Novel second-site suppression of a cold-sensitive defect in phage P22 procapsid assembly.

@article{Bazinet1990NovelSS,
  title={Novel second-site suppression of a cold-sensitive defect in phage P22 procapsid assembly.},
  author={C. Bazinet and R. Villafane and J. King},
  journal={Journal of molecular biology},
  year={1990},
  volume={216 3},
  pages={
          701-16
        }
}
The DNA packaging portal of the phage P22 procapsid is formed of 12 molecules of the 90,000 dalton gene 1 protein. The assembly of this dodecameric complex at a unique capsid vertex requires scaffolding subunits. The mechanism that ensures the location of the 12-fold symmetrical portal at only one of the 12 5-fold vertices of an icosahedral virus capsid presents a unique assembly problem, which, in some viruses, is solved by the portal also acting as initiator of procapsid assembly. Phage P22… Expand
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