Membrane topology of CadA homologous P-type ATPase of Helicobacter pylori as determined by expression of phoA fusions in Escherichia coli and the positive inside rule.

@article{Melchers1999MembraneTO,
  title={Membrane topology of CadA homologous P-type ATPase of Helicobacter pylori as determined by expression of phoA fusions in Escherichia coli and the positive inside rule.},
  author={Klaus Melchers and Alexander Schuhmacher and Anita Buhmann and Thomas Weitzenegger and Dominique Belin and Sandra Grau and Michael Ehrmann},
  journal={Research in microbiology},
  year={1999},
  volume={150 8},
  pages={
          507-20
        }
}
The only experimental data available on the membrane topology of transition metal ATPases are from in vitro studies on two distinct P-type ATPases (CadA and CopA) of a gastric bacterium, Helicobacter pylori, both postulated to contain eight transmembrane domains (H1 to H8). In this study, H. pylori CadA ATPase was subjected to analysis of membrane topology in vivo by expression of ATPase-alkaline phosphatase (AP) hybrid proteins in Escherichia coli using a novel vector, pBADphoA. This vector… CONTINUE READING

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