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 Lloyd, S. A.
Right arrow Articles by Blair, D. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lloyd, S. A.
Right arrow Articles by Blair, D. F.

 Previous Article  |  Next Article 

J. Bacteriol., Jan 1996, 223-231, Vol 178, No. 1
Copyright © 1996, American Society for Microbiology

Torque generation in the flagellar motor of Escherichia coli: evidence of a direct role for FliG but not for FliM or FliN

SA Lloyd, H Tang, X Wang, S Billings and DF Blair
Department of Biology, University of Utah, Salt Lake City 84112, USA.

Among the many proteins needed for assembly and function of bacterial flagella, FliG, FliM, and FliN have attracted special attention because mutant phenotypes suggest that they are needed not only for flagellar assembly but also for torque generation and for controlling the direction of motor rotation. A role for these proteins in torque generation is suggested by the existence of mutations in each of them that produce the Mot- (or paralyzed) phenotype, in which flagella are assembled and appear normal but do not rotate. The presumption is that Mot- defects cause paralysis by specifically disrupting functions essential for torque generation, while preserving the features of a protein needed for flagellar assembly. Here, we present evidence that the reported mot mutations in fliM and fliN do not disrupt torque- generating functions specifically but, instead, affect the incorporation of proteins into the flagellum. The fliM and fliN mutants are immotile at normal expression levels but become motile when the mutant proteins and/or other, evidently interacting flagellar proteins are overexpressed. In contrast, many of the reported fliG mot mutations abolish motility at all expression levels, while permitting flagellar assembly, and thus appear to disrupt torque generation specifically. These mutations are clustered in a segment of about 100 residues at the carboxyl terminus of FliG. A slightly larger carboxyl-terminal segment of 126 residues accumulates in the cells when expressed alone and thus probably constitutes a stable, independently folded domain. We suggest that the carboxyl-terminal domain of FliG functions specifically in torque generation, forming the rotor portion of the site of energy transduction in the flagellar motor.


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]  
  • Blair, K. M., Turner, L., Winkelman, J. T., Berg, H. C., Kearns, D. B. (2008). A Molecular Clutch Disables Flagella in the Bacillus subtilis Biofilm. Science 320: 1636-1638 [Abstract] [Full Text]  
  • Obara, M., Yakushi, T., Kojima, S., Homma, M. (2008). Roles of Charged Residues in the C-Terminal Region of PomA, a Stator Component of the Na+-Driven Flagellar Motor. J. Bacteriol. 190: 3565-3571 [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]  
  • Mashimo, T., Hashimoto, M., Yamaguchi, S., Aizawa, S.-I. (2007). Temperature-Hypersensitive Sites of the Flagellar Switch Component FliG in Salmonella enterica Serovar Typhimurium. J. Bacteriol. 189: 5153-5160 [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]  
  • 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]  
  • Yakushi, T., Yang, J., Fukuoka, H., Homma, M., Blair, D. F. (2006). Roles of Charged Residues of Rotor and Stator in Flagellar Rotation: Comparative Study using H+-Driven and Na+-Driven Motors in Escherichia coli. J. Bacteriol. 188: 1466-1472 [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 Way, S. M., Millas, S. G., Lee, A. H., Manson, M. D. (2004). Rusty, Jammed, and Well-Oiled Hinges: Mutations Affecting the Interdomain Region of FliG, a Rotor Element of the Escherichia coli Flagellar Motor. J. Bacteriol. 186: 3173-3181 [Abstract] [Full Text]  
  • Yorimitsu, T., Kojima, M., Yakushi, T., Homma, M. (2004). Multimeric Structure of the PomA/PomB Channel Complex in the Na+-Driven Flagellar Motor of Vibrio alginolyticus. J Biochem 135: 43-51 [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]  
  • McClain, J., Rollo, D. R., Rushing, B. G., Bauer, C. E. (2002). Rhodospirillum centenum Utilizes Separate Motor and Switch Components To Control Lateral and Polar Flagellum Rotation. J. Bacteriol. 184: 2429-2438 [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]  
  • McCarter, L. L. (2001). Polar Flagellar Motility of the Vibrionaceae. Microbiol. Mol. Biol. Rev. 65: 445-462 [Abstract] [Full Text]  
  • Poggio, S., Osorio, A., Corkidi, G., Dreyfus, G., Camarena, L. (2001). The N Terminus of FliM Is Essential To Promote Flagellar Rotation in Rhodobacter sphaeroides. J. Bacteriol. 183: 3142-3148 [Abstract] [Full Text]  
  • Gosink, K. K., Häse, C. C. (2000). Requirements for Conversion of the Na+-Driven Flagellar Motor of Vibrio cholerae to the H+-Driven Motor of Escherichia coli. J. Bacteriol. 182: 4234-4240 [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]  
  • Sato, K., Homma, M. (2000). Functional Reconstitution of the Na+-driven Polar Flagellar Motor Component of Vibrio alginolyticus. J. Biol. Chem. 275: 5718-5722 [Abstract] [Full Text]  
  • Boles, B. R., McCarter, L. L. (2000). Insertional Inactivation of Genes Encoding Components of the Sodium-Type Flagellar Motor and Switch of Vibrio parahaemolyticus. J. Bacteriol. 182: 1035-1045 [Abstract] [Full Text]  
  • Mathews, M. A. A., Tang, H. L., Blair, D. F. (1998). Domain Analysis of the FliM Protein of Escherichia coli. J. Bacteriol. 180: 5580-5590 [Abstract] [Full Text]  
  • Donato, G. M., Kawula, T. H. (1998). Enhanced Binding of Altered H-NS Protein to Flagellar Rotor Protein FliG Causes Increased Flagellar Rotational Speed and Hypermotility in Escherichia coli. J. Biol. Chem. 273: 24030-24036 [Abstract] [Full Text]  
  • Berlyn, M. K. B. (1998). Linkage Map of Escherichia coli K-12, Edition 10: The Traditional Map. Microbiol. Mol. Biol. Rev. 62: 814-984 [Abstract] [Full Text]  
  • Zhou, J., Lloyd, S. A., Blair, D. F. (1998). Electrostatic interactions between rotor and stator in the bacterial flagellar motor. Proc. Natl. Acad. Sci. USA 95: 6436-6441 [Abstract] [Full Text]  
  • Zhou, J., Sharp, L. L., Tang, H. L., Lloyd, S. A., Billings, S., Braun, T. F., Blair, D. F. (1998). Function of Protonatable Residues in the Flagellar Motor of Escherichia coli: a Critical Role for Asp 32 of MotB. J. Bacteriol. 180: 2729-2735 [Abstract] [Full Text]  
  • Berg, H. C. (1996). Symmetries in bacterial motility. Proc. Natl. Acad. Sci. USA 93: 14225-14228 [Abstract] [Full Text]  
  • Sato, K., Homma, M. (2000). Multimeric Structure of PomA, a Component of the Na+-driven Polar Flagellar Motor of Vibrio alginolyticus. J. Biol. Chem. 275: 20223-20228 [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»