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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

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
PubMed

Insights

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.

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