Septum formation in Escherichia coli: characterization of septal structure and the effects of antibiotics on cell division.
Septa can be demonstrated in sections of Escherichia coli strains B and B/r after fixation with acrolein and glutaraldehyde. The septum consists of an ingrowth of the cytoplasmic membrane and the mucopeptide layer; the outer membrane is excluded from the septum until the cells begin to separate. Mesosomes have also been observed. The septum is highly labile and, except in the chain-forming strains, E. coli D22 env A and CRT 97, not easily preserved by standard procedures. The labile nature of the septum may be due to the presence of autolysin(s) located at the presumptive division site. Blocking division by addition of ampicillin (2 to 5 mug/ml) to cells of E. coli B/r produces a bulge at the middle of the cells; bulge formation is stopped by addition of chloramphenicol. Cephalosporins also induce bulge formation but may stop cell elongation as well as division. Bulge formation, due to the presumed action of an autolysin(s), may be an initial step in the septation sequence when the mucopeptide is modified to allow construction of the septum. In a nonseptate filament-forming strain, PAT 84, which ceases to divide at 42 C, bulge formation only occurs in the presence of ampicillin at the time of a shift-down at 30 C or at 42 C in the presence of NaCl (0.25 to 0.34 M). Experiments with chloramphenicol suggest that the filaments are fully compartmentalized but fail to divide owing to the inactivation, rather than loss of synthesis, of an autolysin at 42 C.
D000171:Acrolein; D000667:Ampicillin / Q000494:pharmacology*; D001426:Bacterial Proteins; D001433:Bacteriolysis; D002455:Cell Division / Q000187:drug effects*; D002462:Cell Membrane; D002473:Cell Wall; D002512:Cephalothin / Q000494:pharmacology*; D002701:Chloramphenicol / Q000494:pharmacology*; D003594:Cytoplasmic Granules; D004926:Escherichia coli / Q000166:cytology* / Q000254:growth & development; D005613:Freeze Etching; D005976:Glutaral; D008854:Microscopy, Electron; D008954:Models, Biological; D009088:Mucoproteins; D009154:Mutation; D012965:Sodium Chloride / Q000494:pharmacology; D013053:Spectrophotometry; D013696:Temperature
D001426:Bacterial Proteins; D009088:Mucoproteins; D012965:Sodium Chloride; D002701:Chloramphenicol; D000171:Acrolein; D000667:Ampicillin; D002512:Cephalothin; D005976:Glutaral