title: Characterization of ftsZ mutations that render Bacillus subtilis resistant to MinC.
abstract: BACKGROUND
  Cell division in Bacillus subtilis occurs precisely at midcell. Positional control of cell division is exerted by two mechanisms: nucleoid occlusion, through Noc, which prevents division through nucleoids, and the Min system, where the combined action of the MinC, D and J proteins prevents formation of the FtsZ ring at cell poles or recently completed division sites.
  
  
  RESULTS
  We used a genetic screen to identify mutations in ftsZ that confer resistance to the lethal overexpression of the MinC/MinD division inhibitor. The FtsZ mutants were purified and found to polymerize to a similar or lesser extent as wild type FtsZ, and all mutants displayed reduced GTP hydrolysis activity indicative of a reduced polymerization turnover. We found that even though the mutations conferred in vivo resistance to MinC/D, the purified FtsZ mutants did not display strong resistance to MinC in vitro.
  
  
  CONCLUSIONS
  Our results show that in B. subtilis, overproduction of MinC can be countered by mutations that alter FtsZ polymerization dynamics. Even though it would be very likely that the FtsZ mutants found depend on other Z-ring stabilizing proteins such as ZapA, FtsA or SepF, we found this not to be the case. This indicates that the cell division process in B. subtilis is extremely robust.
authors: Bacterial Membrane Proteomics Laboratory, Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal.
authors: Inês Filipa Fernandes
authors: IF
authors: de Oliveira
authors: Anabela
authors: A
authors: de Sousa Borges
authors: Viola
authors: V
authors: Kooij
authors: Jeremy
authors: J
authors: Bartosiak-Jentys
authors: Joen
authors: J
authors: Luirink
authors: Dirk-Jan
authors: DJ
authors: Scheffers
mesh_terms: D001412:Bacillus subtilis / Q000166:cytology / Q000235:genetics* / Q000378:metabolism*; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D002455:Cell Division; D003598:Cytoskeletal Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D009154:Mutation; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary
chemical_list: D001426:Bacterial Proteins; D003598:Cytoskeletal Proteins; C071525:FtsZ protein, Bacteria; C080466:MinC protein, Bacteria