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Significance How bacteria sense toxic chemicals and activate genes is crucial for their survival in adverse environments, including under antibacterial treatments. CusS, a membrane-localized sensor protein, and CusR, a response regulator protein, are key contributors toEscherichia coli ’s resistance to the toxic metals copper and silver, and an example of the ubiquitous two-component gene regulation systems in bacteria. Using live-cell single-molecule imaging, we discovered a substrate-sensing–induced mobilization of the sensor protein in the cell membrane, which appears to be important for subsequent interaction with the regulator protein. We determined when sensor–regulator interaction affinity switches on after sensing the metal substrate; this timing appears to facilitate the efficiency of signal transduction events and is likely generalizable for other two-component systems.

Metal-induced sensor mobilization turns on affinity to activate regulator for metal detoxification in live bacteria