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PoMet3 and PoMet14 associated with sulfate assimilation are essential for conidiogenesis and pathogenicity in Pyricularia oryzae

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Abstract

Pyricularia oryzae is the causal agent of blast disease on staple gramineous crops. Sulphur is an essential element for the biosynthesis of cysteine and methionine in fungi. Here, we targeted the P. oryzae PoMET3 encoding the enzyme ATP sulfurylase, and PoMET14 encoding the APS (adenosine-5′-phosphosulphate) kinase that are involved in sulfate assimilation and sulphur-containing amino acids biosynthesis. In P. oryzae, deletion of PoMET3 or PoMET14 separately results in defects of conidiophore formation, significant impairments in conidiation, methionine and cysteine auxotrophy, limited invasive hypha extension, and remarkably reduced virulence on rice and barley. Furthermore, the defects of the null mutants could be restored by supplementing with exogenous cysteine or methionine. Our study explored the biological functions of sulfur assimilation and sulphur-containing amino acids biosynthesis in P. oryzae.

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Acknowledgements

This study was supported by grants from the Ministry of Agriculture of China (2016ZX08009003-001-005), National Science and Technology Major Project (2018ZX08001-03B), and the National Natural Science Foundation of China (No. 31770154).

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Contributions

X-HL, BD, J-PL, and F-CL contributed to the study conception and design. Material preparation, data collection and analysis were performed by YL, MW, QY, Z-ZS, and Q-SL. The manuscript was written by YL, MW, BD, and X-HL. All authors read and approved the final manuscript.

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Correspondence to Xiao-Hong Liu.

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Communicated by M. Kupiec.

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294_2020_1055_MOESM1_ESM.tif

Supplementary file1 Figure S1. Sequence alignment of PoMet3 and PoMet14. The amino acid alignment of the PoMet3 of Saccharomyces cerevisiae (NP_012543.3), Fusarium graminearum (XP_011319833.1), Eremothecium gossypii (NP_986988.1), Kluyveromyces lactis (XP_454393.1), Schizosaccharomyces pombe (NP_595662.2), and Neurospora crassa (XP_964349.1) was performed using ClustalW. The amino acid alignments of the PoMet14 are S. cerevisiae (NP_012925.3), F. graminearum (XP_011317116.1), K. lactis (XP_452124.1), S. pombe (NP_594718.1), N. crassa (XP_958621.1) (TIF 6530 kb)

Supplementary file2 Figure S2. Subcellular location of PoMet3 and PoMet14. Bar = 10 μm (TIF 13247 kb)

294_2020_1055_MOESM3_ESM.tif

Supplementary file3 Figure S3. Growth of M. oryzae mutants on selected sulfur sources. Growth of the strains on MM supplemented with 1 mM selected sulfur sources for 8 days (TIF 8208 kb)

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Li, Y., Wu, M., Yu, Q. et al. PoMet3 and PoMet14 associated with sulfate assimilation are essential for conidiogenesis and pathogenicity in Pyricularia oryzae. Curr Genet 66, 765–774 (2020). https://doi.org/10.1007/s00294-020-01055-1

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  • DOI: https://doi.org/10.1007/s00294-020-01055-1

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