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@article{1707177,
author = {Jurásek, Miroslav and Flärdh, Klas and Vácha, Robert},
article_location = {Amsterdam},
article_number = {8},
doi = {http://dx.doi.org/10.1016/j.bbamem.2019.183144},
keywords = {DivIVA protein; Lipid membrane; Molecular dynamics; Negative curvature; Lipid preference; N-terminal domain},
language = {eng},
issn = {0005-2736},
journal = {BBA Biomembranes},
title = {Effect of membrane composition on DivIVA-membrane interaction.},
url = {https://doi.org/10.1016/j.bbamem.2019.183144},
volume = {1862},
year = {2020}
}
TY - JOUR
ID - 1707177
AU - Jurásek, Miroslav - Flärdh, Klas - Vácha, Robert
PY - 2020
TI - Effect of membrane composition on DivIVA-membrane interaction.
JF - BBA Biomembranes
VL - 1862
IS - 8
SP - 1-9
EP - 1-9
PB - Elsevier
SN - 00052736
KW - DivIVA protein
KW - Lipid membrane
KW - Molecular dynamics
KW - Negative curvature
KW - Lipid preference
KW - N-terminal domain
UR - https://doi.org/10.1016/j.bbamem.2019.183144
L2 - https://doi.org/10.1016/j.bbamem.2019.183144
N2 - 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.
ER -
JURÁSEK, Miroslav, Klas FLÄRDH a Robert VÁCHA. Effect of membrane composition on DivIVA-membrane interaction. \textit{BBA Biomembranes}. Amsterdam: Elsevier, 2020, roč.~1862, č.~8, s.~1-9. ISSN~0005-2736. Dostupné z: https://dx.doi.org/10.1016/j.bbamem.2019.183144.
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