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Signal peptides are allosteric activators of the protein translocase

Author

Listed:
  • Giorgos Gouridis

    (Institute of Molecular Biology and Biotechnology, Foundation of Research and Technology-Hellas, Iraklio, Crete 71110, Greece
    University of Crete, Iraklio, Crete 71409, Greece)

  • Spyridoula Karamanou

    (Institute of Molecular Biology and Biotechnology, Foundation of Research and Technology-Hellas, Iraklio, Crete 71110, Greece)

  • Ioannis Gelis

    (Chemistry & Chemical Biology, Biomedical Engineering, Rutgers University, 599 Taylor Rd, Piscataway, New Jersey 08854, USA)

  • Charalampos G. Kalodimos

    (Chemistry & Chemical Biology, Biomedical Engineering, Rutgers University, 599 Taylor Rd, Piscataway, New Jersey 08854, USA)

  • Anastassios Economou

    (Institute of Molecular Biology and Biotechnology, Foundation of Research and Technology-Hellas, Iraklio, Crete 71110, Greece
    University of Crete, Iraklio, Crete 71409, Greece)

Abstract

Signal peptides as allosteric activators Most secreted proteins contain a cleavable N-terminal signal sequence that mediates their targeting and translocation across membranes. In bacteria, the protein translocation channel is comprised of the SecYEG channel and the ATPase motor, SecA. Targetting of proteins to SecA is thought to involve signal sequence recognition. Gouridis et al. demonstrate that signal sequences have a novel role beyond protein targeting. They can act in trans and allosterically activate the SecYEG translocase. Translocase activation proceeds through two consecutive but distinct signal-peptide-driven states. This study sheds light on a fundamental cellular process.

Suggested Citation

  • Giorgos Gouridis & Spyridoula Karamanou & Ioannis Gelis & Charalampos G. Kalodimos & Anastassios Economou, 2009. "Signal peptides are allosteric activators of the protein translocase," Nature, Nature, vol. 462(7271), pages 363-367, November.
    • Handle: RePEc:nat:nature:v:462:y:2009:i:7271:d:10.1038_nature08559
    DOI: 10.1038/nature08559
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