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J. Biol. Chem., Vol. 279, Issue 43, 44966-44975, October 22, 2004

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Lipid Trafficking Controls Endotoxin Acylation in Outer Membranes of Escherichia coli^*

Wenyi Jia, Ahmed El Zoeiby¶, Tania N. Petruzziello, Bamini Jayabalasingham, Seyedreza Seyedirashti, and Russell E. Bishop||

From the Department of Laboratory Medicine and Pathobiology and the Department of Biochemistry, the University of Toronto, Toronto, Ontario M5S 1A8, Canada

The biogenesis of biological membranes hinges on the coordinated trafficking of membrane lipids between distinct cellular compartments. The bacterial outer membrane enzyme PagP confers resistance to host immune defenses by transferring a palmitate chain from a phospholipid to the lipid A (endotoxin) component of lipopolysaccharide. PagP is an eight-stranded antiparallel -barrel, preceded by an N-terminal amphipathic -helix. The active site is localized inside the -barrel and is aligned with the lipopolysaccharide-containing outer leaflet, but the phospholipid substrates are normally restricted to the inner leaflet of the asymmetric outer membrane. We examined the possibility that PagP activity in vivo depends on the aberrant migration of phospholipids into the outer leaflet. We find that brief addition to Escherichia coli cultures of millimolar EDTA, which is reported to replace a fraction of lipopolysaccharide with phospholipids, rapidly induces palmitoylation of lipid A. Although expression of the E. coli pagP gene is induced during Mg²⁺ limitation by the phoPQ two-component signal transduction pathway, EDTA-induced lipid A palmitoylation occurs more rapidly than pagP induction and is independent of de novo protein synthesis. EDTA-induced lipid A palmitoylation requires functional MsbA, an essential ATP-binding cassette transporter needed for lipid transport to the outer membrane. A potential role for the PagP -helix in phospholipid translocation to the outer leaflet was excluded by showing that -helix deletions are active in vivo. Neither EDTA nor Mg²⁺-EDTA stimulate PagP activity in vitro. These findings suggest that PagP remains dormant in outer membranes until Mg²⁺ limitation promotes the migration of phospholipids into the outer leaflet.

Received for publication, May 4, 2004 , and in revised form, August 16, 2004.

^* This work was supported by in part by Canadian Institutes of Health Research Operating Grant MOP-43886 (to R. E. B.). 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 fellowships from the Fonds de la Recherche en Santé du Quebec and the Canadian Institutes of Health Research training program grant on the structure and function of membrane proteins linked to disease.

^|| To whom correspondence should be addressed: Dept. of Laboratory Medicine and Pathobiology and Dept. of Biochemistry, University of Toronto, 6213 Medical Sciences Bldg., 1 King's College Circle, Toronto, Ontario M5S 1A8, Canada. Tel.: 416-946-7103; Fax: 416-978-5959; E-mail: russell.bishop{at}utoronto.ca.

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