Roles of N‐terminal acetyltransferase complex in phytopathogenic fungi: Promoting diseases with different mechanisms

Abstract N‐terminal acetyltransferase (Nat) complexes are key mediators of protein acetylation and play pivotal roles in various biological processes across diverse organisms. However, their functions in phytopathogenic fungi have not been well established. A recent study revealed that the pathogenic fungus Verticillium dahliae uses the NatA complex to stabilize its proteome and defend against the biocontrol bacterium Bacillus amyloliquefaciens strain TG1‐2, as well as its major antimicrobial compound, surfactin. NatA complex‐mediated acetylation of VdHsp83 facilitates its assembly with VdSti1 and VdHsp70, forming the VdHsp83‐VdSti1‐VdHsp70 chaperone complex that maintains proper protein folding to promote disease. Conversely, B. amyloliquefaciens TG1‐2 inhibits VdHsp83 acetylation, destabilizing the VdHsp83‐VdSti1‐VdHsp70 complex, which leads to protein misfolding, degradation, and apoptosis, ultimately impairing V. dahliae viability. These findings underscore the critical roles of NatA complex‐mediated protein acetylation in the battle between pathogenic fungi and biocontrol bacteria. Together with its regulatory function in pathogenicity, this study unveils different mechanisms employed by the NatA complex in promoting diseases and highlights the potential of targeting NatA complexes as effective strategies for plant disease management.