The conserved carboxy-terminus of the MscS mechanosensitive channel is not essential but increases stability and activity.

@article{Schumann2004TheCC,
  title={The conserved carboxy-terminus of the MscS mechanosensitive channel is not essential but increases stability and activity.},
  author={Ulrike D. Schumann and Michelle D. Edwards and Chan Li and Ian R. Booth},
  journal={FEBS letters},
  year={2004},
  volume={572 1-3},
  pages={
          233-7
        }
}
The Escherichia coli MscS mechanosensitive channel protein has a distinct domain structure that terminates in a conserved seven-strand beta barrel. This distinctive feature suggested it could be a critical determinant of channel stability and activity. Measurements on a protein deleted for the base of the vestibule and the beta barrel (residues 266-286) suggested that the modified channel had reduced activity. However, induction of the mutant protein resulted in membrane protein accumulation… CONTINUE READING
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