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J. Biol. Chem., Vol. 279, Issue 11, 10484-10493, March 12, 2004

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Monoglucosyldiacylglycerol, a Foreign Lipid, Can Substitute for Phosphatidylethanolamine in Essential Membrane-associated Functions in Escherichia coli^*

Malin Wikström, Jun Xie¶, Mikhail Bogdanov¶, Eugenia Mileykovskaya¶, Philip Heacock¶, Åke Wieslander||, and William Dowhan¶**

From the Department of Biochemistry and Biophysics, Stockholm University, Stockholm 10691, Sweden and the ^¶Department of Biochemistry and Molecular Biology, University of Texas School of Medicine, Houston, Texas 77030

The mechanisms by which lipid bilayer properties govern or influence membrane protein functions are little understood, but a liquid-crystalline state and the presence of anionic and nonbilayer (NB)-prone lipids seem important. An Escherichia coli mutant lacking the major membrane lipid phosphatidylethanolamine (NB-prone) requires divalent cations for viability and cell integrity and is impaired in several membrane functions that are corrected by introduction of the "foreign" NB-prone neutral glycolipid -monoglucosyldiacylglycerol (MGlcDAG) synthesized by the MGlcDAG synthase from Acholeplasma laidlawii. Dependence on Mg²⁺ was reduced, and cellular yields and division malfunction were greatly improved. The increased passive membrane permeability of the mutant was not abolished, but protein-mediated osmotic stress adaptation to salts and sucrose was recovered by the presence of MGlcDAG. MGlcDAG also restored tryptophan prototrophy and active transport function of lactose permease, both critically dependent on phosphatidylethanolamine. Three mechanisms can explain the observed effects: NB-prone MGlcDAG improves the quenched lateral pressure profile across the bilayer; neutral MGlcDAG dilutes the high anionic lipid surface charge; MGlcDAG provides a neutral lipid that can hydrogen bond and/or partially ionize. The reduced dependence on Mg²⁺ and lack of correction by high monovalent salts strongly support the essential nature of the NB properties of MGlcDAG.

Received for publication, September 12, 2003 , and in revised form, December 10, 2003.

^* This work was supported in part by National Institutes of Health Grant GM20487 (to W. D.) and the Swedish Science Research Council (to A. W.). 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.

These authors contributed equally to this work.

|| To whom correspondence may be addressed. Tel.: 46-8-16-24-63; Fax: 46-8-15-36-79; E-mail: ake{at}dbb.su.se. ^** To whom correspondence may be addressed: Dept. of Biochemistry and Molecular Biology, 6431 Fannin St., Suite 6.200, University of Texas Medical School, Houston, TX 77030. Tel.: 713-500-6051; Fax: 713-500-0652; E-mail: William.Dowhan{at}uth.tmc.edu.

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