title: On the control of septation in Escherichia coli.
abstract: Mutants of E. coli defective in cell septation (ftsA to ftsG, conditional thermosensitive mutants isolated by Ricard and Hirota) were studied with respect to their membrane protein composition, murein hydrolase activities and rates of synthesis of murein and phospholipids. Three classes of mutants have been distinguished: 1) those affected in both murein and phospholipid synthesis; 2) those affected in either murein or phospholipid synthesis and 3) those affected in neither of these parameters. Overall murein hydrolase activities, after activation, is of the same order in all the mutants screened. In addition to soluble products of murein splitting, we have found insoluble products that appear to be in dynamic equilibrium with the murein of the sacculus. Endogenous levels of cyclic adenosine 3',5'-monophosphate measured after blocking septation showed no variation. This suggests that the cyclic nucleotide is not involved in the metabolic control of septation.
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D002473:Cell Wall / Q000378:metabolism; D000242:Cyclic AMP / Q000378:metabolism; D003960:Diaminopimelic Acid / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology / Q000254:growth & development* / Q000378:metabolism; D006579:Heterozygote; D006867:Hydrolases / Q000378:metabolism; D009154:Mutation; D010457:Peptidoglycan / Q000096:biosynthesis / Q000378:metabolism; D010743:Phospholipids / Q000096:biosynthesis / Q000378:metabolism; D013696:Temperature
chemical_list: D001426:Bacterial Proteins; D010457:Peptidoglycan; D010743:Phospholipids; D003960:Diaminopimelic Acid; D000242:Cyclic AMP; D006867:Hydrolases