Sirt5‐mediated lysine desuccinylation regulates oxidative stress adaptation in Magnaporthe oryzae during host intracellular infection

0301 basic medicine 03 medical and health sciences
DOI: 10.1111/nph.19683 Publication Date: 2024-03-14T07:37:10Z
ABSTRACT
Summary Plant pathogenic fungi elaborate numerous detoxification strategies to suppress host reactive oxygen species (ROS), but their coordination is not well‐understood. Here, we show that Sirt5‐mediated protein desuccinylation in Magnaporthe oryzae central ROS detoxification. SIRT5 encodes a desuccinylase important for virulence via adaptation oxidative stress. Quantitative proteomics analysis identified large number of succinylated proteins targeted by Sirt5, most which were mitochondrial involved phosphorylation, TCA cycle, and fatty acid oxidation. Deletion resulted hypersuccinylation detoxification‐related enzymes, significant reduction NADPH : NADP + GSH GSSG ratios, disrupting redox balance impeding invasive growth. Sirt5 desuccinylated thioredoxin Trx2 glutathione peroxidase Hyr1 activate enzyme activity, likely affecting proper folding. Altogether, this work demonstrates the importance controlling fungal process required detoxifying during M. infection.
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