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.

• Klíčová slova
• Clostridioides difficile, DivIVA, cardiolipin, lipid membrane, phosphatidylglycerol,
• MeSH
• bakteriální proteiny metabolismus   MeSH
• buněčná membrána metabolismus   MeSH
• Clostridioides difficile růst a vývoj   metabolismus   MeSH
• kardiolipiny metabolismus   MeSH
• membránové lipidy metabolismus   MeSH
• proteiny buněčného cyklu metabolismus   MeSH
• transport proteinů MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• bakteriální proteiny MeSH
• DivIVA protein, bacteria MeSH Prohlížeč
• kardiolipiny MeSH
• membránové lipidy MeSH
• proteiny buněčného cyklu MeSH