E. coli sense and respond to a variety of chemical signals by either swimming toward, or away from them in a process known as chemotaxis.  Rationally altering the ligand-specificity of chemotaxis would open the door to engineering bacteria that can follow novel stimuli to transport loads, localize at disease sites, or degrade environmental pollutants.  While using protein engineering to alter the ligand specificities of chemoreceptors is possible, structural constraints enforced by the protein scaffolds and the potential for crosstalk between receptors with overlapping ligand specificities present several challenges.  To overcome these challenges, we used a synthetic riboswitch to activate the translation of a key protein in the chemotaxis pathway in a ligand-dependent fashion.  We will show that these engineered cells migrate toward a new ligand, and recapitulate many of the chemotactic behaviors of natural E. coli, including the ability to sense and respond to chemical gradients.