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Journal of Bacteriology, March 2005, p. 1695-1701, Vol. 187, No. 5
0021-9193/05/$08.00+0     doi:10.1128/JB.187.5.1695-1701.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

A Chimeric N-Terminal Escherichia coli-C-Terminal Rhodobacter sphaeroides FliG Rotor Protein Supports Bidirectional E. coli Flagellar Rotation and Chemotaxis

Karen A. Morehouse,1 Ian G. Goodfellow,2 and R. Elizabeth Sockett1*

Institute of Genetics, School of Biology, University of Nottingham Medical School, Queen's Medical Center, Nottingham,1 School of Animal and Microbial Sciences, University of Reading, Whiteknights, Reading, United Kingdom2

Received 24 September 2004/ Accepted 17 November 2004

Flagellate bacteria such as Escherichia coli and Salmonella enterica serovar Typhimurium typically express 5 to 12 flagellar filaments over their cell surface that rotate in clockwise (CW) and counterclockwise directions. These bacteria modulate their swimming direction towards favorable environments by biasing the direction of flagellar rotation in response to various stimuli. In contrast, Rhodobacter sphaeroides expresses a single subpolar flagellum that rotates only CW and responds tactically by a series of biased stops and starts. Rotor protein FliG transiently links the MotAB stators to the rotor, to power rotation and also has an essential function in flagellar export. In this study, we sought to determine whether the FliG protein confers directionality on flagellar motors by testing the functional properties of R. sphaeroides FliG and a chimeric FliG protein, EcRsFliG (N-terminal and central domains of E. coli FliG fused to an R. sphaeroides FliG C terminus), in an E. coli FliG null background. The EcRsFliG chimera supported flagellar synthesis and bidirectional rotation; bacteria swam and tumbled in a manner qualitatively similar to that of the wild type and showed chemotaxis to amino acids. Thus, the FliG C terminus alone does not confer the unidirectional stop-start character of the R. sphaeroides flagellar motor, and its conformation continues to support tactic, switch-protein interactions in a bidirectional motor, despite its evolutionary history in a bacterium with a unidirectional motor.

* Corresponding author. Mailing address: Institute of Genetics, School of Biology, University of Nottingham, Medical School, QMC, Nottingham NG7 2UH, United Kingdom. Phone: 44 115 919 4496. Fax: 44 115 970 9906. E-mail: liz.sockett{at}nottingham.ac.uk.

Journal of Bacteriology, March 2005, p. 1695-1701, Vol. 187, No. 5
0021-9193/05/$08.00+0     doi:10.1128/JB.187.5.1695-1701.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Wand, M. E., Sockett, R. E., Evans, K. J., Doherty, N., Sharp, P. M., Hardie, K. R., Winzer, K. (2006). Helicobacter pylori FlhB Function: the FlhB C-Terminal Homologue HP1575 Acts as a "Spare Part" To Permit Flagellar Export When the HP0770 FlhBCC Domain Is Deleted.. J. Bacteriol. 188: 7531-7541 [Abstract] [Full Text]  


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