Abstract
Thermotaxis in Escherichia coli as a model system for studying thermosensing mechanisms. All the components involved in the signal transduction circuit have been indentified. Thermosensors are the transmembrane proteins that were originally indentified as chemoreceptors. They regulate the activity of the cytoplasmic histidine kinase CheA. Recent studies revealed some unique and unexpected features of these "thermometer proteins", including effects of receptor covalent modification on thermosensing properties, and uncoupling of intra- and extracellular domains under some conditions. Investigation of thermosensing properties of the sensors should also be required for understanding their chemosensing mechanisms.
