title: Phospholipase activity in bacteriophage-infected Escherichia coli. III. Phopholipase A involvement in lysis of T4-infected cells.
abstract: Bacteriophage studies with Escherichia coli K-12 (gamma)DR-DS-, a mutant lacking the major known fatty acyl hydrolases (phospholipases), and its wild-type parent showed equivalent phage infection with regard to phage production and time of phage release. Further examination of the DR-DS- mutant, however, revealed that the progeny bacteriophage were released without complete dissolution of the host cell. Prolonged cell integrity of the infected mutant was noted by spectrophotometry and supported by direct microscope examination. The phage release occurred at normal "lysis" time with phage yields comparable to that of the wild-type bacteria. Inner membrane degradation was indicated by the release of beta-galactosidase, a cytoplasmic enzyme, and of trichloracetic acid-precipitable RNA. Thus, outer membrane degradation is required for dissolution of phage-infected cells, and this degradation is at least partly dependent on activation of host phospholipases.
mesh_terms: D001426:Bacterial Proteins / Q000378:metabolism; D001433:Bacteriolysis; D002462:Cell Membrane / Q000378:metabolism; D003090:Coliphages / Q000254:growth & development*; D004267:DNA Viruses; D004926:Escherichia coli / Q000201:enzymology* / Q000378:metabolism; D005696:Galactosidases / Q000378:metabolism; D008242:Lysogeny; D009088:Mucoproteins / Q000378:metabolism; D009154:Mutation; D010740:Phospholipases / Q000378:metabolism*; D014498:Uracil / Q000378:metabolism; D014779:Virus Replication
chemical_list: D001426:Bacterial Proteins; D009088:Mucoproteins; D014498:Uracil; D010740:Phospholipases; D005696:Galactosidases