This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hirano, T.
Right arrow Articles by Macnab, R. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hirano, T.
Right arrow Articles by Macnab, R. M.

 Previous Article  |  Next Article 

Journal of Bacteriology, April 2003, p. 2485-2492, Vol. 185, No. 8
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.8.2485-2492.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Substrate Specificity Classes and the Recognition Signal for Salmonella Type III Flagellar Export

Takanori Hirano,1,{dagger} Tohru Minamino,2 Keiichi Namba,2,3 and Robert M. Macnab1*

Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114,1 Protonic NanoMachine Project, ERATO, JST, Seika, Kyoto 619-0237,2 Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka 565-0871, Japan3

Received 24 October 2002/ Accepted 31 January 2003

Most flagellar proteins of Salmonella are exported to their assembly destination via a specialized apparatus. This apparatus is a member of the type III superfamily, which is widely used for secretion of virulence factors by pathogenic bacteria. Extensive studies have been carried out on the export of several of the flagellar proteins, most notably the hook protein (FlgE), the hook-capping protein (FlgD), and the filament protein flagellin (FliC). This has led to the concept of two export specificity classes, the rod/hook type and the filament type. However, little direct experimental evidence has been available on the export properties of the basal-body rod proteins (FlgB, FlgC, FlgF, and FlgG), the putative MS ring-rod junction protein (FliE), or the muramidase and putative rod-capping protein (FlgJ). In this study, we have measured the amounts of these proteins exported before and after hook completion. Their amounts in the culture supernatant from a flgE mutant (which is still at the hook-type specificity stage) were much higher than those from a flgK mutant (which has advanced to the filament-type specificity stage), placing them in the same class as the hook-type proteins. Overproduction of FliE, FlgB, FlgC, FlgF, FlgG, or FlgJ caused inhibition of the motility of wild-type cells and inhibition of the export of the hook-capping protein FlgD. We also examined the question of whether export and translation are linked and found that all substrates tested could be exported after protein synthesis had been blocked by spectinomycin or chloramphenicol. We conclude that the amino acid sequence of these proteins suffices to mediate their recognition and export.

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

{dagger} Present address: Aizawa Team, Soft Nano-Machine Project, CREST, c/o Kochi Sangyo, Tochigi 329-1206, Japan.

Journal of Bacteriology, April 2003, p. 2485-2492, Vol. 185, No. 8
0021-9193/03/$08.00+0     DOI: 10.1128/JB.185.8.2485-2492.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Hirano, T., Mizuno, S., Aizawa, S.-I., Hughes, K. T. (2009). Mutations in Flk, FlgG, FlhA, and FlhE That Affect the Flagellar Type III Secretion Specificity Switch in Salmonella enterica. J. Bacteriol. 191: 3938-3949 [Abstract] [Full Text]  
  • Chevance, F. F.V., Takahashi, N., Karlinsey, J. E., Gnerer, J., Hirano, T., Samudrala, R., Aizawa, S.-I., Hughes, K. T. (2007). The mechanism of outer membrane penetration by the eubacterial flagellum and implications for spirochete evolution. Genes Dev. 21: 2326-2335 [Abstract] [Full Text]  
  • Lee, H. J., Hughes, K. T. (2006). Posttranscriptional Control of the Salmonella enterica Flagellar Hook Protein FlgE. J. Bacteriol. 188: 3308-3316 [Abstract] [Full Text]  
  • Eggenhofer, E., Rachel, R., Haslbeck, M., Scharf, B. (2006). MotD of Sinorhizobium meliloti and Related {alpha}-Proteobacteria Is the Flagellar-Hook-Length Regulator and Therefore Reassigned as FliK. J. Bacteriol. 188: 2144-2153 [Abstract] [Full Text]  
  • Frye, J., Karlinsey, J. E., Felise, H. R., Marzolf, B., Dowidar, N., McClelland, M., Hughes, K. T. (2006). Identification of New Flagellar Genes of Salmonella enterica Serovar Typhimurium. J. Bacteriol. 188: 2233-2243 [Abstract] [Full Text]  
  • Wilharm, G., Lehmann, V., Krauss, K., Lehnert, B., Richter, S., Ruckdeschel, K., Heesemann, J., Trulzsch, K. (2004). Yersinia enterocolitica Type III Secretion Depends on the Proton Motive Force but Not on the Flagellar Motor Components MotA and MotB. Infect. Immun. 72: 4004-4009 [Abstract] [Full Text]  
  • Kelly, A., Goldberg, M. D., Carroll, R. K., Danino, V., Hinton, J. C. D., Dorman, C. J. (2004). A global role for Fis in the transcriptional control of metabolism and type III secretion in Salmonella enterica serovar Typhimurium. Microbiology 150: 2037-2053 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»