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Structural and functional studies on phi 29 DNA polymerase.

M A Blasco1, J A Esteban, J Méndez

  • 1Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma, Madrid, Spain.

Chromosoma
|January 1, 1992
PubMed
Summary
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The Bacillus subtilis phage phi 29 DNA polymerase

Area of Science:

  • Molecular Biology
  • Virology
  • Biochemistry

Background:

  • Bacillus subtilis phage phi 29 DNA polymerase is crucial for protein-primed viral DNA replication.
  • It shares conserved amino acid sequences with eukaryotic DNA polymerases.
  • The C-terminal Lys-X-Tyr (K-Y) motif is a conserved region requiring functional study.

Purpose of the Study:

  • To investigate the functional significance of the C-terminal K-Y motif in phi 29 DNA polymerase.
  • To understand the role of invariant Lys and Tyr residues in DNA polymerization and protein priming.
  • To assess the impact of viral protein p6 on phi 29 DNA polymerase fidelity.

Main Methods:

  • Site-directed mutagenesis was employed to create single point mutants.
  • Mutant proteins were overproduced and characterized biochemically.

Related Experiment Videos

  • Enzyme activity, protein priming capability, and insertion fidelity were measured.

    • Main Results:

    • Invariant Lys and Tyr residues are critical for phi 29 DNA polymerase activity.
    • Specific substitutions of Lys affected protein priming capability, altering enzyme properties.
    • Viral protein p6 significantly enhanced the insertion fidelity of the DNA polymerase.

    Conclusions:

    • The K-Y motif is essential for the catalytic function of phi 29 DNA polymerase.
    • Modifications in the K-Y motif can alter the unique protein-priming mechanism.
    • A proposed 'sliding-back' mechanism may contribute to high replication fidelity.