University of Cambridge > Talks.cam > Bacteriophage 2017 > A novel role for phage P22’s scaffolding protein: triggering portal ring oligomerization and incorporation during procapsid assembly

A novel role for phage P22’s scaffolding protein: triggering portal ring oligomerization and incorporation during procapsid assembly

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  • UserDr. Tina Motwani, University of Connecticut, Storrs, United States
  • ClockTuesday 17 January 2017, 16:00-16:30
  • HouseOnline.

If you have a question about this talk, please contact Ilana Spilka.

The majority of DNA viruses package their genomes into preformed precursor capsids through a portal protein complex incorporated in the capsid at a single vertex. The existence of a unique portal complex is crucial to the formation of mature infectious virions, but how only one portal assembly is selectively incorporated at a special vertex is unclear. Here, we show incorporation of bacteriophage P22 portal protein into PC in vitro as pre-assembled dodecameric rings. A novel role for the scaffolding protein in triggering portal ring formation from portal monomers was also found. Thus, new details are revealed about this critical step in the assembly of icosahedral viruses that use a portal protein in conjunction with a genome-packaging motor to encapsulate their genetic material.

This talk is part of the Bacteriophage 2017 series.

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