Many bacteria make use of a set of dedicated chemoreceptor proteins to control a His-Asp signaling system; this control converts environmental sensory information into instructions that regulate flagellar rotation, enabling chemotaxis. This thesis summarizes my investigations of some of the chemotaxis signaling proteins in Bacillus subtilis, particularly coupling proteins CheW and CheV. Proteins CheA, CheW, CheV, CheY, and FliM were each expressed in B. subtilis as translational fusions with either YFP or CFP. These fusion proteins were then shown to fluoresce in living bacterial cells. Motility experiments were conducted to compare the function of these fusion proteins to their wild type counterparts. This thesis proposes a series of experiments that would use these fluorescent fusion proteins to further explore the idea that these chemotaxis proteins change position when B. subtilis encounters chemostimuli.