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J. Biol. Chem., Vol. 281, Issue 1, 508-517, January 6, 2006

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Molecular Basis of the Interaction between the Flagellar Export Proteins FliI and FliH from Helicobacter pylori^*

Michael C. Lane1, Paul W. O'Toole, and Stanley A. Moore¶2

From the ^¶Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan S7N 5E5, Canada, the Department of Microbiology and Alimentary Pharmabiotic Centre, University College Cork, Western Road, Cork, Ireland, and Institute of Molecular Biosciences, Massey University, Palmerston North, New Zealand

Bacterial flagellar protein export requires an ATPase, FliI, and presumptive inhibitor, FliH. We have explored the molecular basis for FliI/FliH interaction in the human gastric pathogen Helicobacter pylori. By using bioinformatic and biochemical analyses, we showed that residues 1–18 of FliI very likely form an amphipathic -helix upon interaction with FliH, and that residues 21–91 of FliI resemble the N-terminal oligomerization domain of the F₁-ATPase catalytic subunits. A truncated FliI-(2–91) protein was shown to be folded, although the N-terminal 18 residues were likely unstructured. Deletion and scanning mutagenesis showed that residues 1–18 of FliI were essential for the FliI/FliH interaction. Scanning mutation of amino acids in the N-terminal 10 residues of FliI indicated that a cluster of hydrophobic residues in this segment was critical for the interaction with FliH. The interaction between FliI and FliH has similarities to the interaction between the N-terminal -helix of the F₁-ATPase -subunit and the globular domain of the F₁-ATPase -subunit, respectively. This similarity suggests that FliH may function as a molecular stator.

Received for publication, July 5, 2005 , and in revised form, October 26, 2005.

^* This work was supported in part by an establishment grant (to S. A. M.) from the Saskatchewan Heath Research Foundation and a discovery grant from the National Sciences and Engineering Research Council of Canada. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains Fig. S1 and Table S1.

¹ Recipient of a Massey University doctoral scholarship.

² To whom correspondence should be addressed: Dept. of Biochemistry, University of Saskatchewan, 107 Wiggins Rd., Saskatoon, Saskatchewan S7N 5E5, Canada. Tel.: 306-966-4381; Fax: 306-966-4390; E-mail: stan.moore{at}usask.ca.

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