion mutants for each of the four genes were viable, but showed significant defects in mycelial growth, conidiation, septum formation, conidial germination, appressorium formation and pathogenicity. Several proteins responsible for conidiation were predicted to be SUMOylated, suggesting that conidiation is controlled at the post-translational level by SUMOylation. In addition to infection-related development, SUMOylation also played important roles in resistance to nutrient starvation, DNA damage and oxidative stresses. Therefore, SUMOylation is required for infection-related fungal development, stress responses and pathogenicity in M. oryzae. This study provides new insights into the role of SUMOylation in the molecular mechanisms of pathogenesis of the rice blast fungus and other plant pathogens.

SUBMITTER: Lim YJ

PROVIDER: S-EPMC6638150 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature

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SUMOylation is required for fungal development and pathogenicity in the rice blast fungus Magnaporthe oryzae.

Lim You-Jin YJ Kim Ki-Tae KT Lee Yong-Hwan YH

Molecular plant pathology 20180717 9

Amongst the various post-translational modifications (PTMs), SUMOylation is a conserved process of attachment of a small ubiquitin-related modifier (SUMO) to a protein substrate in eukaryotes. This process regulates many important biological mechanisms, including transcriptional regulation, protein stabilization, cell cycle, DNA repair and pathogenesis. However, the functional role of SUMOylation is not well understood in plant-pathogenic fungi, including the model fungal pathogen Magnaporthe or ...[more]

PMID: 29633464

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Project description:Rice blast disease caused by Magnaporthe oryzae is a devastating disease of cultivated rice worldwide. Infections by this fungus lead to a significant reduction in rice yields and threats to food security. To gain better insight into growth and cell death in M. oryzae during infection, we characterized two predicted M. oryzae metacaspase proteins, MoMca1 and MoMca2. These proteins appear to be functionally redundant and can complement the yeast Yca1 homologue. Biochemical analysis revealed that M. oryzae metacaspases exhibited Ca2+-dependent caspase activity in vitro Deletion of both MoMca1 and MoMca2 in M. oryzae resulted in reduced sporulation, delay in conidial germination, and attenuation of disease severity. In addition, the double ΔMomca1mca2 mutant strain showed increased radial growth in the presence of oxidative stress. Interestingly, the ΔMomca1mca2 strain showed an increased accumulation of insoluble aggregates compared to the wild-type strain during vegetative growth. Our findings suggest that MoMca1 and MoMca2 promote the clearance of insoluble aggregates in M. oryzae, demonstrating the important role these metacaspases have in fungal protein homeostasis. Furthermore, these metacaspase proteins may play additional roles, like in regulating stress responses, that would help maintain the fitness of fungal cells required for host infection.IMPORTANCEMagnaporthe oryzae causes rice blast disease that threatens global food security by resulting in the severe loss of rice production every year. A tightly regulated life cycle allows M. oryzae to disarm the host plant immune system during its biotrophic stage before triggering plant cell death in its necrotrophic stage. The ways M. oryzae navigates its complex life cycle remain unclear. This work characterizes two metacaspase proteins with peptidase activity in M. oryzae that are shown to be involved in the regulation of fungal growth and development prior to infection by potentially helping maintain fungal fitness. This study provides new insights into the role of metacaspase proteins in filamentous fungi by illustrating the delays in M. oryzae morphogenesis in the absence of these proteins. Understanding the mechanisms by which M. oryzae morphology and development promote its devastating pathogenicity may lead to the emergence of proper methods for disease control.

Project description:BackgroundMagnaporthe oryzae, the causal agent of blast disease of rice, is the most destructive disease of rice worldwide. The genome of this fungal pathogen has been sequenced and an automated annotation has recently been updated to Version 6 http://www.broad.mit.edu/annotation/genome/magnaporthe_grisea/MultiDownloads.html. However, a comprehensive manual curation remains to be performed. Gene Ontology (GO) annotation is a valuable means of assigning functional information using standardized vocabulary. We report an overview of the GO annotation for Version 5 of M. oryzae genome assembly.MethodsA similarity-based (i.e., computational) GO annotation with manual review was conducted, which was then integrated with a literature-based GO annotation with computational assistance. For similarity-based GO annotation a stringent reciprocal best hits method was used to identify similarity between predicted proteins of M. oryzae and GO proteins from multiple organisms with published associations to GO terms. Significant alignment pairs were manually reviewed. Functional assignments were further cross-validated with manually reviewed data, conserved domains, or data determined by wet lab experiments. Additionally, biological appropriateness of the functional assignments was manually checked.ResultsIn total, 6,286 proteins received GO term assignment via the homology-based annotation, including 2,870 hypothetical proteins. Literature-based experimental evidence, such as microarray, MPSS, T-DNA insertion mutation, or gene knockout mutation, resulted in 2,810 proteins being annotated with GO terms. Of these, 1,673 proteins were annotated with new terms developed for Plant-Associated Microbe Gene Ontology (PAMGO). In addition, 67 experiment-determined secreted proteins were annotated with PAMGO terms. Integration of the two data sets resulted in 7,412 proteins (57%) being annotated with 1,957 distinct and specific GO terms. Unannotated proteins were assigned to the 3 root terms. The Version 5 GO annotation is publically queryable via the GO site http://amigo.geneontology.org/cgi-bin/amigo/go.cgi. Additionally, the genome of M. oryzae is constantly being refined and updated as new information is incorporated. For the latest GO annotation of Version 6 genome, please visit our website http://scotland.fgl.ncsu.edu/smeng/GoAnnotationMagnaporthegrisea.html. The preliminary GO annotation of Version 6 genome is placed at a local MySql database that is publically queryable via a user-friendly interface Adhoc Query System.ConclusionOur analysis provides comprehensive and robust GO annotations of the M. oryzae genome assemblies that will be solid foundations for further functional interrogation of M. oryzae.

Dataset Information

SUMOylation is required for fungal development and pathogenicity in the rice blast fungus Magnaporthe oryzae.

Publications

SUMOylation is required for fungal development and pathogenicity in the rice blast fungus Magnaporthe oryzae.

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