Deletion analysis of the FliM flagellar switch protein of Salmonella typhimurium.

@article{Toker1996DeletionAO,
  title={Deletion analysis of the FliM flagellar switch protein of Salmonella typhimurium.},
  author={Aysegul Toker and May Kihara and Robert M. Macnab},
  journal={Journal of bacteriology},
  year={1996},
  volume={178 24},
  pages={
          7069-79
        }
}
The flagellar switch of Salmonella typhimurium and Escherichia coli is composed of three proteins, FliG, FliM, and FliN. The switch complex modulates the direction of flagellar motor rotation in response to information about the environment received through the chemotaxis signal transduction pathway. In particular, chemotaxis protein CheY is believed to bind to switch protein FliM, inducing clockwise filament rotation and tumbling. To investigate the function of FliM and its interactions with… CONTINUE READING

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Domain analysis of the FliM protein of Escherichia coli.

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References

Publications referenced by this paper.
SHOWING 1-10 OF 29 REFERENCES

Motility protein complexes in the bacterial flagellar motor.

  • Journal of molecular biology
  • 1996
VIEW 14 EXCERPTS
HIGHLY INFLUENTIAL

Model of functional regions of the FliM protein (see text). The horizontal axis shows 10-amino-acid segments of the protein. Functional regions are indicated by coded bars above the FliM sequence (■

E. Katayama, T. Shiraishi, K. Oosawa, N. Baba, S.-I. Aizawa
  • FIG
  • 1996
VIEW 1 EXCERPT