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J. Biol. Chem., Vol. 278, Issue 41, 40050-40056, October 10, 2003

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The MinD Membrane Targeting Sequence Is a Transplantable Lipid-binding Helix^*

Tim H. Szeto , Susan L. Rowland , Cheryl L. Habrukowich  and Glenn F. King   ¶

From the Departments of Biochemistry and Microbiology, University of Connecticut Health Center, Farmington, Connecticut 06032

MinD is a ubiquitous ATPase that plays a crucial role in selection of the division site in eubacteria, chloroplasts, and probably also Archaea. It was recently demonstrated that membrane localization of MinD is mediated by an 8–12-residue C-terminal motif termed the membrane targeting sequence or MTS. In this study we show that the MinD MTS is a transplantable lipid-binding motif that can effectively target heterologous proteins to the cell membrane. We demonstrate that eubacterial MTSs interact directly with lipid bilayers as an amphipathic helix, with a distinct preference for anionic phospholipids. Moreover, we provide evidence that the phospholipid preference of each MTS, as well as its affinity for biological membranes, has been evolutionarily "tuned" to its specific role in different bacteria. We propose a model to describe how the MTS is coupled to ATP binding to regulate the reversible membrane association of Escherichia coli MinD during its pole-to-pole oscillation cycle.

Received for publication, June 27, 2003 , and in revised form, July 25, 2003.

Note Added in Proof—Following acceptance of this manuscript, a complementary study was published that provides further experimental support for our proposal that the MinD membrane targeting sequence interacts with lipid bilayers as an amphipathic helix (Zhou, H., and Lutkenhaus, J. (2003) J. Bacteriol. 185, 4326–4335). However, the two studies propose different molecular mechanisms for the reversible membrane association of E. coli MinD.

^* This work was supported by NIAID National Institutes of Health Grant AI-048583 (to G. F. K.). 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.

^¶ To whom correspondence should be addressed: Dept. of Biochemistry, University of Connecticut Health Center, 263 Farmington Ave., Farmington CT 06032-3305. Tel.: 860-679-8364; Fax: 860-679-1652; E-mail: glenn{at}psel.uchc.edu.

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