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Effect of membrane composition on DivIVA-membrane interaction.

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F20%3A00114560" target="_blank" >RIV/00216224:14740/20:00114560 - isvavai.cz</a>

  • Result on the web

    <a href="https://doi.org/10.1016/j.bbamem.2019.183144" target="_blank" >https://doi.org/10.1016/j.bbamem.2019.183144</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1016/j.bbamem.2019.183144" target="_blank" >10.1016/j.bbamem.2019.183144</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Effect of membrane composition on DivIVA-membrane interaction.

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2020

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    BBA Biomembranes

  • ISSN

    0005-2736

  • e-ISSN

    1879-2642

  • Volume of the periodical

    1862

  • Issue of the periodical within the volume

    8

  • Country of publishing house

    NL - THE KINGDOM OF THE NETHERLANDS

  • Number of pages

    9

  • Pages from-to

    1-9

  • UT code for WoS article

    000537573200001

  • EID of the result in the Scopus database

    2-s2.0-85076861655