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Journal of Bacteriology, February 2006, p. 1466-1472, Vol. 188, No. 4
0021-9193/06/$08.00+0     doi:10.1128/JB.188.4.1466-1472.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Roles of Charged Residues of Rotor and Stator in Flagellar Rotation: Comparative Study using H+-Driven and Na+-Driven Motors in Escherichia coli

Toshiharu Yakushi,1 Junghoon Yang,2 Hajime Fukuoka,1 Michio Homma,1* and David F. Blair2*

Graduate School of Biological Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan,1 Department of Biology, University of Utah, Salt Lake City, Utah 841122

Received 15 September 2005/ Accepted 23 November 2005

In Escherichia coli, rotation of the flagellar motor has been shown to depend upon electrostatic interactions between charged residues of the stator protein MotA and the rotor protein FliG. These charged residues are conserved in the Na+-driven polar flagellum of Vibrio alginolyticus, but mutational studies in V. alginolyticus suggested that they are relatively unimportant for motor rotation. The electrostatic interactions detected in E. coli therefore might not be a general feature of flagellar motors, or, alternatively, the V. alginolyticus motor might rely on similar interactions but incorporate additional features that make it more robust against mutation. Here, we have carried out a comparative study of chimeric motors that were resident in E. coli but engineered to use V. alginolyticus stator components, rotor components, or both. Charged residues in the V. alginolyticus rotor and stator proteins were found to be essential for motor rotation when the proteins functioned in the setting of the E. coli motor. Patterns of synergism and suppression in rotor/stator double mutants indicate that the V. alginolyticus proteins interact in essentially the same way as their counterparts in E. coli. The robustness of the rotor-stator interface in V. alginolyticus is in part due to the presence of additional charged residues in PomA but appears mainly due to other factors, because an E. coli motor using both rotor and stator components from V. alginolyticus remained sensitive to mutation. Motor function in V. alginolyticus may be enhanced by the proteins MotX and MotY.

* Corresponding author. Mailing address for Michio Homma: Graduate School of Biological Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan. Phone: 81 52 789 2991. Fax: 81 52 789 3001. E-mail: g44416{at}nucc.cc.nagoya-u.ac.jp. Mailing address for David F. Blair: Department of Biology, University of Utah, Salt Lake City, UT 84112. Phone: (801) 585-3709. Fax: (801) 581-4668. E-mail: blair{at}bioscience.utah.edu.

Journal of Bacteriology, February 2006, p. 1466-1472, Vol. 188, No. 4
0021-9193/06/$08.00+0     doi:10.1128/JB.188.4.1466-1472.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Terashima, H., Abe-Yoshizumi, R., Kojima, S., Homma, M. (2008). Cell-free Synthesis of the Torque-Generating Membrane Proteins, PomA and PomB, of the Na+-driven Flagellar Motor in Vibrio alginolyticus. J Biochem 144: 635-642 [Abstract] [Full Text]  
  • Obara, M., Yakushi, T., Kojima, S., Homma, M. (2008). Roles of Charged Residues in the C-Terminal Region of PomA, a Stator Component of the Na+-Driven Flagellar Motor. J. Bacteriol. 190: 3565-3571 [Abstract] [Full Text]  
  • de Kerchove, A. J., Elimelech, M. (2007). Impact of Alginate Conditioning Film on Deposition Kinetics of Motile and Nonmotile Pseudomonas aeruginosa Strains. Appl. Environ. Microbiol. 73: 5227-5234 [Abstract] [Full Text]  
  • Mashimo, T., Hashimoto, M., Yamaguchi, S., Aizawa, S.-I. (2007). Temperature-Hypersensitive Sites of the Flagellar Switch Component FliG in Salmonella enterica Serovar Typhimurium. J. Bacteriol. 189: 5153-5160 [Abstract] [Full Text]  
  • Brown, P. N., Terrazas, M., Paul, K., Blair, D. F. (2007). Mutational Analysis of the Flagellar Protein FliG: Sites of Interaction with FliM and Implications for Organization of the Switch Complex. J. Bacteriol. 189: 305-312 [Abstract] [Full Text]  


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