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Journal of Bacteriology, January 2005, p. 778-784, Vol. 187, No. 2
0021-9193/05/$08.00+0     doi:10.1128/JB.187.2.778-784.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Deletion Analysis of the Carboxyl-Terminal Region of the PomB Component of the Vibrio alginolyticus Polar Flagellar Motor

Toshiharu Yakushi,* Naoko Hattori, and Michio Homma

Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa-Ku, Nagoya, Japan

Received 13 July 2004/ Accepted 11 October 2004

The stator of the sodium-driven flagellar motor of Vibrio alginolyticus is a membrane protein complex composed of four PomA and two PomB subunits. PomB has a peptidoglycan-binding motif in the C-terminal region. In this study, four kinds of PomB deletions in the C terminus were constructed. None of the deletion proteins restored motility of the {Delta}pomB strain. The PomA protein was coisolated with all of the PomB derivatives under detergent-solubilized conditions. Homotypic disulfide cross-linking of all of the deletion derivatives through naturally occurring Cys residues was detected. We conclude that the C-terminal region of PomB is essential for motor function but not for oligomerization of PomB with itself or PomA.

* Corresponding author. Mailing address: Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa-Ku, Nagoya 464-8602, Japan. Phone: 81-52-789-2992. Fax: 81-52-789-3001. E-mail: 4juji{at}cc.nagoya-u.ac.jp.

Journal of Bacteriology, January 2005, p. 778-784, Vol. 187, No. 2
0021-9193/05/$08.00+0     doi:10.1128/JB.187.2.778-784.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Kojima, S., Furukawa, Y., Matsunami, H., Minamino, T., Namba, K. (2008). Characterization of the Periplasmic Domain of MotB and Implications for Its Role in the Stator Assembly of the Bacterial Flagellar Motor. J. Bacteriol. 190: 3314-3322 [Abstract] [Full Text]  


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