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J. Biol. Chem., Vol. 278, Issue 24, 22161-22167, June 13, 2003

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Export of -Lactamase Is Independent of the Signal Recognition Particle^*

Daniel Beha , Sandra Deitermann  , Matthias Müller  and Hans-Georg Koch  ¶

From the Institute for Biochemistry and Molecular Biology, Hermann-Herder-Strasse 7, 79104 Freiburg, Germany, Faculty of Biology, and Albert-Ludwigs-Universität Freiburg, Hermann-Herder-Strasse 7, 79104 Freiburg, Germany

In Escherichia coli, three different types of proteins engage the SecY translocon of the inner bacterial membrane for translocation or insertion: 1) polytopic membrane proteins that prior to their insertion into the membrane are targeted to the translocon using the bacterial signal recognition particle (SRP) and its receptor; 2) secretory proteins that are targeted to and translocated across the SecY translocon in a SecA- and SecB-dependent reaction; and 3) membrane proteins with large periplasmic domains, requiring SRP for targeting and SecA for the translocation of the periplasmic moiety. In addition to its role as a targeting device for membrane proteins, a function of the bacterial SRP in the export of SecB-independent secretory proteins has also been postulated. In particular, -lactamase, a hydrolytic enzyme responsible for cleavage of the -lactam ring containing antibiotics, is considered to be recognized and targeted by SRP. To examine the role of the SRP pathway in -lactamase targeting and export, we performed a detailed in vitro analysis. Chemical cross-linking and membrane binding assays did not reveal any significant interaction between SRP and -lactamase nascent chains. More importantly, membrane vesicles prepared from mutants lacking a functional SRP pathway did block the integration of SRP-dependent membrane proteins but supported the export of -lactamase in the same way as that of the SRP-independent protein OmpA. These data demonstrate that in contrast to previous results, the bacterial SRP is not involved in the export of -lactamase and further suggest that secretory proteins of Gram-negative bacteria in general are not substrates of SRP.

Received for publication, January 28, 2003 , and in revised form, April 7, 2003.

^* This work was supported by Sonderforschungsbereich Grant 388, the Fonds der Chemischen Industrie, and European Union Grant QLK3-CT-1999-0917. 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.: 49-761-2035250; Fax: 49-761-2035253; E-mail: Hans-Georg.Koch{at}biochemie.uni-freiburg.de.

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