title: Baseplate protein of bacteriophage T4 with both structural and lytic functions.
abstract: Analyses of a new bacteriophage T4 mutant that permits lysis of infected cells in the absence of e lysozyme showed that the strain carried a suppressor mutation in gene 5, a gene whose polypeptide product (gp5) is an integral component of the virion baseplate. Indirect experiments indicated that cell lysis was caused by the lytic action of mutant gp5. With regard to the physiological role of normal gp5, we speculate that it functions in the initiation of infection by catalyzing local cell wall digestion to facilitate penetration of the tail tube through the cell envelope. The proposed lytic activity of gp5 may also be responsible for the well-known phenomenon of lysis from without observed with T4.
mesh_terms: D001433:Bacteriolysis; D004926:Escherichia coli; D005814:Genes, Viral; D009113:Muramidase / Q000235:genetics; D009154:Mutation; D013489:Suppression, Genetic; D013604:T-Phages / Q000235:genetics / Q000254:growth & development / Q000502:physiology*; D010948:Viral Plaque Assay; D014764:Viral Proteins / Q000502:physiology*
chemical_list: D014764:Viral Proteins; D009113:Muramidase