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J. Biol. Chem., Vol. 283, Issue 46, 31269-31273, November 14, 2008

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Minireview

Mechanisms of YidC-mediated Insertion and Assembly of Multimeric Membrane Protein Complexes^*

Stefan Kol, Nico Nouwen, and Arnold J. M. Driessen¹

From the Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, the Zernike Institute of Advanced Materials, and the Kluyver Centre for the Genomics of Industrial Microorganisms, University of Groningen, 9751 NN Haren, The Netherlands and the Laboratoire de Symbiosis Tropicales et Méditerranéennes, Campus International de Baillarguet TA A-82/J, 34398 Montpellier Cedex 5, France

The YidC protein fulfills a dual and essential role in the assembly of inner membrane proteins in Escherichia coli. Besides interacting with transmembrane segments of newly synthesized membrane proteins that insert into the membrane via the SecYEG complex, YidC also functions as an independent membrane protein insertase and assists in membrane protein folding. Here, we discuss the mechanisms of YidC substrate recognition and membrane insertion with emphasis on its role in the assembly of multimeric membrane protein complexes such as the F₁F₀-ATP synthase.

^* This work was supported by the Earth and Life Science Foundation, subsidized by the Netherlands Organization for Scientific Research, and by European Community Grant LSHG-CT-2004–504601 (European Membrane Protein Consortium). This minireview will be reprinted in the 2008 Minireview Compendium, which will be available in January, 2009.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. 1 and 2.

¹ To whom correspondence should be addressed. Tel.: 31-50-363-2164; Fax: 31-50-363-2164; E-mail: a.j.m.driessen{at}rug.nl.

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