Polymer stability plays an important role in the positional regulation of FtsZ.
We conducted a series of experiments examining the effect of polymer stability on FtsZ localization dynamics in Bacillus subtilis. A loss-of-function mutation in ezrA, a putative polymer-destabilizing factor, suppresses the defects in FtsZ polymer stability associated with minCD overexpression. In addition, a mutation that is predicted to stabilize the FtsZ polymer leads to the formation of polar FtsZ rings. These data support the hypothesis that carefully balanced polymer stability is important for the assembly and localization of FtsZ during the bacterial cell cycle.
Levin
P A
PA
Department of Biology, Washington University, St. Louis, Missouri 63130, USA. plevin@biology.wustl.edu
Schwartz
R L
RL
Grossman
A D
AD
D000251:Adenosine Triphosphatases / Q000235:genetics / Q000378:metabolism; D000483:Alleles; D001412:Bacillus subtilis / Q000235:genetics / Q000254:growth & development* / Q000378:metabolism*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D003598:Cytoskeletal Proteins; D029968:Escherichia coli Proteins; D020558:GTP Phosphohydrolases / Q000235:genetics / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D006160:Guanosine Triphosphate / Q000378:metabolism; D009154:Mutation; D011108:Polymers / Q000737:chemistry*
D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; D029968:Escherichia coli Proteins; C121014:EzrA protein, Bacillus subtilis; C071525:FtsZ protein, Bacteria; C080466:MinC protein, Bacteria; D011108:Polymers; D006160:Guanosine Triphosphate; D000251:Adenosine Triphosphatases; D020558:GTP Phosphohydrolases; C072069:MinD protein, E coli