Topology of the hydrophobic membrane-bound components of the histidine periplasmic permease. Comparison with other members of the family.

@article{Kerppola1992TopologyOT,
  title={Topology of the hydrophobic membrane-bound components of the histidine periplasmic permease. Comparison with other members of the family.},
  author={R E Kerppola and Giovanna Ferro-Luzzi Ames},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 4},
  pages={2329-36}
}
The membrane-bound complex of periplasmic permeases comprises two hydrophobic proteins which have been hypothesized to be integral membrane-spaninning proteins. We have investigated the topological organization of the hydrophobic components of the Salmonella typhimurium histidine permease, HisQ and HisM. Both proteins are digested by trypsin and proteinase K when either inside-out or right-side-out membrane vesicles are used. Therefore, these proteins are exposed to both surfaces of the… CONTINUE READING

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