Journal of Bacteriology, February 2006, p. 1188-1190, Vol. 188, No. 3
0021-9193/06/$08.00+0 doi:10.1128/JB.188.3.1188-1190.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Topologically Fixed SecG Is Fully Functional
Eli O. van der Sluis,
Erhard van der Vries,
Greetje Berrelkamp,
Nico Nouwen, and
Arnold J. M. Driessen*
Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and Materials Science Center Plus, University of Groningen, 9751 NN Haren, The Netherlands
Received 19 September 2005/
Accepted 28 October 2005
It has been proposed that the bitopic membrane protein SecG undergoes topology inversion during translocation of (pre)proteins via SecYEG. Here we show that SecG covalently cross-linked to SecY cannot invert its topology while remaining fully functional in protein translocation. Our results strongly disfavor topology inversion of SecG during protein translocation.
* Corresponding author. Mailing address: Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and Materials Science Center Plus, Kerklaan 30, University of Groningen, 9751 NN Haren, The Netherlands. Phone: 31503632164. Fax: 31503632164. E-mail: a.j.m.driessen{at}rug.nl.
Journal of Bacteriology, February 2006, p. 1188-1190, Vol. 188, No. 3
0021-9193/06/$08.00+0 doi:10.1128/JB.188.3.1188-1190.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
This article has been cited by other articles:
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Sugai, R., Takemae, K., Tokuda, H., Nishiyama, K.-i.
(2007). Topology Inversion of SecG Is Essential for Cytosolic SecA-dependent Stimulation of Protein Translocation. J. Biol. Chem.
282: 29540-29548
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Copyright © 2006 by the American Society for Microbiology. All rights reserved.