FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activity.

@article{Minamino2000FliHAS,
  title={FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activity.},
  author={Tohru Minamino and Robert M. Macnab},
  journal={Molecular microbiology},
  year={2000},
  volume={37 6},
  pages={1494-503}
}
Both FliH and the ATPase FliI are cytoplasmic components of the Salmonella type III flagellar export apparatus. Dominance and inhibition data have suggested that the N-terminus of FliI interacts with FliH and that this interaction is important for the ATPase function of the C-terminal domain of FliI. N-terminally histidine-tagged, wild-type FliI retarded untagged FliH in a Ni-NTA affinity chromatography assay, as did N-His-tagged versions of FliI carrying catalytic mutations. In contrast, N-His… CONTINUE READING

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