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(Received for publication, August 6, 1996, and in revised form, September 27, 1996)
From the Department of Molecular Biophysics and Biochemistry, Yale
University, New Haven, Connecticut 06520-8114
FliI is a protein needed for flagellar assembly
in Salmonella typhimurium. It shows sequence similarity to
the catalytic
Volume 271, Number 50,
Issue of December 13, 1996
pp. 31981-31988
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
AN ATPase INVOLVED IN FLAGELLAR ASSEMBLY IN SALMONELLA
TYPHIMURIUM
subunit of the F0F1-ATPase
and is even more closely related to putative ATPases in Type III
bacterial secretory pathways. A His-tagged version of FliI, which was
fully functional in complementation tests, was purified to homogeneity.
It had an ATPase activity of 0.16 s
1 at 25 °C and pH
7, and a Km for ATP of 0.3 mM;
Mg2+ was required. The activity was not affected by
inhibitors of the F-, V- or P-type ATPases, or inhibitors of the Type I
or Type II bacterial secretory pathways. Mutations K188I and Y363S
decreased the ATPase activity about 100-fold, increased the
Km about 10-fold, blocked flagellar assembly, and
were dominant. Other FliI mutations that disrupted flagellar protein
export were found near the N terminus; they permitted essentially
wild-type ATPase activity, were not dominant, and showed a
dosage-dependent phenotype. We propose that FliI has a
C-terminal ATPase domain and an N-terminal domain that interacts with
other components in the flagellum-specific export apparatus.
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