Extracellular proteases modify cell wall turnover in Bacillus subtilis.
The rate of turnover of peptidoglycan in exponentially growing cultures of Bacillus subtilis was observed to be sensitive to extracellular protease. In protease-deficient mutants the rates of cell wall turnover were greater than that of wild-type strain 168, whereas hyperprotease-producing strains exhibited decreased rates of peptidoglycan turnover. The rate of peptidogylcan turnover in a protease-deficient strain was decreased when the mutant was grown in the presence of a hyperprotease-producing strain. The addition of phenylmethylsulfonyl fluoride, a serine protease inhibitor, to cultures of hyperprotease-producing strains increased their rates of cell wall turnover. Isolated cell walls of all protease mutants contained autolysin levels equal to or greater than that of wild-type strain 168. The presence of filaments, or cells with incomplete septa, was observed in hyperprotease-producing strains or when a protease-deficient strain was grown in the presence of subtilisin. The results suggest that the turnover of cell walls in B. subtilis may be regulated by extracellular proteases.
D001412:Bacillus subtilis / Q000166:cytology / Q000201:enzymology / Q000378:metabolism*; D001433:Bacteriolysis; D002458:Cell Fractionation; D002473:Cell Wall / Q000378:metabolism; D009154:Mutation; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism*; D010457:Peptidoglycan / Q000378:metabolism*; D010664:Phenylmethylsulfonyl Fluoride / Q000494:pharmacology; D013381:Subtilisins / Q000494:pharmacology
D010457:Peptidoglycan; D010664:Phenylmethylsulfonyl Fluoride; D010447:Peptide Hydrolases; D013381:Subtilisins; D009238:N-Acetylmuramoyl-L-alanine Amidase