Topologically Fixed SecG Is Fully Functional-Reference-Cited by-同舟云学术

Topologically Fixed SecG Is Fully Functional

Published:2006-02 Issue:3 Volume:188 Page:1188-1190
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

van der Sluis Eli O.¹,van der Vries Erhard¹,Berrelkamp Greetje¹,Nouwen Nico¹,Driessen Arnold J. M.¹

Affiliation:

1. Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and Materials Science Center Plus, University of Groningen, 9751 NN Haren, The Netherlands

Abstract

ABSTRACT 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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.188.3.1188-1190.2006

Reference23 articles.

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3. de Keyzer, J., C. van der Does, and A. J. M. Driessen. 2003. The bacterial translocase: a dynamic protein channel complex. Cell, Mol. Life Sci.60:2034-2052.

4. de Keyzer, J., E. O. van der Sluis, R. E. Spelbrink, N. Nijstad, B. de Kruijff, N. Nouwen, C. van der Does, and A. J. M. Driessen. 2005. Covalently dimerized SecA is functional in protein translocation. J. Biol. Chem.280:35255-35260.

5. Duong, F., and W. Wickner. 1997. Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme. EMBO J.16:2756-2768.

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