Bacteriophage phi 29 early protein p17. Self-association and hetero-association with the viral histone-like protein

Paola Crucitti1, Ana M Abril, Margarita Salas

  • 1Centro de Biologia Molecular Severo Ochoa (CSIC-UAM), Universidad Autonoma, Canto Blanco, 28049 Madrid, Spain.

Insights

Bacillus subtilis phage Phi29 gene 17 protein p17 optimizes viral DNA replication initiation by aiding origin-binding protein p6. This protein is crucial early in infection, especially at low multiplicities, and also regulates its own transcription.

Area of Science:

  • Virology
  • Molecular Biology
  • Genetics

Background:

  • Bacillus subtilis phage Phi29 gene 17 encodes protein p17, essential for early phage replication at low infection multiplicities.
  • Protein p17 is thought to recruit limiting initiation factors to viral origins.
  • Its function becomes dispensable as replication proteins accumulate.

Purpose of the Study:

  • Investigate protein p17 dimerization and the role of its coiled-coil region.
  • Elucidate the interaction between protein p17 and viral origin-binding protein p6.

Main Methods:

  • Protein dimerization studies.
  • Analysis of coiled-coil region function.
  • Investigation of protein p17 and p6 interactions.

Main Results:

  • Protein p17 dimerization and coiled-coil region were studied.
  • The interaction between protein p17 and origin-binding protein p6 was analyzed.
  • Results suggest p17 optimizes p6 binding to viral DNA ends.

Conclusions:

  • Protein p17 facilitates the initiation of Bacillus subtilis phage Phi29 replication.
  • p17 optimizes origin-binding protein p6's interaction with viral DNA.
  • Protein p17 negatively modulates its own transcription.

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