Abstract
Aer, the aerotaxis receptor in Escherichia coli, is a member of a novel class of flavoproteins that act as redox sensors. The internal energy of the cell is coupled to the redox state of the electron transport system, and this status is sensed by Aer(FAD). This is a more versatile sensory response system than if E. coli sensed oxygen per se. Energy-depleting conditions that decrease electron transport also alter the redox state of the electron transport system. Aer responds by sending a signal to the flagellar motor to change direction. The output of other sensory systems that utilize redox sensors is more commonly transcriptional regulation than a behavioral response. Analysis in silico showed Aer to be part of a superfamily of PAS domain proteins that sense the intracellular environment. In Aer, FAD binds to the PAS domain. By using site-specific mutagenesis, residues critical for FAD binding and sensory transduction were identified in the PAS domain. The PAS domain appears to interact with a linker region in the C-terminus. The linker region is a member of a HAMP domain family, which has signal transduction roles in other systems.