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DNA polymerase mu, a candidate hypermutase?

J F Ruiz1, O Domínguez, T Laín de Lera

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

Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences
|February 24, 2001
PubMed
Summary

A novel DNA polymerase, Pol mu, plays a key role in somatic hypermutation of immunoglobulin genes. Its error-prone nature, similar to TdT, suggests involvement in DNA repair and recombination processes.

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Area of Science:

  • Molecular Biology
  • Immunology
  • Genetics

Background:

  • Human cells possess a newly identified DNA polymerase, Pol mu.
  • Pol mu shares 42% amino acid identity with terminal deoxynucleotidyl transferase (TdT), crucial for antigen-receptor diversity.

Purpose of the Study:

  • To review evidence for Pol mu's role in immunoglobulin gene somatic hypermutation.
  • To discuss the structural basis for Pol mu's error-prone DNA polymerization.
  • To predict Pol mu's involvement in DNA end-filling during V(D)J recombination and double-strand break repair.

Main Methods:

  • Review of existing evidence on Pol mu expression and activity.
  • Comparative analysis of Pol mu sequence with TdT.
  • Extrapolation from DNA polymerase beta (Pol beta) crystal structures.

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Main Results:

  • Pol mu exhibits preferential expression in secondary lymphoid organs and is associated with germinal centers.
  • Pol mu demonstrates low base discrimination during DNA polymerization, a mutator phenotype enhanced by Mn2+ ions.
  • Structural similarities suggest Pol mu's suitability for DNA end-filling.

Conclusions:

  • Pol mu is implicated in somatic hypermutation of immunoglobulin genes.
  • The enzyme's structural characteristics support its role in error-prone DNA synthesis.
  • Pol mu likely participates in V(D)J recombination and non-homologous end-joining DNA repair pathways.