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Analysis of the FliM/FliG motor protein interaction by two-hybrid mutation suppression analysis

Department of Biological Sciences, California State University, Long Beach, Long Beach, CA 90840, USA

Correspondence
Donna L. Marykwas
dmarykwa{at}csulb.edu

The Escherichia coli motor proteins FliM and FliG physically interact, presumably to control one or more of the functions of the bacterial flagellum clockwise/counterclockwise (CW/CCW) switch. We have previously demonstrated this interaction using the yeast two-hybrid system and have identified mutations in fliG that disrupt the interaction. Starting with the most interaction-defective of these fliG mutants, we mutagenized fliM to identify suppressor mutations that restore the FliM/FliG two-hybrid interaction. Certain fliM suppressor mutations exhibit allele specificity. These mutations help define a FliG-interaction surface on FliM. Moreover, the pattern of suppression suggests that two distinct sites on FliG interact with FliM, perhaps with two FliM molecules in a dimer per molecule of FliG.

Three supplementary figures, showing fliM mutagenesis to isolate suppressors of fliG mutations disrupting FliM/FliG interaction, mapping of fliM suppressor mutations by multifragment cloning in vivo, and an E. coli FliG model, a supplementary table listing primers used in this study, and the coordinates for the modelled structures of E. coli FliG and FliM, are available with the online version of this paper.