This Article
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 Williams, A. W.
Right arrow Articles by Macnab, R. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Williams, A. W.
Right arrow Articles by Macnab, R. M.

 Previous Article  |  Next Article 

J. Bacteriol., 05 1996, 2960-2970, Vol 178, No. 10
Copyright © 1996, American Society for Microbiology

Mutations in fliK and flhB affecting flagellar hook and filament assembly in Salmonella typhimurium

AW Williams, S Yamaguchi, F Togashi, SI Aizawa, I Kawagishi and RM Macnab
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114, USA.

Mutations in the fliK gene of Salmonella typhimurium commonly cause failure to terminate hook assembly and initiate filament assembly (polyhook phenotype). Polyhook mutants give rise to pseudorevertants which are still defective in hook termination but have recovered the ability to assemble filament (polyhook-filament phenotype). The polyhook mutations have been found to be either frameshift or nonsense, resulting in truncation of the C terminus of FliK. Intragenic suppressors of frameshift mutations were found to be ones that restored the original frame (and therefore the C-terminal sequence), but in most cases with substantial loss of natural sequence and sometimes the introduction of artificial sequence; in no cases did intragenic suppression occur when significant disruption remained within the C- terminal region. By use of a novel PCR protocol, in-frame deletions affecting the N-terminal and central regions of FliK were constructed and the resulting phenotypes were examined. Small deletions resulted in almost normal hook length control and almost wild-type swarming. Larger deletions resulted in loss of control of hook length and poor swarming. The largest deletions severely affected filament assembly as well as hook length control. Extragenic suppressors map to an unlinked gene, flhB, which encodes an integral membrane protein (T. Hirano, S. Yamaguchi, K. Oosawa, and S.-I. Aizawa, J. Bacteriol. 176:5439-5449, 1994; K. Kutsukake, T. Minamino, and T. Yokoseki, J. Bacteriol. 176:7625-7629, 1994). They were either point mutations in the C- terminal cytoplasmic region of FlhB or frameshift or nonsense mutations close to the C terminus. The processes of hook and filament assembly and the roles of FliK and FlhB in these processes are discussed in light of these and other available data. We suggest that FliK measures hook length and, at the appropriate point, sends a signal to FlhB to switch the substrate specificity of export from hook protein to late proteins such as flagellin.


This article has been cited by other articles:

  • Bjornfot, A.-C., Lavander, M., Forsberg, A., Wolf-Watz, H. (2009). Autoproteolysis of YscU of Yersinia pseudotuberculosis Is Important for Regulation of Expression and Secretion of Yop Proteins. J. Bacteriol. 191: 4259-4267 [Abstract] [Full Text]  
  • Douillard, F. P., Ryan, K. A., Hinds, J., O'Toole, P. W. (2009). Effect of FliK mutation on the transcriptional activity of the {sigma}54 sigma factor RpoN in Helicobacter pylori. Microbiology 155: 1901-1911 [Abstract] [Full Text]  
  • Smith, T. G., Pereira, L., Hoover, T. R. (2009). Helicobacter pylori FlhB processing-deficient variants affect flagellar assembly but not flagellar gene expression. Microbiology 155: 1170-1180 [Abstract] [Full Text]  
  • Riordan, K. E., Sorg, J. A., Berube, B. J., Schneewind, O. (2008). Impassable YscP Substrates and Their Impact on the Yersinia enterocolitica Type III Secretion Pathway. J. Bacteriol. 190: 6204-6216 [Abstract] [Full Text]  
  • Arrach, N., Zhao, M., Porwollik, S., Hoffman, R. M., McClelland, M. (2008). Salmonella Promoters Preferentially Activated Inside Tumors. Cancer Res. 68: 4827-4832 [Abstract] [Full Text]  
  • Wood, S. E., Jin, J., Lloyd, S. A. (2008). YscP and YscU Switch the Substrate Specificity of the Yersinia Type III Secretion System by Regulating Export of the Inner Rod Protein YscI. J. Bacteriol. 190: 4252-4262 [Abstract] [Full Text]  
  • Malapaka, V. R.R., Barrese, A. A., Tripp, B. C., Tripp, B. C. (2007). High-Throughput Screening for Antimicrobial Compounds Using a 96-Well Format Bacterial Motility Absorbance Assay. J Biomol Screen 12: 849-854 [Abstract]  
  • Wand, M. E., Sockett, R. E., Evans, K. J., Doherty, N., Sharp, P. M., Hardie, K. R., Winzer, K. (2006). Helicobacter pylori FlhB Function: the FlhB C-Terminal Homologue HP1575 Acts as a "Spare Part" To Permit Flagellar Export When the HP0770 FlhBCC Domain Is Deleted.. J. Bacteriol. 188: 7531-7541 [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]  
  • Kenjale, R., Wilson, J., Zenk, S. F., Saurya, S., Picking, W. L., Picking, W. D., Blocker, A. (2005). The Needle Component of the Type III Secreton of Shigella Regulates the Activity of the Secretion Apparatus. J. Biol. Chem. 280: 42929-42937 [Abstract] [Full Text]  
  • Ferris, H. U., Furukawa, Y., Minamino, T., Kroetz, M. B., Kihara, M., Namba, K., Macnab, R. M. (2005). FlhB Regulates Ordered Export of Flagellar Components via Autocleavage Mechanism. J. Biol. Chem. 280: 41236-41242 [Abstract] [Full Text]  
  • Ryan, K. A., Karim, N., Worku, M., Penn, C. W., O'Toole, P. W. (2005). Helicobacter pylori Flagellar Hook-Filament Transition Is Controlled by a FliK Functional Homolog Encoded by the Gene HP0906. J. Bacteriol. 187: 5742-5750 [Abstract] [Full Text]  
  • McMurry, J. L., Van Arnam, J. S., Kihara, M., Macnab, R. M. (2004). Analysis of the Cytoplasmic Domains of Salmonella FlhA and Interactions with Components of the Flagellar Export Machinery. J. Bacteriol. 186: 7586-7592 [Abstract] [Full Text]  
  • Alegria, M. C., Docena, C., Khater, L., Ramos, C. H. I., da Silva, A. C. R., Farah, C. S. (2004). New Protein-Protein Interactions Identified for the Regulatory and Structural Components and Substrates of the Type III Secretion System of the Phytopathogen Xanthomonas axonopodis Pathovar citri. J. Bacteriol. 186: 6186-6197 [Abstract] [Full Text]  
  • Van Arnam, J. S., McMurry, J. L., Kihara, M., Macnab, R. M. (2004). Analysis of an Engineered Salmonella Flagellar Fusion Protein, FliR-FlhB. J. Bacteriol. 186: 2495-2498 [Abstract] [Full Text]  
  • Creasey, E. A., Delahay, R. M., Daniell, S. J., Frankel, G. (2003). Yeast two-hybrid system survey of interactions between LEE-encoded proteins of enteropathogenic Escherichia coli. Microbiology 149: 2093-2106 [Abstract] [Full Text]  
  • Hirano, T., Minamino, T., Namba, K., Macnab, R. M. (2003). Substrate Specificity Classes and the Recognition Signal for Salmonella Type III Flagellar Export. J. Bacteriol. 185: 2485-2492 [Abstract] [Full Text]  
  • Edqvist, P. J., Olsson, J., Lavander, M., Sundberg, L., Forsberg, A., Wolf-Watz, H., Lloyd, S. A. (2003). YscP and YscU Regulate Substrate Specificity of the Yersinia Type III Secretion System. J. Bacteriol. 185: 2259-2266 [Abstract] [Full Text]  
  • Lavander, M., Sundberg, L., Edqvist, P. J., Lloyd, S. A., Wolf-Watz, H., Forsberg, A. (2002). Proteolytic Cleavage of the FlhB Homologue YscU of Yersinia pseudotuberculosis Is Essential for Bacterial Survival but Not for Type III Secretion. J. Bacteriol. 184: 4500-4509 [Abstract] [Full Text]  
  • Matz, C., van Vliet, A. H. M., Ketley, J. M., Penn, C. W. (2002). Mutational and transcriptional analysis of the Campylobacter jejuni flagellar biosynthesis gene flhB. Microbiology 148: 1679-1685 [Abstract] [Full Text]  
  • Tamano, K., Katayama, E., Toyotome, T., Sasakawa, C. (2002). Shigella Spa32 Is an Essential Secretory Protein for Functional Type III Secretion Machinery and Uniformity of Its Needle Length. J. Bacteriol. 184: 1244-1252 [Abstract] [Full Text]  
  • Chilcott, G. S., Hughes, K. T. (2000). Coupling of Flagellar Gene Expression to Flagellar Assembly in Salmonella enterica Serovar Typhimurium and Escherichia coli. Microbiol. Mol. Biol. Rev. 64: 694-708 [Abstract] [Full Text]  
  • Minamino, T., Macnab, R. M. (2000). Domain Structure of Salmonella FlhB, a Flagellar Export Component Responsible for Substrate Specificity Switching. J. Bacteriol. 182: 4906-4914 [Abstract] [Full Text]  
  • Bonifield, H. R., Yamaguchi, S., Hughes, K. T. (2000). The Flagellar Hook Protein, FlgE, of Salmonella enterica Serovar Typhimurium Is Posttranscriptionally Regulated in Response to the Stage of Flagellar Assembly. J. Bacteriol. 182: 4044-4050 [Abstract] [Full Text]  
  • Kihara, M., Miller, G. U., Macnab, R. M. (2000). Deletion Analysis of the Flagellar Switch Protein FliG of Salmonella. J. Bacteriol. 182: 3022-3028 [Abstract] [Full Text]  
  • Muramoto, K., Makishima, S., Aizawa, S.-I., Macnab, R. M. (1999). Effect of Hook Subunit Concentration on Assembly and Control of Length of the Flagellar Hook of Salmonella. J. Bacteriol. 181: 5808-5813 [Abstract] [Full Text]  
  • Limberger, R. J., Slivienski, L. L., Izard, J., Samsonoff, W. A. (1999). Insertional Inactivation of Treponema denticola tap1 Results in a Nonmotile Mutant with Elongated Flagellar Hooks. J. Bacteriol. 181: 3743-3750 [Abstract] [Full Text]  
  • Minamino, T., Macnab, R. M. (1999). Components of the Salmonella Flagellar Export Apparatus and Classification of Export Substrates. J. Bacteriol. 181: 1388-1394 [Abstract] [Full Text]  
  • Karlinsey, J. E., Tsui, H.-C. T., Winkler, M. E., Hughes, K. T. (1998). Flk Couples flgM Translation to Flagellar Ring Assembly in Salmonella typhimurium. J. Bacteriol. 180: 5384-5397 [Abstract] [Full Text]  
  • Hueck, C. J. (1998). Type III Protein Secretion Systems in Bacterial Pathogens of Animals and Plants. Microbiol. Mol. Biol. Rev. 62: 379-433 [Abstract] [Full Text]  
  • Ciacci-Woolwine, F., Blomfield, I. C., Richardson, S. H., Mizel, S. B. (1998). Salmonella Flagellin Induces Tumor Necrosis Factor Alpha in a Human Promonocytic Cell Line. Infect. Immun. 66: 1127-1134 [Abstract] [Full Text]  
  • Makishima, S., Komoriya, K., Yamaguchi, S., Aizawa, S.-I. (2001). Length of the Flagellar Hook and the Capacity of the Type III Export Apparatus. Science 291: 2411-2413 [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»