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J Biol Chem. 2013 Sep 13;288(37):26625-34. doi: 10.1074/jbc.M113.491688. Epub 2013 Aug 6.

Bacterial division proteins FtsZ and ZipA induce vesicle shrinkage and cell membrane invagination.

Author information

1
From the Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas (CIB-CSIC), 28040 Madrid, Spain.

Abstract

Permeable vesicles containing the proto-ring anchoring ZipA protein shrink when FtsZ, the main cell division protein, polymerizes in the presence of GTP. Shrinkage, resembling the constriction of the cytoplasmic membrane, occurs at ZipA densities higher than those found in the cell and is modulated by the dynamics of the FtsZ polymer. In vivo, an excess of ZipA generates multilayered membrane inclusions within the cytoplasm and causes the loss of the membrane function as a permeability barrier. Overproduction of ZipA at levels that block septation is accompanied by the displacement of FtsZ and two additional division proteins, FtsA and FtsN, from potential septation sites to clusters that colocalize with ZipA near the membrane. The results show that elementary constriction events mediated by defined elements involved in cell division can be evidenced both in bacteria and in vesicles.

KEYWORDS:

Bacterial Membrane; Cell Division; Escherichia coli; FtsZ; Giant Vesicles; Membrane Function; Protein-Protein Interactions; Synthetic Biology; ZipA

PMID:
23921390
PMCID:
PMC3772209
DOI:
10.1074/jbc.M113.491688
[Indexed for MEDLINE]
Free PMC Article
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