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DNA polymerase active site is highly mutable: evolutionary consequences.

P H Patel1, L A Loeb

  • 1The Joseph Gottstein Memorial Cancer Laboratory, Department of Pathology, University of Washington School of Medicine, Seattle, WA 98195-7705, USA.

Proceedings of the National Academy of Sciences of the United States of America
|May 11, 2000
PubMed
Summary
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DNA polymerases

Area of Science:

  • Molecular Biology
  • Enzymology
  • Biochemistry

Background:

  • DNA polymerases possess highly conserved active sites.
  • Understanding active site tolerance to mutation is crucial for enzyme evolution studies.

Purpose of the Study:

  • To investigate the mutational tolerance of the DNA polymerase I active site.
  • To determine the impact of mutations on enzyme activity and properties.

Main Methods:

  • Random mutagenesis of a 13-amino acid stretch (motif A) in Thermus aquaticus DNA polymerase I.
  • Genetic complementation for selection of active mutants.
  • Sequencing and analysis of approximately 8,000 active polymerase mutants.

Main Results:

  • All residues in motif A, except Asp-610, are mutable without loss of wild-type activity.

Related Experiment Videos

  • Diverse amino acid substitutions were observed, with conservative changes at structural regions.
  • Several mutants displayed enhanced DNA polymerase activity or incorporated ribonucleotide analogs.

    • Conclusions:

    • The polymerase active site exhibits significant in vivo mutability, allowing for enzyme evolution.
    • High mutability may be essential for survival in environments requiring increased mutagenesis.
    • The adaptability of polymerase active sites contrasts with the conserved nature of nucleotide sequences.