Issue 4, 2010
From the journal:

Molecular BioSystems

SecB—A chaperone dedicated to protein translocation†

Philipp Bechtluft,a   Nico Nouwen,b   Sander J. Tansc  and  Arnold J. M. Driessen*a  

* Corresponding authors

a Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and the Zernike Institute for Advanced Materials, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands
E-mail: a.j.m.driessen@rug.nl
Fax: +31-50-3632154
Tel: +31-50-3632164

b Laboratoire des Symbioses Tropicales et Méditerranéennes, Campus International de Baillarguet, TA 10/J-34398 Montpellier cedex 5, France

c FOM Institute for Atomic and Molecular Physics (AMOLF), Kruislaan 407, 1098 SJ Amsterdam, The Netherlands

Abstract

SecB is a molecular chaperone in Gram-negative bacteria dedicated to the post-translational translocation of proteins across the cytoplasmic membrane. The entire surface of this chaperone is used for both of its native functions in protein targeting and unfolding. Single molecule studies revealed how SecB affects the folding pathway of proteins and how it prevents the tertiary structure formation and aggregation to support protein translocation.

Graphical abstract: SecB—A chaperone dedicated to protein translocation

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Article information

DOI
https://doi.org/10.1039/B915435C
Article type
Review Article
Submitted
29 Jul 2009
Accepted
25 Sep 2009
First published
19 Oct 2009

Mol. BioSyst., 2010,6, 620-627

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SecB—A chaperone dedicated to protein translocation

P. Bechtluft, N. Nouwen, S. J. Tans and A. J. M. Driessen, Mol. BioSyst., 2010, 6, 620 DOI: 10.1039/B915435C

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