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The MinD membrane targeting sequence is a transplantable lipid-binding helix.
Tim H Szeto1, Susan L Rowland, Cheryl L Habrukowich
1Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06032, USA.
The Journal of Biological Chemistry
|July 29, 2003
Summary
The MinD membrane targeting sequence (MTS) is a transplantable motif that binds anionic phospholipids. Its evolutionary tuning optimizes bacterial cell division site selection.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- MinD is an ATPase essential for bacterial cell division site selection.
- MinD's membrane localization is mediated by a C-terminal membrane targeting sequence (MTS).
- The MTS is an 8-12 amino acid motif.
Purpose of the Study:
- To investigate the MinD MTS as a transplantable lipid-binding motif.
- To understand the interaction of MTS with lipid bilayers.
- To explore the evolutionary tuning of MTS for specific bacterial roles.
Main Methods:
- Demonstration of MTS as a heterologous protein targeting motif.
- Analysis of MTS interaction with lipid bilayers.
- Investigation of phospholipid preference and membrane affinity.
Main Results:
- The MinD MTS is a transplantable motif that targets proteins to the cell membrane.
- MTS interacts with lipid bilayers as an amphipathic helix, preferring anionic phospholipids.
- MTS phospholipid preference and membrane affinity are evolutionarily tuned to bacterial roles.
Conclusions:
- The MinD MTS is a versatile, transplantable lipid-binding motif.
- Evolutionary adaptation of MTS optimizes its function in diverse bacteria.
- A model for MTS-ATP binding coupling in MinD oscillation is proposed.