Proteomic Insights into the Regulatory Role of CobQ\nDeacetylase in Aeromonas hydrophila

Post-translational\nmodifications are crucial in regulating biological\nfunctions across both prokaryotes and eukaryotes. In Aeromonas hydrophila, CobQ, a recently identified\nnovel deacetylase, plays a significant role in lysine deacetylation,\ninfluencing bacterial metabolism and stress responses. The present\nstudy utilized quantitative proteomics to investigate the impact of <i>cobQ</i> deletion on the global protein expression profile in A. hydrophila. Through data-independent acquisition\nmass spectrometry, we identified 233 upregulated and 41 downregulated\nproteins in the <i>cobQ</i> deletion mutant (<i>ΔahcobQ</i>) strain compared to the wild-type (WT) strain. Key differentially\nexpressed proteins were involved in oxidative phosphorylation, bacterial\nsecretion, and ribosomal function. Additionally, phenotypic assays\ndemonstrated that the <i>ΔahcobQ</i> strain exhibited\nan increased resistance to oxidative phosphorylation inhibitors, suggesting\na pivotal role for AhCobQ in energy metabolism. Outer membrane proteins\nand efflux pumps also showed altered expression, indicating potential\nimplications for membrane permeability and antibiotic resistance.\nThese results suggested that AhCobQ plays a vital regulatory role\nin maintaining metabolic homeostasis and responding to environmental\nstress, highlighting its potential as a target for therapeutic interventions\nagainst A. hydrophila infections.