Capsid localization of the bacteriophage P4 Psu protein.

Academic Article

Abstract

  • In addition to its polarity-suppressing activity, the Psu protein of bacteriophage P4 also serves to stabilize the capsid against heat treatment and binds externally to the phage capsid. However, the heat stability is lost upon purification of the virus, indicating a loss of Psu protein from the capsid. By using three-dimensional reconstruction from cryo-electron micrographs of P4 psu1 amber mutants lacking Psu, and of P4 virions, which have been saturated with Psu protein to regain heat stability, we have determined the position of this protein on the virus surface. Our results are consistent with the hypothesis that the function of Psu is to stabilize the hexameric capsomer assembly.
  • Authors

    Published In

  • Virology  Journal
  • Keywords

  • Capsid, Capsid Proteins, Coliphages, Cryopreservation, Defective Viruses, Image Processing, Computer-Assisted, Microscopy, Electron, Models, Structural, Mutation, Virion
  • Digital Object Identifier (doi)

    Author List

  • Dokland T; Isaksen ML; Fuller SD; Lindqvist BH
  • Start Page

  • 682
  • End Page

  • 687
  • Volume

  • 194
  • Issue

  • 2