Cell-division control in Escherichia coli: specific induction of the SOS function SfiA protein is sufficient to block septation.
Blocks in DNA replication cause a rapid arrest of cell division in Escherichia coli. We have previously established that the function SfiA (SulA), induced under these conditions as part of the SOS response, is involved in this inhibition of division. To separate the effects of SfiA from those of other SOS functions, we have constructed a plac-sfiA operon fusion, permitting specific induction of SfiA protein by addition of the lac operon inducer isopropyl beta-D-thiogalactopyranoside (IPTG). In lon mutants, in which the unstable SfiA protein has a longer half-life, IPTG caused a rapid arrest of cell division. Under these conditions, there is no concomitant induction of the SOS response. IPTG also caused a rapid arrest of cell division in lon+ strains. These results demonstrate that induction of the SfiA protein is sufficient to cause inhibition of division. Mutations in the sfiB gene can suppress IPTG-induced SfiA-mediated inhibition of division. At higher SfiA concentrations, however, even sfiB mutants cease division; an additional mutation genetically inseparable from sfiB restores normal division. These observations reinforce the hypothesis that the SfiB protein, probably required for cell septation, is the target of action of the SfiA division inhibitor.
D001426:Bacterial Proteins / Q000096:biosynthesis*; D002455:Cell Division; D004261:DNA Replication / Q000187:drug effects; D004926:Escherichia coli / Q000166:cytology* / Q000235:genetics; D007544:Isopropyl Thiogalactoside / Q000494:pharmacology; D009154:Mutation; D009876:Operon
D001426:Bacterial Proteins; D007544:Isopropyl Thiogalactoside