This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Obara, M.
Right arrow Articles by Homma, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Obara, M.
Right arrow Articles by Homma, M.

 Previous Article  |  Next Article 

Journal of Bacteriology, May 2008, p. 3565-3571, Vol. 190, No. 10
0021-9193/08/$08.00+0     doi:10.1128/JB.00849-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Roles of Charged Residues in the C-Terminal Region of PomA, a Stator Component of the Na+-Driven Flagellar Motor{triangledown}

Madoka Obara, Toshiharu Yakushi,{dagger} Seiji Kojima, and Michio Homma*

Division of Biological Science, Graduate School of Science, Nagoya University, Furo-Cho, Chikusa-Ku, Nagoya 464-8602, Japan

Received 1 June 2007/ Accepted 22 February 2008

Bacterial flagellar motors use specific ion gradients to drive their rotation. It has been suggested that the electrostatic interactions between charged residues of the stator and rotor proteins are important for rotation in Escherichia coli. Mutational studies have indicated that the Na+-driven motor of Vibrio alginolyticus may incorporate interactions similar to those of the E. coli motor, but the other electrostatic interactions between the rotor and stator proteins may occur in the Na+-driven motor. Thus, we investigated the C-terminal charged residues of the stator protein, PomA, in the Na+-driven motor. Three of eight charge-reversing mutations, PomA(K203E), PomA(R215E), and PomA(D220K), did not confer motility either with the motor of V. alginolyticus or with the Na+-driven chimeric motor of E. coli. Overproduction of the R215E and D220K mutant proteins but not overproduction of the K203E mutant protein impaired the motility of wild-type V. alginolyticus. The R207E mutant conferred motility with the motor of V. alginolyticus but not with the chimeric motor of E. coli. The motility with the E211K and R232E mutants was similar to that with wild-type PomA in V. alginolyticus but was greatly reduced in E. coli. Suppressor analysis suggested that R215 may participate in PomA-PomA interactions or PomA intramolecular interactions to form the stator complex.

* Corresponding author. Mailing address: Division of Biological Science, Graduate School of Science, Nagoya University, Furo-Cho, Chikusa-Ku, Nagoya 464-8602, Japan. Phone: 81-52-789-2991. Fax: 81-52-789-3001. E-mail: g44416a{at}cc.nagoya-u.ac.jp

{triangledown} Published ahead of print on 7 March 2008.

{dagger} Present address: Applied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University, Yamaguchi 753-8515, Japan.

Journal of Bacteriology, May 2008, p. 3565-3571, Vol. 190, No. 10
0021-9193/08/$08.00+0     doi:10.1128/JB.00849-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Wilhelms, M., Vilches, S., Molero, R., Shaw, J. G., Tomas, J. M., Merino, S. (2009). Two Redundant Sodium-Driven Stator Motor Proteins Are Involved in Aeromonas hydrophila Polar Flagellum Rotation. J. Bacteriol. 191: 2206-2217 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»