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

The Journal of Biological Chemistry
Tim H SzetoGlenn F King

Abstract

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.

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Related Concepts

ATP Binding
Establishment and Maintenance of Localization
Biological Membrane
Molecular Helix
Alkalescens-Dispar Group
Carboxy-Terminal Amino Acid
Chimeric Proteins, Recombinant
Adenosine Triphosphatases
Helix (Snails)
Archaea

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