Structural inhibition and reactivation of Escherichia coli septation by elements of the SOS and TER pathways.
The inhibition of cell division caused by induction of the SOS pathway in Escherichia coli structurally blocks septation, as deduced from two sets of results. Potential septation sites active at the time of SOS induction became inactivated, while those initiated during the following doubling time were active. Penicillin resistance increased in wild-type UV light-irradiated cells, a behavior similar to that observed in mutants in which structural blocks were introduced by inactivation of FtsA. Potential septation sites that have been structurally blocked by either the SOS division inhibitor, furazlocillin inhibition of PBP3, or inactivation of a TER pathway component, FtsA3, could be reactivated one doubling time after removal of the inhibitory agent in the presence of an active lon gene product. Reactivation of potential septation sites blocked by the presence of an inactivated FtsA3 was significantly lower when the lon protease was not active, suggesting that Lon plays a role in the removal of inactivated TER pathway products from the blocked potential septation sites.
D049069:ATP-Dependent Proteases; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D002352:Carrier Proteins; D002455:Cell Division; D004260:DNA Repair; D010450:Endopeptidases / Q000378:metabolism; D004926:Escherichia coli / Q000166:cytology* / Q000187:drug effects / Q000235:genetics; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D006360:Heat-Shock Proteins; D006602:Hexosyltransferases / Q000378:metabolism; D009097:Multienzyme Complexes / Q000378:metabolism; D002267:Muramoylpentapeptide Carboxypeptidase; D010400:Penicillin G / Q000494:pharmacology; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases / Q000378:metabolism; D049070:Protease La; D013014:SOS Response, Genetics; D012697:Serine Endopeptidases; D014466:Ultraviolet Rays
D001426:Bacterial Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D009097:Multienzyme Complexes; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D010450:Endopeptidases; D002267:Muramoylpentapeptide Carboxypeptidase; D049069:ATP-Dependent Proteases; D012697:Serine Endopeptidases; C483567:Lon protein, E coli; D049070:Protease La; D010400:Penicillin G