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 Kihara, M.
Right arrow Articles by Macnab, R. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kihara, M.
Right arrow Articles by Macnab, R. M.

 Previous Article  |  Next Article 

Journal of Bacteriology, June 2000, p. 3022-3028, Vol. 182, No. 11
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Deletion Analysis of the Flagellar Switch Protein FliG of Salmonella

May Kihara, Gabriele U. Miller, and Robert M. Macnab*

Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114

Received 14 December 1999/Accepted 7 March 2000

The flagellar motor/switch complex, consisting of the three proteins FliG, FliM, and FliN, plays a central role in bacterial motility and chemotaxis. We have analyzed FliG, using 10-amino-acid deletions throughout the protein and testing the deletion clones for their motility and dominance properties and for interaction of the deletion proteins with the MS ring protein FliF. Only the N-terminal 46 amino acids of FliG (segments 1 to 4) were important for binding to FliF; consistent with this, an N-terminal fragment consisting of residues 1 to 108 bound FliF strongly, whereas a C-terminal fragment consisting of residues 109 to 331 did not bind FliF at all. Deletions in the region from residues 37 to 96 (segments 4 to 9), 297 to 306 (segment 30), and 317 to 326 (segment 32) permitted swarming, though not at wild-type levels; all other deletions caused paralyzed or, more commonly, nonflagellate phenotype. Except for those near the N terminus, deletions had a dominant negative effect on wild-type cells.

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

Journal of Bacteriology, June 2000, p. 3022-3028, Vol. 182, No. 11
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Konishi, M., Kanbe, M., McMurry, J. L., Aizawa, S.-I. (2009). Flagellar Formation in C-Ring-Defective Mutants by Overproduction of FliI, the ATPase Specific for Flagellar Type III Secretion. J. Bacteriol. 191: 6186-6191 [Abstract] [Full Text]  
  • Passmore, S. E., Meas, R., Marykwas, D. L. (2008). Analysis of the FliM/FliG motor protein interaction by two-hybrid mutation suppression analysis. Microbiology 154: 714-724 [Abstract] [Full Text]  
  • Brown, P. N., Terrazas, M., Paul, K., Blair, D. F. (2007). Mutational Analysis of the Flagellar Protein FliG: Sites of Interaction with FliM and Implications for Organization of the Switch Complex. J. Bacteriol. 189: 305-312 [Abstract] [Full Text]  
  • Blair, D. F. (2006). Fine structure of a fine machine.. J. Bacteriol. 188: 7033-7035 [Full Text]  
  • Thomas, D. R., Francis, N. R., Xu, C., DeRosier, D. J. (2006). The Three-Dimensional Structure of the Flagellar Rotor from a Clockwise-Locked Mutant of Salmonella enterica Serovar Typhimurium.. J. Bacteriol. 188: 7039-7048 [Abstract] [Full Text]  
  • Paul, K., Harmon, J. G., Blair, D. F. (2006). Mutational Analysis of the Flagellar Rotor Protein FliN: Identification of Surfaces Important for Flagellar Assembly and Switching.. J. Bacteriol. 188: 5240-5248 [Abstract] [Full Text]  
  • Paul, K., Blair, D. F. (2006). Organization of FliN Subunits in the Flagellar Motor of Escherichia coli.. J. Bacteriol. 188: 2502-2511 [Abstract] [Full Text]  
  • Lowder, B. J., Duyvesteyn, M. D., Blair, D. F. (2005). FliG Subunit Arrangement in the Flagellar Rotor Probed by Targeted Cross-Linking. J. Bacteriol. 187: 5640-5647 [Abstract] [Full Text]  
  • Brown, P. N., Mathews, M. A. A., Joss, L. A., Hill, C. P., Blair, D. F. (2005). Crystal Structure of the Flagellar Rotor Protein FliN from Thermotoga maritima. J. Bacteriol. 187: 2890-2902 [Abstract] [Full Text]  
  • Morehouse, K. A., Goodfellow, I. G., Sockett, R. E. (2005). A Chimeric N-Terminal Escherichia coli-C-Terminal Rhodobacter sphaeroides FliG Rotor Protein Supports Bidirectional E. coli Flagellar Rotation and Chemotaxis. J. Bacteriol. 187: 1695-1701 [Abstract] [Full Text]  
  • Slivienski-Gebhardt, L. L., Izard, J., Samsonoff, W. A., Limberger, R. J. (2004). Development of a Novel Chloramphenicol Resistance Expression Plasmid Used for Genetic Complementation of a fliG Deletion Mutant in Treponema denticola. Infect. Immun. 72: 5493-5497 [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]  
  • Gauthier, A., Finlay, B. B. (2003). Translocated Intimin Receptor and Its Chaperone Interact with ATPase of the Type III Secretion Apparatus of Enteropathogenic Escherichia coli. J. Bacteriol. 185: 6747-6755 [Abstract] [Full Text]  
  • Grunenfelder, B., Gehrig, S., Jenal, U. (2003). Role of the Cytoplasmic C Terminus of the FliF Motor Protein in Flagellar Assembly and Rotation. J. Bacteriol. 185: 1624-1633 [Abstract] [Full Text]  
  • Thomas, D., Morgan, D. G., DeRosier, D. J. (2001). Structures of Bacterial Flagellar Motors from Two FliF-FliG Gene Fusion Mutants. J. Bacteriol. 183: 6404-6412 [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»