Exonuclease mutations in DNA polymerase epsilon reveal replication strand specific mutation patterns and human origins of replication

Genome Res. 2014 Nov;24(11):1740-50. doi: 10.1101/gr.174789.114. Epub 2014 Sep 16.

Abstract

Tumors with somatic mutations in the proofreading exonuclease domain of DNA polymerase epsilon (POLE-exo*) exhibit a novel mutator phenotype, with markedly elevated TCT→TAT and TCG→TTG mutations and overall mutation frequencies often exceeding 100 mutations/Mb. Here, we identify POLE-exo* tumors in numerous cancers and classify them into two groups, A and B, according to their mutational properties. Group A mutants are found only in POLE, whereas Group B mutants are found in POLE and POLD1 and appear to be nonfunctional. In Group A, cell-free polymerase assays confirm that mutations in the exonuclease domain result in high mutation frequencies with a preference for C→A mutation. We describe the patterns of amino acid substitutions caused by POLE-exo* and compare them to other tumor types. The nucleotide preference of POLE-exo* leads to increased frequencies of recurrent nonsense mutations in key tumor suppressors such as TP53, ATM, and PIK3R1. We further demonstrate that strand-specific mutation patterns arise from some of these POLE-exo* mutants during genome duplication. This is the first direct proof of leading strand-specific replication by human POLE, which has only been demonstrated in yeast so far. Taken together, the extremely high mutation frequency and strand specificity of mutations provide a unique identifier of eukaryotic origins of replication.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Ataxia Telangiectasia Mutated Proteins / genetics
  • Ataxia Telangiectasia Mutated Proteins / metabolism
  • Class Ia Phosphatidylinositol 3-Kinase
  • Codon, Nonsense
  • DNA Mutational Analysis
  • DNA Polymerase II / chemistry
  • DNA Polymerase II / genetics*
  • DNA Polymerase II / metabolism
  • DNA Polymerase III / genetics
  • DNA Polymerase III / metabolism
  • DNA Replication*
  • Databases, Genetic
  • Exonucleases / chemistry
  • Exonucleases / genetics*
  • Exonucleases / metabolism
  • Genome-Wide Association Study
  • Humans
  • Microsatellite Instability
  • Models, Molecular
  • Mutation, Missense*
  • Neoplasms / enzymology
  • Neoplasms / genetics
  • Neoplasms / metabolism
  • Phosphatidylinositol 3-Kinases / genetics
  • Phosphatidylinositol 3-Kinases / metabolism
  • Protein Structure, Tertiary
  • Replication Origin / genetics
  • Tumor Suppressor Protein p53 / genetics
  • Tumor Suppressor Protein p53 / metabolism

Substances

  • Codon, Nonsense
  • Tumor Suppressor Protein p53
  • PIK3R1 protein, human
  • Class Ia Phosphatidylinositol 3-Kinase
  • ATM protein, human
  • Ataxia Telangiectasia Mutated Proteins
  • POLD1 protein, human
  • DNA Polymerase II
  • DNA Polymerase III
  • Exonucleases