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Mechanism of the Prokaryotic Transmembrane Disulfide Reduction Pathway and Its In Vitro Reconstitution from Purified Components

Authors

  • Dr. Goran Malojčić,

    Corresponding author
    1. Institute for Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich (Switzerland)
    2. Present address: Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, MA 02138 (USA)
    • Institute for Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich (Switzerland)
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  • Dr. Eric R. Geertsma,

    1. Institute of Biochemistry, University of Zurich, 8057 Zurich (Switzerland)
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  • Dr. Maurice S. Brozzo,

    1. Institute for Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich (Switzerland)
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  • Prof. Dr. Rudi Glockshuber

    Corresponding author
    1. Institute for Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich (Switzerland)
    • Institute for Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich (Switzerland)
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  • We thank Raimund Dutzler (University of Zurich), Hauke Hennecke (ETH Zurich), and Hans-Martin Fischer (ETH Zurich) for fruitful discussions throughout this project. We are grateful to Hiang Dreher-Teo for technical assistance. This project was supported by the Swiss National Science Foundation and the ETH Zurich within the framework of the NCCR Structural Biology program, and E.R.G. is supported by the HFSP Long Term Fellowship. G.M. and E.R.G. contributed equally to this work.

Abstract

original image

Dsb-Verbindung: Der Redoxpfad, der Reduktionsäquivalente aus dem bakteriellen Cytoplasma über die innere Membran zu den drei reduktiven Dsb-Pfaden im ansonsten oxidierenden Periplasma überführt (siehe Schema; TR=Thioredoxin-Reduktase, Trx=Thioredoxin) wurde aus den aufgereinigten Komponenten rekonstituiert. Der Transfer der Reduktionsäquivalente über die Membran wurde nachgewiesen, und Details des Mechanismus wurden aufgeklärt.

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