Proteomic Insights into the Regulatory Role of CobQ Deacetylase in Aeromonas hydrophila

Post-translational
modifications are crucial in regulating biological
functions across both prokaryotes and eukaryotes. In Aeromonas hydrophila, CobQ, a recently identified
novel deacetylase, plays a significant role in lysine deacetylation,
influencing bacterial metabolism and stress responses. The present
study utilized quantitative proteomics to investigate the impact of cobQ deletion on the global protein expression profile in A. hydrophila. Through data-independent acquisition
mass spectrometry, we identified 233 upregulated and 41 downregulated
proteins in the cobQ deletion mutant (ΔahcobQ) strain compared to the wild-type (WT) strain. Key differentially
expressed proteins were involved in oxidative phosphorylation, bacterial
secretion, and ribosomal function. Additionally, phenotypic assays
demonstrated that the ΔahcobQ strain exhibited
an increased resistance to oxidative phosphorylation inhibitors, suggesting
a pivotal role for AhCobQ in energy metabolism. Outer membrane proteins
and efflux pumps also showed altered expression, indicating potential
implications for membrane permeability and antibiotic resistance.
These results suggested that AhCobQ plays a vital regulatory role
in maintaining metabolic homeostasis and responding to environmental
stress, highlighting its potential as a target for therapeutic interventions
against A. hydrophila infections.