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Are phospholipid domains important for functioning of the Min system in Escherichia coli?



Are phospholipid domains important for functioning of the Min system in Escherichia coli?



Abstracts of the General Meeting of the American Society for Microbiology 102: 256



Previously utilizing 10-N-nonyl acridine orange (NAO) as a tag for cardiolipin (CL), we visualized CL domains at the poles and septal areas of E. coli cells. We suggested that these domains are involved in marking the division site. The MinCDE system in E. coli undergoes rapid oscillations moving from cell pole to pole to prevent the placement of the division site at the poles. Oscillation occurs in a similar manner in division mutants but within segments of the filamentous cells. Using a low concentration of NAO (50 nM) that does not inhibit cell growth, we investigated the possibility that CL domains also oscillate along the membrane in concert with MinD. However, no CL-domain oscillation was observed. Moreover, CL domains were observed in a minCDE deletion mutant, indicating that the Min system is not required for CL-domain formation. On the other hand the CL domains may be important for self-assembly of the membrane-associated component of the Min system, MinD, into size-limited two-dimensional lattice structures. We examined the behavior of a GFP-MinD fusion in a phosphatidylethanolamine (PE)-lacking filamentous mutant of E. coli. Previously, we demonstrated that the lack of PE did not prevent localization of FtsZ, FtsA and ZipA in these cells, but the proteins often formed aberrant spiral structures. The change in PL composition did not block the movement of GFP-MinD, but strongly decreased its rate. Other characteristics of GFP-MinD assembly and migration were also changed compared with those in filamentous cells with wild type PL composition. In PE-lacking cells GFP-MinD was organized in a "zigzag" pattern of compact spots along the filamentous cells. The spots appeared and disappeared in an apparently random manner, although a spiral trajectory might be an explanation for their movement. In PE-lacking filaments, CL domains often exhibit a similar zigzag pattern of localization. We suggest that the change in PL composition and the CL-domain pattern of localization in the membrane results in an alteration of MinD assembly-disassembly, and as a consequence, in an alteration of the trajectory of Min system movement.

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Accession: 034438151

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