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

Investor logo

Warning

This publication doesn't include Faculty of Medicine. It includes Central European Institute of Technology. Official publication website can be found on muni.cz.

Authors

LABAJOVA N. BARANOVA N. JURÁSEK Miroslav VÁCHA Robert LOOSE M. BARAK I.

Year of publication 2021
Type Article in Periodical
Magazine / Source International Journal of Molecular Sciences
MU Faculty or unit

Central European Institute of Technology

Citation
Web https://www.mdpi.com/1422-0067/22/15/8350
Doi http://dx.doi.org/10.3390/ijms22158350
Keywords Clostridioides difficile; DivIVA; lipid membrane; cardiolipin; phosphatidylglycerol
Description 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.
Related projects:

You are running an old browser version. We recommend updating your browser to its latest version.

More info