Ligand binding induces an asymmetrical transmembrane signal through a receptor dimer.

Two ligand (aspartate)-binding pockets are formed at the interface between the subunits of the Tar homodimer, a bacterial chemoreceptor. Using mutant heterodimers of a hybrid receptor, Taz1, which consists of the external domain of Tar and the cytoplasmic domain of EnvZ, we disrupted either one or the other of the two ligand-binding pockets. We found that occupation of only one of the ligand-binding pockets was sufficient for induction of a transmembrane signal, and that the subunit responsible for the binding of the amino group of the ligand transduces the signal.