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J. Biol. Chem., Vol. 279, Issue 43, 45102-45109, October 22, 2004
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From the Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710
MsbA is an essential ABC transporter in Escherichia coli required for exporting newly synthesized lipids from the inner to the outer membrane. It remains uncertain whether or not MsbA catalyzes trans-bilayer lipid movement (i.e. flip-flop) within the inner membrane. We now show that newly synthesized lipid A accumulates on the cytoplasmic side of the inner membrane after shifting an E. coli msbA missense mutant to the non-permissive temperature. This conclusion is based on the selective inhibition of periplasmic, but not cytoplasmic, covalent modifications of lipid A that occur in polymyxin-resistant strains of E. coli. The accessibility of newly synthesized phosphatidylethanolamine to membrane impermeable reagents, like 2,4,6-trinitrobenzene sulfonic acid, is also reduced severalfold. Our data showed that MsbA facilitates the rapid translocation of some lipids from the cytoplasmic to the periplasmic side of the inner membrane in living cells.
Received for publication, July 19, 2004 , and in revised form, August 2, 2004.
* This research was supported by National Institutes of Health Grant GM-51310 (to C. R. H. R.). 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 National Institute of Health Grant 1 F32 AI-10613-01. Present address: Dept. of Biological Sciences, Louisiana State University, Baton Rouge, LA 70803.
Supported in part by the Duke University Cell and Molecular Biology training program (GM-07184).
¶ To whom correspondence should be addressed. Tel.: 919-684-5326; Fax: 919-684-8885; E-mail: raetz{at}biochem.duke.edu.
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