title: Initiation of P22 procapsid assembly in vivo.
abstract: The procapsids of all double-stranded DNA phages have a unique portal vertex, which is the locus of DNA packaging and DNA injection. Procapsid assembly is also initiated at this vertex, which is defined by the presence of a cyclic dodecamer of the portal protein. Assembly of the procapsid shell of phage P22 requires the gene 5 coat protein and the gene 8 scaffolding protein. We report here that removal of gene product (gp) 1 portal protein of P22 by mutation does not slow the rate of polymerization of coat and scaffolding subunits into shells, indicating that the portal ring is dispensable for shell initiation. Mutant scaffolding subunits specified by tsU172 copolymerize with coat subunits into procapsids at restrictive temperature, and also correctly autoregulate their synthesis. However, the shell structures formed from the temperature-sensitive scaffolding subunits fail to incorporate the portal ring and the three minor DNA injection proteins. This mutation identifies a domain of the scaffolding protein specifically involved in organization of the portal vertex. The results suggest that it is a complex of the scaffolding protein that initiates procapsid assembly and organizes the portal ring.
authors.affiliation: Department of Biology, MIT Cambridge 02139.
authors.forename: C
authors.initials: C
authors.lastname: Bazinet
authors.forename: J
authors.initials: J
authors.lastname: King
mesh_terms: D002213:Capsid / Q000502:physiology*; D002499:Centrifugation, Density Gradient; D009024:Morphogenesis; D009154:Mutation; D012483:Salmonella Phages / Q000254:growth & development*; D012588:Scintillation Counting; D014764:Viral Proteins / Q000502:physiology
chemical_list: D014764:Viral Proteins