Effect of membrane composition on DivIVA-membrane interaction.

J 2020

Effect of membrane composition on DivIVA-membrane interaction.

JURÁSEK, Miroslav; Klas FLÄRDH a Robert VÁCHA

Základní údaje

Originální název

Effect of membrane composition on DivIVA-membrane interaction.

Autoři

JURÁSEK, Miroslav (203 Česká republika, domácí); Klas FLÄRDH (752 Švédsko) a Robert VÁCHA (203 Česká republika, garant, domácí)

Vydání

BBA Biomembranes, Amsterdam, Elsevier, 2020, 0005-2736

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.747

Kód RIV

RIV/00216224:14740/20:00114560

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1016/j.bbamem.2019.183144

UT WoS

000537573200001

EID Scopus

2-s2.0-85076861655

Klíčová slova anglicky

DivIVA protein; Lipid membrane; Molecular dynamics; Negative curvature; Lipid preference; N-terminal domain

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 15. 3. 2021 18:51, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

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.

Návaznosti

GA17-11571S, projekt VaV

Název: Amfifilní peptidy na fosfolipidových membránách

Investor: Grantová agentura ČR, Amphiphilic Peptides at Phospholipid Membranes

LM2015085, projekt VaV

Název: CERIT Scientific Cloud (Akronym: CERIT-SC)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CERIT Scientific Cloud

LQ1601, projekt VaV

Název: CEITEC 2020 (Akronym: CEITEC2020)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC 2020

MUNI/G/1100/2016, interní kód MU

Název: Computational chemistry for Wnt signaling pathway

Investor: Masarykova univerzita, Computational chemistry for Wnt signaling pathway, INTERDISCIPLINARY - Mezioborové výzkumné projekty

Citovat

JURÁSEK, Miroslav; Klas FLÄRDH a Robert VÁCHA. Effect of membrane composition on DivIVA-membrane interaction. 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.

@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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