1887

Abstract

The 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 that disrupt the interaction. Starting with the most interaction-defective of these mutants, we mutagenized to identify suppressor mutations that restore the FliM/FliG two-hybrid interaction. Certain 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.

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2008-03-01
2024-04-28
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