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

J 2021

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

LABAJOVA, N.; N. BARANOVA; Miroslav JURÁSEK; Robert VÁCHA; M. LOOSE et. al.

Základní údaje

Originální název

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

Autoři

LABAJOVA, N.; N. BARANOVA; Miroslav JURÁSEK (203 Česká republika, domácí); Robert VÁCHA (203 Česká republika, garant, domácí); M. LOOSE a I. BARAK

Vydání

International Journal of Molecular Sciences, Basel, Multidisciplinary Digital Publishing Institute, 2021, 1422-0067

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Švýcarsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Kód RIV

RIV/00216224:14740/21:00119690

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.3390/ijms22158350

UT WoS

000681815400001

EID Scopus

2-s2.0-85111971816

Klíčová slova anglicky

Clostridioides difficile; DivIVA; lipid membrane; cardiolipin; phosphatidylglycerol

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 5. 5. 2022 16:23, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

DivIVA is a protein initially identified as a spatial regulator of cell division in the model organism Bacillus subtilis, but its homologues are present in many other Gram-positive bacteria, including Clostridia species. Besides its role as topological regulator of the Min system during bacterial cell division, DivIVA is involved in chromosome segregation during sporulation, genetic competence, and cell wall synthesis. DivIVA localizes to regions of high membrane curvature, such as the cell poles and cell division site, where it recruits distinct binding partners. Previously, it was suggested that negative curvature sensing is the main mechanism by which DivIVA binds to these specific regions. Here, we show that Clostridioides difficile DivIVA binds preferably to membranes containing negatively charged phospholipids, especially cardiolipin. Strikingly, we observed that upon binding, DivIVA modifies the lipid distribution and induces changes to lipid bilayers containing cardiolipin. Our observations indicate that DivIVA might play a more complex and so far unknown active role during the formation of the cell division septal membrane.

Návaznosti

GA20-20152S, projekt VaV

Název: Proteinová přitažlivost a selektivita pro buněčné membrány

Investor: Grantová agentura ČR, Protein Affinity and Selectivity to Cellular 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

90070, velká výzkumná infrastruktura

Název: IT4Innovations

Citovat

LABAJOVA, N.; N. BARANOVA; Miroslav JURÁSEK; Robert VÁCHA; M. LOOSE a I. BARAK. Cardiolipin-Containing Lipid Membranes Attract the Bacterial Cell Division Protein DivIVA. International Journal of Molecular Sciences. Basel: Multidisciplinary Digital Publishing Institute, 2021, roč. 22, č. 15, s. 8350-8370. ISSN 1422-0067. Dostupné z: https://dx.doi.org/10.3390/ijms22158350.

@article{1838601,
   author = {Labajova, N. and Baranova, N. and Jurásek, Miroslav and Vácha, Robert and Loose, M. and Barak, I.},
   article_location = {Basel},
   article_number = {15},
   doi = {http://dx.doi.org/10.3390/ijms22158350},
   keywords = {Clostridioides difficile; DivIVA; lipid membrane; cardiolipin; phosphatidylglycerol},
   language = {eng},
   issn = {1422-0067},
   journal = {International Journal of Molecular Sciences},
   title = {Cardiolipin-Containing Lipid Membranes Attract the Bacterial Cell Division Protein DivIVA},
   url = {https://www.mdpi.com/1422-0067/22/15/8350},
   volume = {22},
   year = {2021}
}

TY  - JOUR
ID  - 1838601
AU  - Labajova, N. - Baranova, N. - Jurásek, Miroslav - Vácha, Robert - Loose, M. - Barak, I.
PY  - 2021
TI  - Cardiolipin-Containing Lipid Membranes Attract the Bacterial Cell Division Protein DivIVA
JF  - International Journal of Molecular Sciences
VL  - 22
IS  - 15
SP  - 8350
EP  - 8350
PB  - Multidisciplinary Digital Publishing Institute
SN  - 14220067
KW  - Clostridioides difficile
KW  - DivIVA
KW  - lipid membrane
KW  - cardiolipin
KW  - phosphatidylglycerol
UR  - https://www.mdpi.com/1422-0067/22/15/8350
N2  - DivIVA is a protein initially identified as a spatial regulator of cell division in the model organism Bacillus subtilis, but its homologues are present in many other Gram-positive bacteria, including Clostridia species. Besides its role as topological regulator of the Min system during bacterial cell division, DivIVA is involved in chromosome segregation during sporulation, genetic competence, and cell wall synthesis. DivIVA localizes to regions of high membrane curvature, such as the cell poles and cell division site, where it recruits distinct binding partners. Previously, it was suggested that negative curvature sensing is the main mechanism by which DivIVA binds to these specific regions. Here, we show that Clostridioides difficile DivIVA binds preferably to membranes containing negatively charged phospholipids, especially cardiolipin. Strikingly, we observed that upon binding, DivIVA modifies the lipid distribution and induces changes to lipid bilayers containing cardiolipin. Our observations indicate that DivIVA might play a more complex and so far unknown active role during the formation of the cell division septal membrane.
ER  -

LABAJOVA, N.; N. BARANOVA; Miroslav JURÁSEK; Robert VÁCHA; M. LOOSE a I. BARAK. Cardiolipin-Containing Lipid Membranes Attract the Bacterial Cell Division Protein DivIVA. \textit{International Journal of Molecular Sciences}. Basel: Multidisciplinary Digital Publishing Institute, 2021, roč.~22, č.~15, s.~8350-8370. ISSN~1422-0067. Dostupné z: https://dx.doi.org/10.3390/ijms22158350.

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