To survive, evade immune responses, and replicate within a eukaryotic host, pathogenic and symbiotic bacteria must be able to modulate the responses of the host. For many species of Gram-negative bacteria that live in close association with eukaryotes, the ability of the bacteria to manipulate the host is dependent upon the function of a bacterial nanomachine called the Type III Secretion System (T3SS). This syringe-like macromolecular protein structure, called the "needle complex," spans the bacterial envelope and has a needle-like extension that protrudes from the bacterial surface and interacts with the host cell membrane. A narrow channel traverses the needle complex and allows for proteins to pass from the bacterial cytoplasm directly to the host cell cytoplasm. There, they function to create an environment suitable for bacterial survival and replication. These proteins, called "effectors," are often precisely targeted to the T35 machine by specialized proteins called "chaperones." Using Salmonella enterica serovar Typhimurium as a model system, I have identified mechanisms that coordinate the expression of the T3S chaperone SicP and its cognate effector SptP. I have found that expression of sicP is required for wild type levels of sptP translation. Translation of the effector is coupled to translation of its chaperone, and in the absence of translational coupling, an inhibitory RNA structure prevents translation of sptP, which I have identified and characterized. Furthermore, I have found that translational coupling is essential for the efficient secretion of SptP through the T3SS, which likely reflects a defect in SicP/SptP complex assembly when the synthesis of the two proteins is not suitably coordinated. The data presented here not only illuminate an important aspect of T3SS biology, but they also show how the genomic organization of functionally related proteins can have a significant impact on protein function.