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J. Biol. Chem., Vol. 280, Issue 2, 974-983, January 14, 2005

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Depletion of Apolipoprotein N-Acyltransferase Causes Mislocalization of Outer Membrane Lipoproteins in Escherichia coli^*

Carine Robichon, Dominique Vidal-Ingigliardi, and Anthony P. Pugsley

From the Molecular Genetics Unit, CNRS URA2172, Institut Pasteur, 25 Rue du Dr. Roux, 75724 Paris Cedex 5, France

Lipoproteins in Gram-negative Enterobacteriaceae carry three fatty acids on the N-terminal cysteine residue, two as a diacylglyceride and one through an N-linkage following signal peptide cleavage. Most lipoproteins are anchored in the outer membrane, facing the periplasm, but some lipoproteins remain in the plasma membrane, depending on the amino acid at position +2, immediately after the fatty-acylated cysteine. In vitro, the last step in lipoprotein maturation, N-acylation of apolipoproteins by the plasma membrane apolipoprotein N-acyltransferase (Lnt), is necessary for efficient recognition of outer membrane lipoproteins by the Lol system, which transports them from the plasma to the outer membrane (Fukuda, A., Matsuyama, S.-I., Hara, T., Nakayama, J., Nagasawa, H., and Tokuda, H. (2002) J. Biol. Chem. 277, 43512–43518). To study the role of Lnt in vivo, we constructed a conditional lnt mutant of Escherichia coli. The apo-form of peptidoglycan-anchored major lipoprotein (Lpp) and two other outer membrane lipoproteins accumulated in the plasma membrane when lnt expression was reduced. We also found that Lnt is an essential protein in E. coli and that the lethality is partially because of the retention of apoLpp in the plasma membrane. Topology mapping of Lnt with -galactosidase and alkaline phosphatase fusions indicated the presence of six membrane-spanning segments. The lnt gene in a mutant of Salmonella enterica displaying thermosensitive Lnt activity (Gupta, S. D., Gan, K., Schmid, M. B., and Wu, H. C. (1993) J. Biol. Chem. 268, 16551–16556) was found to carry a mutation causing a single glutamate to lysine substitution at a highly conserved position in the last predicted periplasmic loop of the protein.

Received for publication, September 27, 2004 , and in revised form, October 27, 2004.

^* This work was supported in part by the European Commission Grant HPRN-2000-00075. 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.

Supported by grants from the Ministère d'Enseignement et Recherche, the Fondation pour la Recherche Médicale (FRM), and the CANAM. Present address: Dept. of Microbiology and Molecular Genetics, Harvard Medical, School, 200 Longwood Ave., Boston, MA 02115.

To whom correspondence should be addressed. Tel.: 33-145688494; Fax: 33-145688960; E-mail: max{at}pasteur.fr.

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