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Journal of Bacteriology, December 2009, p. 7147-7156, Vol. 191, No. 23
0021-9193/09/$08.00+0     doi:10.1128/JB.00749-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Functional Analysis of the Helicobacter pylori Flagellar Switch Proteins {triangledown} ,§

Andrew C. Lowenthal,1,2,{dagger} Marla Hill,1,{dagger} Laura K. Sycuro,3,4 Khalid Mehmood,1,5 Nina R. Salama,3 and Karen M. Ottemann1*

Department of Microbiology and Environmental Toxicology, University of California, Santa Cruz, Santa Cruz, California 95064,1 Department of Molecular, Cell & Developmental Biology, University of California, Santa Cruz, Santa Cruz, California 95064,2 Division of Human Biology, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109,3 Molecular and Cellular Biology Graduate Program, University of Washington, Seattle, Washington 98195,4 Department of Microbiology, Quaid-i-Azam University, Islamabad 45320, Pakistan5

Received 10 June 2009/ Accepted 11 September 2009

Helicobacter pylori uses flagellum-mediated chemotaxis to promote infection. Bacterial flagella change rotational direction by changing the state of the flagellar motor via a subcomplex referred to as the switch. Intriguingly, the H. pylori genome encodes four switch complex proteins, FliM, FliN, FliY, and FliG, instead of the more typical three of Escherichia coli or Bacillus subtilis. Our goal was to examine whether and how all four switch proteins participate in flagellation. Previous work determined that FliG was required for flagellation, and we extend those findings to show that all four switch proteins are necessary for normal numbers of flagellated cells. Furthermore, while fliY and fliN are partially redundant with each other, both are needed for wild-type levels of flagellation. We also report the isolation of an H. pylori strain containing an R54C substitution in fliM, resulting in bacteria that swim constantly and do not change direction. Along with data demonstrating that CheY-phosphate interacts with FliM, these findings suggest that FliM functions in H. pylori much as it does in other organisms.

* Corresponding author. Mailing address: Department of Microbiology and Environmental Toxicology, University of California, Santa Cruz, Santa Cruz, CA 95064. Phone: (831) 459-3482. Fax: (831) 459-3524. E-mail: ottemann{at}ucsc.edu

{triangledown} Published ahead of print on 18 September 2009.

§ Supplemental material for this article may be found at http://jb.asm.org/.

{dagger} These authors contributed equally to this work.

Journal of Bacteriology, December 2009, p. 7147-7156, Vol. 191, No. 23
0021-9193/09/$08.00+0     doi:10.1128/JB.00749-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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