MoRad6‐mediated ubiquitination pathways are essential for development and pathogenicity in<i>Magnaporthe oryzae</i>

Shi, Huanbin; Chen, Yaping; Dong, Bo; Lu, Jianping; Liu, Xiao-Hong; Lin, Fu‐Cheng

doi:10.1111/1462-2920.13515

Cited by 26 publications

(29 citation statements)

References 64 publications

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“…Post-translational modification by ubiquitin is essential for regulation of protein abundance and function. Previous studies have revealed importance of the ubiquitin system in the model plant pathogenic fungus M. oryzae ( McCafferty and Talbot, 1998 ; Oh et al, 2012 ; Prakash et al, 2016 ; Shi et al, 2016 ). However, little has been addressed on the deubiquitination process.…”

Section: Discussionmentioning

confidence: 99%

A Deubiquitinating Enzyme Ubp14 Is Required for Development, Stress Response, Nutrient Utilization, and Pathogenesis of Magnaporthe oryzae

et al. 2018

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Ubiquitination is an essential protein modification in eukaryotic cells, which is reversible. Deubiquitinating enzymes (DUBs) catalyze deubiquitination process to reverse ubiquitination, maintain ubiquitin homeostasis or promote protein degradation by recycling ubiquitins. In order to investigate effects of deubiquitination process in plant pathogenic fungus Magnaporthe oryzae, we generated deletion mutants of MoUBP14. Ortholog of MoUbp14 was reported to play general roles in ubiquitin-mediated protein degradation in Saccharomyces cerevisiae. The ΔMoubp14 mutant lost its pathogenicity and was severely reduced in mycelial growth, sporulation, carbon source utilization, and increased in sensitivity to distinct stresses. The mutant was blocked in penetration, which could due to defect in turgor generation. It is also blocked in invasive growth, which could due to reduction in stress tolerance and nutrient utilization. Deletion of UBP14 also led to accumulation of free polyubiquitin chains. Pulldown assay identified some proteins related to carbohydrate metabolism and stress response may putatively interact with MoUbp14, including two key rate-limiting enzymes of gluconeogenesis, MoFbp1 and MoPck1. These two proteins were degraded when the glucose was supplied to M. oryzae grown in low glucose media for a short period of time (∼12 h), and this process required MoUbp14. In summary, pleiotropic phenotypes of the deletion mutants indicated that MoUbp14 is required for different developments and pathogenicity of M. oryzae.

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Section: Discussionmentioning

confidence: 99%

A Deubiquitinating Enzyme Ubp14 Is Required for Development, Stress Response, Nutrient Utilization, and Pathogenesis of Magnaporthe oryzae

et al. 2018

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“…To test whether MoGrp1 contributes to intron splicing, two genes, MST7 and MoRAD6, which are important to fungal growth, conidiation, and pathogenicity in M. oryzae (Zhao et al 2005;Shi et al 2016a), were selected for analysis. The intron splicing efficiency was evaluated by RT-PCR with a pair of primers amplifying the intron region.…”

Section: Mogrp1 Is Necessary For Normal Splicing Of Genes Involved Inmentioning

confidence: 99%

A glycine-rich protein MoGrp1 functions as a novel splicing factor to regulate fungal virulence and growth in Magnaporthe oryzae

et al. 2019

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Glycine-rich proteins (GRPs) have diverse amino acid sequences and are involved in a variety of biological processes. The role of GRPs in plant pathogenic fungi has not been reported. In this study, we identified and functionally characterized a novel gene named MoGRP1 in Magnaporthe oryzae, which encodes a protein that has an N-terminal RNA recognition motif (RRM) and a C-terminal glycine-rich domain with four Arg-Gly-Gly (RGG) repeats. Deletion of MoGRP1 resulted in dramatic reductions in fungal virulence, mycelial growth, and conidiation. The ΔMogrp1 mutants were also defective in cell wall integrity and in their responses to different stresses. MoGrp1 was localized to the nucleus and was co-immunoprecipitated with several components of the spliceosome, including subunits of the U1 snRNP and U2 snRNP complexes. Moreover, MoGrp1 exhibited binding affinity for poly(U). Importantly, MoGrp1 was responsible for the normal splicing of genes involved in infection-related morphogenesis. Domain deletion assays showed that both the RRM domain and its two adjacent RGG repeats were essential to the full function of MoGrp1. Notably, the nine amino acids between the first and the second RGG repeats were indispensable for nuclear localization and for the biological functions of MoGrp1. Taken together, our data suggest that MoGrp1 functions as a novel splicing factor with poly(U) binding activity to regulate fungal virulence, development, and stress responses in the rice blast fungus.

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“…Recent evidence has shown that conidial germination is delayed by a proteasome inhibitor Bertomzib, indicating that the ubiquitin system plays a critical role in triggering germination (Oh et al ., ). Our previous results identified an RING‐type ubiquitin ligase MoUbr1 involved in activating conidial germination (Shi et al ., ). In this study, we found that Δ Mofbx15 , Δ Mocdc4 and Δ Mofwd1 also displayed obvious germination defects in different degrees, with Δ Mofwd1 the most severe, suggesting that conidial germination is regulated by a complex network in which the ubiquitin system components take part.…”

Section: Discussionmentioning

confidence: 97%

“…The expression of MoFrq was monitored by qPCR. Protein extraction and western blotting were performed as previously described (Shi et al, 2016).…”

Section: Fluorescent-microscopy Observationmentioning

confidence: 99%

F‐box proteins MoFwd1, MoCdc4 and MoFbx15 regulate development and pathogenicity in the rice blast fungus Magnaporthe oryzae

Shi

Chen

Zhu

et al. 2019

Environmental Microbiology

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Summary The Skp1‐Cul1‐F‐box‐protein (SCF) ubiquitin ligases are important parts of the ubiquitin system controlling many cellular biological processes in eukaryotes. However, the roles of SCF ubiquitin ligases remain unclear in phytopathogenic Magnaporthe oryzae. Here, we cloned 24 F‐box proteins and confirmed that 17 proteins could interact with MoSkp1, showing their potential to participate in SCF complexes. To determine their functions, null mutants of 21 F‐box‐containing genes were created. Among them, the F‐box proteins MoFwd1, MoCdc4 and MoFbx15 were found to be required for growth, development and full virulence. Fluorescent‐microscopy observations demonstrated that both MoFbx15 and MoCdc4 were localized to the nucleus, compared with MoFwd1, which was distributed in the cytosol. MoCdc4 and MoFwd1 bound to MoSkp1 via the F‐box domain, the deletion of which abrogated their function. Race tube and qRT‐PCR assays confirmed that MoFwd1 was involved in circadian rhythm by regulating transcription and protein stability of the core circadian clock regulator MoFRQ. Moreover, MoFWD1 also orchestrates conidial germination by influencing conidial amino acids pools and oxidative stress release. Overall, our results indicate that SCF ubiquitin ligases play indispensable roles in development and pathogenicity in M. oryzae.

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MoRad6‐mediated ubiquitination pathways are essential for development and pathogenicity inMagnaporthe oryzae

Cited by 26 publications

References 64 publications

A Deubiquitinating Enzyme Ubp14 Is Required for Development, Stress Response, Nutrient Utilization, and Pathogenesis of Magnaporthe oryzae

A Deubiquitinating Enzyme Ubp14 Is Required for Development, Stress Response, Nutrient Utilization, and Pathogenesis of Magnaporthe oryzae

A glycine-rich protein MoGrp1 functions as a novel splicing factor to regulate fungal virulence and growth in Magnaporthe oryzae

F‐box proteins MoFwd1, MoCdc4 and MoFbx15 regulate development and pathogenicity in the rice blast fungus Magnaporthe oryzae

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