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Journal of Bacteriology, February 2002, p. 771-776, Vol. 184, No. 3
0021-9193/01/$04.00+0 DOI: 10.1128/JB.184.3.771-776.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114,1 Department of Biology, College of Wooster, Wooster, Ohio 446912
Received 8 August 2001/ Accepted 2 November 2001
Flagellar assembly requires the expression of a large number of flagellum-specific genes. However, mutations in a number of other genes in Salmonella and Escherichia coli have been shown to have pleiotropic effects that affect flagellar assembly. FlgH (the L-ring subunit of the flagellar basal body) is a lipoprotein whose modification is important for L-ring assembly. We therefore tested whether the lack of motility of Salmonella mutants defective in lipoprotein biogenesis is a result of inability to modify FlgH. Our results show that temperature-sensitive apolipoprotein N-acyltransferase [lnt(Ts)] mutants are nonflagellate at 42°C. However, the flagellar assembly defect occurs at a much earlier step in the pathway than L-ring assembly. These mutants failed to assemble even an MS ring, presumably because of the observed decrease in transcription of fliF. In contrast, temperature-sensitive diacylglycerol transferase [lgt(Ts)] mutants were motile at 42°C, provided the strains carried an lpp (Braun lipoprotein) mutation to permit growth. We have isolated second-site mutants from an lgt(Ts) lpp+ strain that grow but are nonflagellate at 42°C. Thus, lipoprotein biogenesis is a factor that is important for flagellar assembly.
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