The dodecahedral framework of the bacteriophage phi 6 nucleocapsid is composed of protein P1.
The outer layer of the bacteriophage phi 6 nucleocapsid (NC) was removed by EDTA and reassociated with the core in the presence of Ca2+ or Mg2+. The core was relatively inaccessible to trypsin digestion, was composed of protein P1, and was in the dodecahedral framework reported previously. (H.T. Steely, Jr., and D. Lang, J. Virol. 51:479-483, 1984; Y. Yang and D. Lang, J. Virol. 51:484-488, 1984). The double-stranded RNA genome became RNase sensitive after EDTA treatment of the nucleocapsid.
D001435:Bacteriophages / Q000648:ultrastructure*; D002213:Capsid / Q000502:physiology*; D002413:Cations, Divalent / Q000502:physiology; D012321:DNA-Directed RNA Polymerases / Q000502:physiology; D004492:Edetic Acid; D008854:Microscopy, Electron; D008970:Molecular Weight; D009024:Morphogenesis; D011549:Pseudomonas; D014357:Trypsin; D014758:Viral Core Proteins / Q000502:physiology*; D014764:Viral Proteins / Q000502:physiology*
D002413:Cations, Divalent; D014758:Viral Core Proteins; D014764:Viral Proteins; D004492:Edetic Acid; D012321:DNA-Directed RNA Polymerases; D014357:Trypsin