Mutants of Streptococcus pneumoniae that contain a temperature-sensitive autolysin.
Two mutants of Streptococcus pneumoniae deficient in autolysin activity produced a protein that showed immunological identity with the N-acetyl-muramyl-L-alanyl-amidase present in the wild-type strain, when tested with antiserum obtained against this enzyme. The protein was produced by the mutant cultures grown either at 37 degrees C or at 30 degrees C, although only the cell extracts obtained at 30 degrees C showed significant cell wall hydrolysing activity. In contrast to the lysis resistance of these bacteria grown at 37 degrees C, mutant cultures grown at 30 degrees C exhibited significant degrees of autolysis when treated with detergent or cell wall inhibitors. Extracts of the mutant cultures contained a cell wall hydrolysing activity that was rapidly inactivated during incubation at 37 degrees C.
D000581:Amidohydrolases / Q000032:analysis*; D001433:Bacteriolysis; D005779:Immunodiffusion; D009154:Mutation; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000032:analysis*; D010400:Penicillin G / Q000378:metabolism; D013296:Streptococcus pneumoniae / Q000032:analysis / Q000235:genetics* / Q000378:metabolism; D013696:Temperature
D000581:Amidohydrolases; D009238:N-Acetylmuramoyl-L-alanine Amidase; D010400:Penicillin G