DivIVA is a crucial membrane-binding protein that helps to localize other proteins to negatively curved membranes at cellular poles and division septa in Gram-positive bacteria. The N-terminal domain of DivIVA is responsible for membrane binding. However, to which lipids the domain binds or how it recognizes the membrane negative curvature remains elusive. Using computer simulations, we demonstrate that the N-terminal domain of Streptomyces coelicolor DivIVA adsorbs to membranes with affinity and orientation dependent on the lipid composition. The domain interacts non-specifically with lipid phosphates via its arginine-rich tip and the strongest interaction is with cardiolipin. Moreover, we observed a specific attraction between a negatively charged side patch of the domain and ethanolamine lipids, which addition caused the change of the domain orientation from perpendicular to parallel alignment to the membrane plane. Similar but less electrostatically dependent behavior was observed for the N-terminal domain of Bacillus subtilis. The domain propensity for lipids which prefer negatively curved membranes could be a mechanism for the cellular localization of DivIVA protein.

Department of Biology Lund University Sölvegatan 35 Lund 223 62 Sweden

Faculty of Science Masaryk University Kamenice 753 5 Brno 625 00 Czech Republic

Faculty of Science Masaryk University Kamenice 753 5 Brno 625 00 Czech Republic; CEITEC Central European Institute of Technology Masaryk University Kamenice 753 5 Brno 625 00 Czech Republic

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Cardiolipin-Containing Lipid Membranes Attract the Bacterial Cell Division Protein DivIVA