Direct monitoring of interaction between Escherichia coli proteins, MinC and monomeric FtsZ, in solution.

MinC plays an important role in regulation of the cell division site in Escherichia coli. Previous studies using sedimentation and electron microscopic methods suggested that MinC interacts with the FtsZ polymer and inhibits further FtsZ polymerization. However, it is difficult to clarify details regarding specific molecular interactions by such static analytic methods. In this study, a fluorescence resonance energy transfer (FRET) method was developed to directly observe the interaction between Cy3-labeled MinC and Cy5-labeled FtsZ in solution. FRET analysis indicated that MinC interacts with monomeric rather than polymeric FtsZ in solution. This suggests that interactions between monomeric FtsZ and MinC are important for controlling of FtsZ polymerization by MinC.