Structural aberrations in T-even bacteriophage. VII. In vitro analysis of the canavanine-mediated inhibition of proteolytic cleavage.
Canavanine arrests a critical function in head morphogenesis and the potential for forming giant T-even phage particles termed lollipops is induced. Formation of the particles requires the addition of arginine and the restoration of normal functions. We now report on an investigation into the effects of canavanine on both the T4-induced proteolytic activity and on the substrate proteins. Using an in vitro cleavage assay we have shown that the gene 21-dependent proteolytic activity from canavanine-treated extracts is markedly inhibited, whereas the substrate proteins retain a high susceptibility for cleavage. The proteolytic activity in extracts treated with canavanine followed by arginine is readily detectable, and proteins previously synthesized in the presence of canavanine can be cleaved. Protein synthesis is apparently required for the appearance of the proteolytic activity after the canavanine-arginine treatment. Mixing experiments suggest the requirement for a component of the gene 21-dependent proteolytic activity that is not coded for by gene 21.
D001120:Arginine / Q000494:pharmacology; D002172:Canavanine / Q000494:pharmacology*; D002474:Cell-Free System; D003090:Coliphages / Q000254:growth & development* / Q000378:metabolism; D004267:DNA Viruses; D005796:Genes; D009024:Morphogenesis / Q000187:drug effects; D010447:Peptide Hydrolases / Q000378:metabolism*; D014764:Viral Proteins / Q000096:biosynthesis / Q000378:metabolism*
D014764:Viral Proteins; D002172:Canavanine; D001120:Arginine; D010447:Peptide Hydrolases