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Papers In Press, published online ahead of print October 28, 2004
J. Biol. Chem, 10.1074/jbc.M411059200
Submitted on September 27, 2004
Revised on October 27, 2004
Accepted on October 28, 2004

Depletion of apolipoprotein N-acyltransferase causes mislocalization of outer membrane lipoproteins in escherichia coli

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

Molecular Genetics Unit, Institut Pasteur, Paris 75724

Corresponding Author: max{at}pasteur.fr

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 et al. 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 due to the retention of apoLpp in the plasma membrane. Topology mapping of Lnt with ß-galactosidase and alkaline phosphatase fusions indicated the presence of 6 membrane-spanning segments. The lnt gene in a mutant of Salmonella enterica displaying thermosensitive Lnt activity (Gupta et al. 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.


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