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Papers In Press, published online ahead of print July 25, 2003
J. Biol. Chem, 10.1074/jbc.M306876200
Submitted on June 27, 2003
Revised on July 25, 2003
Accepted on July 25, 2003

The MinD membrane targeting sequence is a transplantable lipid-binding helixi

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

Department of Biochemistry, University of Connecticut Health Center, Farmington, CT 06032

Corresponding Author: glenn{at}psel.uchc.edu

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 in order to regulate the reversible membrane association of E. coli MinD during its pole-to-pole oscillation cycle.nk


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