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Gene Review

motA  -  motility protein protein A

Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

 
 
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Disease relevance of motA

  • Torque generation in the flagellar motor of Escherichia coli: evidence of a direct role for FliG but not for FliM or FliN [1].
  • An extreme clockwise switch bias mutation in fliG of Salmonella typhimurium and its suppression by slow-motile mutations in motA and motB [2].
 

High impact information on motA

  • To study interactions between the Mot proteins themselves and between them and other components of the flagellar motor, we attempted to isolate extragenic suppressors of 13 dominant or partially dominant motB missense mutations [3].
  • Impressive progress has been made in understanding the mechanism of bacterial chemotaxis and function of the flagellar motor, but how the direction of rotation is reversed by the 'flagellar switch'--a central step in chemotaxis--remains obscure and calls for new experimental approaches [4].
  • The specificity of fumarate as a switching factor of the bacterial flagellar motor [5].
  • Geometry of the flagellar motor in the cytoplasmic membrane of Salmonella typhimurium as determined by stereo-photogrammetry of quick-freeze deep-etch replica images [6].
  • Within this complex, the receptor regulates the autophosphorylation activity of histidine kinase CheA, thereby controlling the signals sent to the flagellar motor and the receptor adaptation system [7].
 

Biological context of motA

  • Correlation between phosphorylation of the chemotaxis protein CheY and its activity at the flagellar motor [8].
  • A spontaneous fliL mutant of S. typhimurium, containing a frameshift mutation about 40% from the 3' end of the gene, was moderately motile but swarmed poorly, suggesting that FliL might be a component of the flagellar motor or switch [9].

References

  1. Torque generation in the flagellar motor of Escherichia coli: evidence of a direct role for FliG but not for FliM or FliN. Lloyd, S.A., Tang, H., Wang, X., Billings, S., Blair, D.F. J. Bacteriol. (1996) [Pubmed]
  2. An extreme clockwise switch bias mutation in fliG of Salmonella typhimurium and its suppression by slow-motile mutations in motA and motB. Togashi, F., Yamaguchi, S., Kihara, M., Aizawa, S.I., Macnab, R.M. J. Bacteriol. (1997) [Pubmed]
  3. Motility protein interactions in the bacterial flagellar motor. Garza, A.G., Harris-Haller, L.W., Stoebner, R.A., Manson, M.D. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  4. Bacterial chemotaxis: unsolved mystery of the flagellar switch. Eisenbach, M., Caplan, S.R. Curr. Biol. (1998) [Pubmed]
  5. The specificity of fumarate as a switching factor of the bacterial flagellar motor. Barak, R., Giebel, I., Eisenbach, M. Mol. Microbiol. (1996) [Pubmed]
  6. Geometry of the flagellar motor in the cytoplasmic membrane of Salmonella typhimurium as determined by stereo-photogrammetry of quick-freeze deep-etch replica images. Katayama, E., Shiraishi, T., Oosawa, K., Baba, N., Aizawa, S. J. Mol. Biol. (1996) [Pubmed]
  7. Conserved glycine residues in the cytoplasmic domain of the aspartate receptor play essential roles in kinase coupling and on-off switching. Coleman, M.D., Bass, R.B., Mehan, R.S., Falke, J.J. Biochemistry (2005) [Pubmed]
  8. Correlation between phosphorylation of the chemotaxis protein CheY and its activity at the flagellar motor. Barak, R., Eisenbach, M. Biochemistry (1992) [Pubmed]
  9. Characterization of the fliL gene in the flagellar regulon of Escherichia coli and Salmonella typhimurium. Raha, M., Sockett, H., Macnab, R.M. J. Bacteriol. (1994) [Pubmed]
 
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