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Related Experiment Videos

The Nu1 subunit of bacteriophage lambda terminase.

W Parris1, A Davidson, C L Keeler

  • 1Department of Medical Genetics Building, University of Toronto, Canada.

The Journal of Biological Chemistry
|June 15, 1988
PubMed
Summary
This summary is machine-generated.

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Bacteriophage lambda DNA packaging is driven by terminase enzyme. Purified gpNu1 subunit shows DNA binding and independent ATPase activity, complementing other subunits in DNA packaging and cleavage.

Area of Science:

  • Molecular Biology
  • Virology
  • Biochemistry

Background:

  • Bacteriophage lambda DNA maturation and packaging rely on the terminase enzyme, a complex of gpNu1 and gpA subunits.
  • The holoenzyme exhibits multifunctional activity, including DNA binding at the cos site, DNA packaging into proheads, and DNA-dependent ATPase activity.

Purpose of the Study:

  • To characterize the gpNu1 subunit of bacteriophage lambda terminase.
  • To investigate the biochemical properties of purified gpNu1, including its aggregation state, DNA binding, and ATPase activity.

Main Methods:

  • High-level expression and purification of the gpNu1 protein.
  • Gel filtration and sedimentation velocity centrifugation to determine protein aggregation.
  • Filter binding assays for DNA binding analysis.

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  • ATPase assays to assess enzymatic activity.

    • Main Results:

    • Purified gpNu1 has a monomeric molecular weight of 21,200 and exists as a large aggregate (Mr > 500,000).
    • gpNu1 specifically binds to lambda DNA and exhibits DNA-independent ATPase activity.
    • Purified gpNu1 complements gpA-containing extracts in lambda DNA packaging and cos cleavage assays.

    Conclusions:

    • The gpNu1 subunit possesses DNA binding and ATPase activities, crucial for bacteriophage lambda DNA packaging.
    • gpNu1's properties are consistent with its predicted functions based on its amino acid sequence.
    • The study provides insights into the individual contributions of terminase subunits to DNA packaging and cleavage.