Identification and characterization of a negative regulator of FtsZ ring formation in Bacillus subtilis.
During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. We have identified a regulator of FtsZ ring formation in Bacillus subtilis. This protein, EzrA, modulates the frequency and position of FtsZ ring formation. The loss of ezrA resulted in cells with multiple FtsZ rings located at polar as well as medial sites. Moreover, the critical concentration of FtsZ required for ring formation was lower in ezrA null mutants than in wild-type cells. EzrA was associated with the cell membrane and also colocalized with FtsZ to the nascent septal site. We propose that EzrA interacts either with FtsZ or with one of its binding partners to promote depolymerization.
Levin
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Department of Biology, Building 68-530, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Kurtser
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Grossman
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D000483:Alleles; D001412:Bacillus subtilis / Q000378:metabolism* / Q000502:physiology; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002455:Cell Division; D002462:Cell Membrane / Q000378:metabolism; D002874:Chromosome Mapping; D003598:Cytoskeletal Proteins; D008856:Microscopy, Fluorescence; D016366:Open Reading Frames; D011108:Polymers / Q000378:metabolism; D011487:Protein Conformation; D013171:Spores, Bacterial; D013696:Temperature
D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C121014:EzrA protein, Bacillus subtilis; C071525:FtsZ protein, Bacteria; D011108:Polymers