Novel mechanism of cell division inhibition associated with the SOS response in Escherichia coli.
Certain Escherichia coli strains were shown to possess a novel system of cell division inhibition, called the SfiC+ phenotype. SfiC+ filamentation had a number of properties similar to those of sfiA-dependent division inhibition previously described: (i) both are associated with the SOS response induced by expression of the recA(Tif) mutation, (ii) both are associated with cell death, (iii) both are amplified in mutants lacking the Lon protease, and (iv) both are suppressed by sfiB mutations. SfiC+ filamentation and sfiA-dependent division inhibition differed in (i) the physiological conditions under which loss of viability is observed, (ii) the extent of amplification in lon mutants, (iii) their genetic regulation (SfiC+ filamentation is not under direct negative control of the LexA repressor), and (iv) their genetic determinants (SfiC+ filamentation depends on a locus, sfiC+, near 28 min on the E. coli map and distinct from sfiA).
D049069:ATP-Dependent Proteases; D002455:Cell Division; D004261:DNA Replication; D010450:Endopeptidases / Q000502:physiology; D004926:Escherichia coli / Q000166:cytology* / Q000235:genetics; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D006360:Heat-Shock Proteins; D009154:Mutation; D049070:Protease La; D011938:Rec A Recombinases / Q000235:genetics* / Q000502:physiology; D012697:Serine Endopeptidases; D013696:Temperature
D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D011938:Rec A Recombinases; D010450:Endopeptidases; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; C483567:Lon protein, E coli; D049070:Protease La