RESUMO
Chemoreceptors are dimeric proteins that contain a periplasmic or extracellular domain for ligand binding and an extremely well-conserved cytoplasmic domain for output response control. This latter domain consists in a long α-helical hairpin that forms a four-helix coiled-coil bundle in the dimer. Dimers associate into trimers of dimers in the crystal structure obtained for the cytoplasmic domain of the Escherichia coli serine chemoreceptor, Tsr. Further studies confirmed that this crystal structure reflects the basic unit within the in vivo organization of chemoreceptors. The trimers of dimers form large and stable chemoreceptor clusters in all the prokaryotes that have been studied. Here, we describe the use of TMEA, a trifunctional cross-linker that reacts with sulfhydryl groups, as a tool to study the geometry and dynamics of the interaction between receptors of the same or different types in living cells.