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Updated: May 26, 2026

Monitoring Stub1-Mediated Pexophagy
Published on: May 12, 2023
The PEX7-mediated peroxisomal import system is required for fungal development and pathogenicity in Magnaporthe
Jaeduk Goh1, Junhyun Jeon, Kyoung Su Kim
1Department of Agricultural Biotechnology, Center for Fungal Genetic Resources, Plant Genomics and Breeding Institute, Seoul National University, Seoul, Korea.
Abstract:
In eukaryotes, microbodies called peroxisomes play important roles in cellular activities during the life cycle. Previous studies indicate that peroxisomal functions are important for plant infection in many phytopathogenic fungi, but detailed relationships between fungal pathogenicity and peroxisomal function still remain unclear. Here we report the importance of peroxisomal protein import through PTS2 (Peroxisomal Targeting Signal 2) in fungal development and pathogenicity of Magnaporthe oryzae. Using an Agrobacterium tumefaciens-mediated transformation library, a pathogenicity-defective mutant was isolated from M. oryzae and identified as a T-DNA insert in the PTS2 receptor gene, MoPEX7. Gene disruption of MoPEX7 abolished peroxisomal localization of a thiolase (MoTHL1) containing PTS2, supporting its role in the peroxisomal protein import machinery. ΔMopex7 showed significantly reduced mycelial growth on media containing short-chain fatty acids as a sole carbon source. ΔMopex7 produced fewer conidiophores and conidia, but conidial germination was normal. Conidia of ΔMopex7 were able to develop appressoria, but failed to cause disease in plant cells, except after wound inoculation. Appressoria formed by ΔMopex7 showed a defect in turgor generation due to a delay in lipid degradation and increased cell wall porosity during maturation. Taken together, our results suggest that the MoPEX7-mediated peroxisomal matrix protein import system is required for fungal development and pathogenicity M. oryzae.
Insights
The peroxisomal targeting signal 2 (PTS2) receptor, MoPEX7, is crucial for the fungal pathogen Magnaporthe oryzae. Its disruption impairs fungal development and pathogenicity by affecting peroxisomal protein import and lipid metabolism.
Area of Science:
- Plant pathology
- Mycology
- Cell biology
Background:
- Peroxisomes are vital organelles in eukaryotic cells, involved in various metabolic processes.
- Peroxisomal functions are known to influence pathogenicity in phytopathogenic fungi, but specific mechanisms remain elusive.
- The import of matrix proteins into peroxisomes is mediated by targeting signals like PTS2.
Purpose of the Study:
- To investigate the role of peroxisomal protein import via PTS2 in the development and pathogenicity of the rice blast fungus, Magnaporthe oryzae.
- To elucidate the function of the PTS2 receptor gene, MoPEX7, in M. oryzae.
Main Methods:
- Isolation and characterization of a pathogenicity-defective mutant using Agrobacterium tumefaciens-mediated transformation.
- Gene disruption of the MoPEX7 gene in M. oryzae.
- Analysis of peroxisomal protein import by examining the localization of a PTS2-containing thiolase (MoTHL1).
- Assessment of fungal growth, development (conidiation), and pathogenicity assays on host plants.
Main Results:
- Disruption of MoPEX7 abolished the peroxisomal import of MoTHL1, confirming MoPEX7's role in the PTS2 import pathway.
- The ΔMopex7 mutant exhibited significantly reduced mycelial growth on fatty acids and impaired conidiophore/conidia production.
- While conidial germination and appressoria formation were normal, ΔMopex7 conidia failed to cause disease, except in wounded tissues.
- Defective appressoria in ΔMopex7 showed impaired turgor generation due to delayed lipid degradation and increased cell wall porosity.
Conclusions:
- The MoPEX7-mediated peroxisomal protein import system is essential for the vegetative growth and development of M. oryzae.
- Proper peroxisomal function, regulated by MoPEX7, is critical for M. oryzae pathogenicity, particularly for appressorial function and host cell penetration.
- This study highlights the importance of peroxisomal matrix protein import in fungal pathogenesis.
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