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

Authors
  • Passmore, Steven E
  • Meas, Rithy
  • Marykwas, Donna L
Type
Published Article
Journal
Microbiology (Reading, England)
Publication Date
Mar 01, 2008
Volume
154
Issue
Pt 3
Pages
714–724
Identifiers
DOI: 10.1099/mic.0.2007/014597-0
PMID: 18310018
Source
Medline
License
Unknown

Abstract

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.

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