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T7 ejectosome assembly: A story unfolds.

Sebastian Leptihn1, Julia Gottschalk1, Andreas Kuhn1

  • 1Institute of Microbiology and Molecular Biology, University of Hohenheim , Stuttgart, Germany.

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Summary

Bacteriophage T7 DNA ejection relies on viral proteins gp15 and gp16 forming an ejectosome. These proteins undergo unfolding and refolding to create a channel for DNA translocation across the host cell envelope.

Keywords:
CD spectroscopyT7 phagedynamicsejectosomefluorescencegp15gp16hydrophobicitylipid bindingprotein foldingprotein hydrationprotein structure

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Virology

Background:

  • T7 phage DNA translocation is mediated by an ejectosome complex.
  • This complex comprises viral proteins gp14, gp15, and gp16, forming an internal core within the virion.
  • Gp16 interacts with lipid bilayers, while gp15 binds to DNA.

Purpose of the Study:

  • To analyze the structure and stability of T7 phage proteins gp15 and gp16.
  • To investigate their behavior in the presence of lipids and chemical denaturants.
  • To propose a model for ejectosome assembly within the host cell.

Main Methods:

  • Structural analysis of gp15 and gp16.
  • Lipid interaction studies.
  • Chemical denaturation assays.

Main Results:

  • Gp15 and gp16 exhibit structural plasticity, refolding after thermal unfolding.
  • Analysis of protein structure in the presence of lipids and denaturants.
  • Observations support a model of protein unfolding during translocation and refolding for channel formation.

Conclusions:

  • The T7 phage ejectosome proteins gp15 and gp16 possess conformational flexibility crucial for DNA ejection.
  • Protein unfolding and refolding are key mechanisms for channel formation across the host cell envelope.
  • A model for ejectosome assembly is proposed based on structural and stability analyses.