Signal peptides are allosteric activators of the protein translocase

Giorgos Gouridis, Spyridoula Karamanou, Ioannis Gelis, Charalampos G. Kalodimos and Anastassios Economou ()
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Giorgos Gouridis: Institute of Molecular Biology and Biotechnology, Foundation of Research and Technology-Hellas, Iraklio, Crete 71110, 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

Nature, 2009, vol. 462, issue 7271, 363-367

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.

Date: 2009
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DOI: 10.1038/nature08559

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