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.

Basic information

Original name

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

Authors

LABAJOVA, N., N. BARANOVA, Miroslav JURÁSEK (203 Czech Republic, belonging to the institution), Robert VÁCHA (203 Czech Republic, guarantor, belonging to the institution), M. LOOSE and I. BARAK

Edition

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

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

Switzerland

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 6.208

RIV identification code

RIV/00216224:14740/21:00119690

Organization unit

Central European Institute of Technology

DOI

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

UT WoS

000681815400001

Keywords in English

Clostridioides difficile; DivIVA; lipid membrane; cardiolipin; phosphatidylglycerol

Abstract

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.

Links

GA20-20152S, research and development project

Name: Proteinová přitažlivost a selektivita pro buněčné membrány

Investor: Czech Science Foundation

LM2015085, research and development project

Name: CERIT Scientific Cloud (Acronym: CERIT-SC)

Investor: Ministry of Education, Youth and Sports of the CR, CERIT Scientific Cloud

LQ1601, research and development project

Name: CEITEC 2020 (Acronym: CEITEC2020)

Investor: Ministry of Education, Youth and Sports of the CR

90070, large research infrastructures

Name: IT4Innovations

Citovat

LABAJOVA, N., N. BARANOVA, Miroslav JURÁSEK, Robert VÁCHA, M. LOOSE and I. BARAK. Cardiolipin-Containing Lipid Membranes Attract the Bacterial Cell Division Protein DivIVA. International Journal of Molecular Sciences. Basel: Multidisciplinary Digital Publishing Institute, 2021, vol. 22, No 15, p. 8350-8370. ISSN 1422-0067. Available from: 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 and 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, vol.~22, No~15, p.~8350-8370. ISSN~1422-0067. Available from: https://dx.doi.org/10.3390/ijms22158350.

Detailed Information on Publication Record