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Journal of Biochemistry Advance Access originally published online on July 15, 2009
Journal of Biochemistry 2009 146(5):643-650; doi:10.1093/jb/mvp109
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© The Authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved

Mutational Analysis of the GTP-binding Motif of FlhF which Regulates the Number and Placement of the Polar Flagellum in Vibrio alginolyticus

Akiko Kusumoto*, Noriko Nishioka, Seiji Kojima and Michio Homma{dagger}

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

{dagger}To whom correspondence should be addressed. Tel: +81-52-789-2991, Fax: +81-52-789-3001, E-mail: g44416a{at}cc.nagoya-u.ac.jp

Received April 16, 2009; Accepted June 29, 2009


  Abstract

Precise regulation of the number and placement of flagella is critical for the mono-flagellated bacterium Vibrio alginolyticus to swim efficiently. We previously proposed a model in which the putative GTPase FlhF determines the polar location and generation of the flagellum, the putative ATPase FlhG interacts with FlhF to prevent FlhF from localizing to the pole, and thus FlhG negatively regulates the flagellar number in V. alginolyticus cells. To investigate the role of the GTP-binding motif of FlhF, we generated a series of alanine-replacement mutations at the positions that are highly conserved among homologous proteins. The results indicate that there is a correlation between the polar localization and the ability to produce flagella in the mutants. We investigated whether the mutations in the GTP-binding motif affected the ability to interact with FlhG. In contrast to our prediction, no significant difference was detected in the interaction with FlhG between the wild-type and mutant FlhFs. We showed that the GTP-binding motif of FlhF is important for polar localization of the flagellum but not for the interaction with FlhG.

Key Words: bacterial flagella, GTP-binding motif, polar flagellum

Abbreviations: SRP, signal recognition particle; EGFP, enhanced green fluorescent protein; Pof, polar flagellum; Laf, lateral flagella

*Present address: Research Center for Animal Hygiene and Food Safety, Obihiro University of Agriculture and Veterinary Medicine, Inada-cho, Obihiro, Hokkaido 080-8555, Japan.


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