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J. Biol. Chem., Vol. 279, Issue 3, 1659-1664, January 16, 2004

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SecYEG Proteoliposomes Catalyze the -Dependent Membrane Insertion of FtsQ^*

Martin van der Laan, Nico Nouwen, and Arnold J. M. Driessen

From the Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands

In Escherichia coli, the insertion of most inner membrane proteins is mediated by the Sec translocase. Ribosome-bound nascent chains of Sec-dependent inner membrane proteins are targeted to the SecYEG complex via the signal recognition particle pathway. We now demonstrate that the signal recognition particle-dependent co-translational membrane targeting and membrane insertion of FtsQ can be reconstituted with proteoliposomes containing purified SecYEG. SecA and a transmembrane electrical potential are essential for the translocation of the large periplasmic domain of FtsQ, whereas co-reconstituted YidC has an inhibitory effect. These data demonstrate that membrane protein insertion can be reconstituted with a minimal set of purified Sec components.

Received for publication, June 19, 2003 , and in revised form, October 24, 2003.

^* This work was supported by the Earth and Life Sciences Foundation, which is subsidized by the Netherlands Organization for Scientific Research. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 31-50-3632164; Fax: 31-50-3632154; E-mail: a.j.m.driessen{at}biol.rug.nl.

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