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Originally published In Press as doi:10.1074/jbc.M403229200 on May 12, 2004
J. Biol. Chem., Vol. 279, Issue 30, 31026-31032, July 23, 2004
Targeting and Translocation of Two Lipoproteins in Escherichia coli via the SRP/Sec/YidC Pathway*
Linda Fröderberg ,
Edith N. G. Houben¶,
Louise Baars ,
Joen Luirink¶, and
Jan-Willem de Gier ||
From the
Department of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, SE-106 91 Stockholm, Sweden and the ¶Department of Microbiology, BioCentrum Amsterdam, De Boelelaan 1087, 1081 HV Amsterdam, The Netherlands
In Escherichia coli, two main protein targeting pathways to the inner membrane exist: the SecB pathway for the essentially posttranslational targeting of secretory proteins and the SRP pathway for cotranslational targeting of inner membrane proteins (IMPs). At the inner membrane both pathways converge at the Sec translocase, which is capable of both linear transport into the periplasm and lateral transport into the lipid bilayer. The Sec-associated YidC appears to assist the lateral transport of IMPs from the Sec translocase into the lipid bilayer. It should be noted that targeting and translocation of only a handful of secretory proteins and IMPs have been studied. These model proteins do not include lipoproteins. Here, we have studied the targeting and translocation of two secretory lipoproteins, the murein lipoprotein and the bacteriocin release protein, using a combined in vivo and in vitro approach. The data indicate that both murein lipoprotein and bacteriocin release protein require the SRP pathway for efficient targeting to the Sec translocase. Furthermore, we show that YidC plays an important role in the targeting/translocation of both lipoproteins.
Received for publication, March 23, 2004
, and in revised form, May 12, 2004.
* This work was supported by grants from the Swedish Research Council, the Carl Tryggers Stiftelse, the European Molecular Biology Organization (EMBO) Young Investigator Program (to J. W. dG.), and the Dutch Research Council (to J.L.). 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.
Recipient of an EMBO short term fellowship.
|| To whom correspondence should be addressed. Tel.: 46-8-164389 (laboratory)/162420 (office); Fax: 46-8-153679; E-mail: degier{at}dbb.su.se.

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Copyright © 2004 by the American Society for Biochemistry and Molecular Biology.
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