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Journal of Bacteriology, July 2003, p. 3983-3988, Vol. 185, No. 13
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.13.3983-3988.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

The ATPase FliI Can Interact with the Type III Flagellar Protein Export Apparatus in the Absence of Its Regulator, FliH

Tohru Minamino,1,2 Bertha González-Pedrajo,3 May Kihara,3 Keiichi Namba,1,2,4 and Robert M. Macnab3*

Protonic NanoMachine Project, ERATO,1 Dynamic NanoMachine Project, ICORP, JST,2 Graduate School of Frontier Biosciences, Osaka University, Seika, Kyoto 619-0237, Japan,4 Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, 06520-81143

Received 5 February 2003/ Accepted 21 April 2003

Salmonella FliI is the ATPase that drives flagellar protein export. It normally exists as a complex together with the regulatory protein FliH. A fliH null mutant was slightly motile, with overproduction of FliI resulting in substantial improvement of its motility. Mutations in the cytoplasmic domains of FlhA and FlhB, which are integral membrane components of the type III flagellar export apparatus, also resulted in substantially improved motility, even at normal FliI levels. Thus, FliH, though undoubtedly important, is not essential.


* Corresponding author. Mailing address: Yale University, Department of Molecular Biophysics and Biochemistry 0734, 266 Whitney Ave., P.O. Box 208114, New Haven, CT 06520-8114. Phone: (203) 432-5590. Fax: (203) 432-9782. E-mail: robert.macnab{at}yale.edu.


Journal of Bacteriology, July 2003, p. 3983-3988, Vol. 185, No. 13
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.13.3983-3988.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.




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