Functional Identification of AcsR, a MarR Family Transcriptional Regulator Involved in the Regulation of Aromatic Compound-Degrading Genes in Corynebacterium glutamicum

The MarR (multiple antibiotic resistance regulator) family regulators, which are widely conserved across various organisms, play pivotal roles in metabolism, stress response mechanisms, and virulence factor production. However, the regulatory functions of these factors in the degradation of aromatic compounds within Corynebacterium glutamicum remain largely uncharacterized. In this study, we identified a MarR-type regulator, designated AcsR (encoded by ncgl2425), which directly represses the expression of the catechol 2,3-dioxygenase gene ncgl2007 (c23o) and the heavy metal (nickel) transport system permease gene ncgl2351, while activating the expression of ncgl2258 encoding an ABC-type C4-dicarboxylate-binding periplasmic protein. AcsR binds specifically as a dimer to a 6 bp inverted repeat sequence, and this binding is disrupted by catechol in vitro. Correspondingly, catechol induces the expression of c23o in vivo. Phenotypic analysis revealed that the ΔacsR mutant exhibited enhanced resistance to multiple aromatic compounds but increased sensitivity to antibiotics, heavy metals, and oxidants. Collectively, these findings demonstrate that AcsR is an important regulator of stress adaptation in C. glutamicum and provide new insights into the regulatory mechanisms of aromatic compound degradation in this industrially important bacterium.