Reduced fungal protein acetylation mediates the antimicrobial activity of a rhizosphere bacterium against a phytopathogenic fungus

Ying-Chao Zhang, Xin Zhan, Jun-Yu Chen, Ding-Tian Yu, Tao Zhang, Huiming Zhang and Cheng-Guo Duan ()
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Ying-Chao Zhang: Chinese Academy of Sciences
Xin Zhan: Chinese Academy of Sciences
Jun-Yu Chen: Chinese Academy of Sciences
Ding-Tian Yu: Chinese Academy of Sciences
Tao Zhang: Chinese Academy of Sciences
Huiming Zhang: Chinese Academy of Sciences
Cheng-Guo Duan: Chinese Academy of Sciences

Nature Communications, 2025, vol. 16, issue 1, 1-15

Abstract: Abstract Rhizosphere microbes can protect plants from phytopathogens, but the molecular mechanisms are often poorly understood. Here, we report that a rhizosphere bacterium, Bacillus amyloliquefaciens strain TG1-2 displays antimicrobial activity against various phytopathogenic fungi and oomycetes, in a process that is mediated by the NatA acetyltransferase complex in the phytopathogenic fungus Verticillium dahliae. We show that acetylation of the molecular chaperone Hsp83 by NatA facilitates the formation of a co-chaperone complex Hsp83-Sti1-Hsp70 involved in protein quality control. Dysfunction of NatA or disruption of Hsp83 acetylation results in dissociation of the co-chaperon complex, increasing protein degradation and fungal apoptosis. Notably, TG1-2 and its major antimicrobial compound surfactin induce a reduction in Hsp83 acetylation, enhancing protein degradation and fungal apoptosis. Thus, our study provides insights into the mechanisms underlying the antimicrobial action of a rhizosphere strain against phytopathogenic fungi.

Date: 2025
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DOI: 10.1038/s41467-025-60870-7

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