Article
- The EMBO Journal (2008) 27, 1134 - 1144
- doi:10.1038/emboj.2008.48
Published online: 13 March 2008
Subject Categories:
The bacterial flagellar switch complex is getting more complex
Galit N Cohen-Ben-Lulu1, Noreen R Francis2, Eyal Shimoni3, Dror Noy4, Yaacov Davidov1, Krishna Prasad1, Yael Sagi1, Gary Cecchini5,6, Rose M Johnstone7 and Michael Eisenbach1
- Department of Biological Chemistry, The Weizmann Institute of Science, Rehovot, Israel
- Department of Biology, Brandeis University, Waltham, MA, USA
- Electron Microscopy Unit, The Weizmann Institute of Science, Rehovot, Israel
- Department of Plant Sciences, The Weizmann Institute of Science, Rehovot, Israel
- Molecular Biology, VA Medical Center, San Francisco, CA, USA
- Department of Biochemistry and Biophysics, University of California, San Francisco, CA, USA
- Department of Biochemistry, McGill University, Montreal, Quebec, Canada
Correspondence to:
Michael Eisenbach, Department of Biological Chemistry, The Weizmann Institute of Science, POB 26, 76100 Rehovot, Israel. Tel.: +972 8 934 3923; Fax: +972 8 947 2722; E-mail: m.eisenbach@weizmann.ac.il
Received 16 October 2007; Accepted 25 February 2008
Abstract
The mechanism of function of the bacterial flagellar switch, which determines the direction of flagellar rotation and is essential for chemotaxis, has remained an enigma for many years. Here we show that the switch complex associates with the membrane-bound respiratory protein fumarate reductase (FRD). We provide evidence that FRD binds to preparations of isolated switch complexes, forms a 1:1 complex with the switch protein FliG, and that this interaction is required for both flagellar assembly and switching the direction of flagellar rotation. We further show that fumarate, known to be a clockwise/switch factor, affects the direction of flagellar rotation through FRD. These results not only uncover a new component important for switching and flagellar assembly, but they also reveal that FRD, an enzyme known to be primarily expressed and functional under anaerobic conditions in Escherichia coli, nonetheless, has important, unexpected functions under aerobic conditions.
Keywords:
- bacterial chemotaxis,
- bacterial motility,
- flagellar assembly,
- FliG,
- fumarate reductase
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