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PMID: 8491729 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Genetic and biochemical analysis of Salmonella typhimurium FliI, a flagellar protein related to the catalytic subunit of the F0F1 ATPase and to virulence proteins of mammalian and plant pathogens.

Journal of bacteriology ·Vol. 175 ·No. 10 ·1993-05-00 ·Pages 3131-8

Dreyfus G, Williams AW, Kawagishi I, Macnab RM

Abstract

FliI is a Salmonella typhimurium protein that is needed for flagellar assembly and may be involved in a specialized protein export pathway that proceeds without signal peptide cleavage. FliI shows extensive sequence similarity to the catalytic beta subunit of the F0F1 ATPase (A. P. Volger, M. Homma, V. M. Irikura, and R. M. Macnab, J. Bacteriol. 173:3564-3572, 1991). It is even more similar to the Spa47 protein of Shigella flexneri (M. M. Venkatesan, J. M. Buysse, and E. V. Oaks, J. Bacteriol. 174:1990-2001, 1992) and the HrpB6 protein of Xanthomonas campestris (S. Fenselau, I. Balbo, and U. Bonas, Mol. Plant-Microbe Interact. 5:390-396, 1992), which are believed to play a role in the export of virulence proteins. Site-directed mutagenesis of residues in FliI that correspond to catalytically important residues in the F1 beta subunit resulted in loss of flagellation, supporting the hypothesis that FliI is an ATPase. FliI was overproduced and purified almost to homogeneity. It demonstrated ATP binding but not hydrolysis. An antibody raised against FliI permitted detection of the protein in wild-type cells and an estimate of about 1,500 subunits per cell. An antibody directed against the F1 beta subunit of Escherichia coli cross-reacted with FliI, confirming that the proteins are structurally related. The relationship between three proteins involved in flagellar assembly (FliI, FlhA, and FliP) and homologs in a variety of virulence systems is discussed.

MeSH Terms
Adenosine Triphosphate/metabolism Bacteria/pathogenicity Bacterial Proteins/genetics,immunology,metabolism Base Sequence Cross Reactions Flagella/physiology Genetic Complementation Test Molecular Sequence Data Multigene Family/genetics Mutagenesis, Site-Directed Plant Diseases Proteins Proton-Translocating ATPases/genetics,immunology,metabolism Recombinant Proteins/immunology,metabolism Salmonella typhimurium/genetics,pathogenicity Virulence Virulence Factors
Chemicals
Bacterial Proteins Proteins Recombinant Proteins Virulence Factors fliI protein, bacteria Adenosine Triphosphate Proton-Translocating ATPases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Dreyfus G
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511-8148.
Williams A W
Kawagishi I
Macnab R M
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.175.10.3131-3138.1993
Published
1993-05-00
Pages
3131-8
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC204635
Subset
IM
Grants
NIAID NIH HHS · AI12202 · United States
External Links
PubMed source DOI: 10.1128/jb.175.10.3131-3138.1993 PMC Full Text View journal details
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