The transport process of the ABC transporter superfamily is important for understanding the etiology of a number of major human diseases. One well-studied example of ABC transporters is the maltose transport complex (MTC) of Escherichia coli. This simple, well-characterized transporter is easily manipulated, and thus, serves as a good model for better understanding the assembly and interactions of ABC transporters in eukaryotic organisms. The E. coli MTC is a tetrameric complex, MalFGK2. In this study, five previously characterized MalG mutants were used to investigate changes in MalF that will suppress the Mal- phenotype of the mutants, and thus, suggest a specific protein-protein interaction. Strains carrying mutagenized MalF-encoding plasmids exhibit a Mal+ phenotype. Further tests on these candidates are underway to examine the relevant interactions between MalF and MalG.