Impairment of cell division in tolA mutants of Escherichia coli at low and high medium osmolarities.
Mutations in the tolA gene of Escherichia coli cause the cell to become sensitive to detergents and to some antibiotics, to release periplasmic enzymes and to be resistant to group A colicins; tolA mutations also lead to mucoid phenotype. TolA is a three-domain protein anchored in the inner membrane by its N-terminal domain. The second domain is proposed to span the periplasmic space and to interact with trimeric porins of the outer membrane. TolA proteins are considered to be located in the adhesion zones between inner and outer membranes. Our observations by confocal and electron microscopy have revealed that tolA mutants show modified morphology and produce DNA-free cells. Increasing or decreasing medium osmolarity amplifies these defects; mutants become essentially unable to locate the division site properly so that cells of highly unequal lengths are produced. Moreover, septation is impaired with asymmetric constrictions and oblique septa. These results suggest that TolA could play a role in positioning the division sites via the organisation of either the outer membrane or the possible adhesion zones.
D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000235:genetics / Q000502:physiology*; D001692:Biological Transport; D003470:Culture Media / Q000494:pharmacology*; D004926:Escherichia coli / Q000166:cytology / Q000187:drug effects* / Q000235:genetics; D029968:Escherichia coli Proteins; D008854:Microscopy, Electron; D009994:Osmolar Concentration; D010641:Phenotype