Over‐expression of human DNA polymerase lambda in E. coli and characterization of the recombinant enzyme

@article{Shimazaki2002OverexpressionOH,
  title={Over‐expression of human DNA polymerase lambda in E. coli and characterization of the recombinant enzyme},
  author={N. Shimazaki and Kenta Yoshida and Toshiko Kobayashi and S. Toji and K. Tamai and O. Koiwai},
  journal={Genes to Cells},
  year={2002},
  volume={7}
}
Background: DNA polymerase lambda (Pol λ) was recently identified as a new member of the family X of DNA polymerases in eukaryotic cells. Pol λ contains a nuclear localization signal (NLS), a BRCA1‐C terminal (BRCT) domain, a proline‐rich region, helix‐hairpin‐helix (HhH) and pol X motifs. Since the amino acid sequence for Pol λ shares a high degree of homology to Pol β, Pol λ is considered to have a similar enzymatic nature to Pol β. 
DNA polymerase lambda directly binds to proliferating cell nuclear antigen through its confined C‐terminal region
TLDR
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The analysis using isotope a-32P-dCTP incorporation in vitro showed that the purified recombinant POL λ2 exhibited DNA polymerase activity and might be involved in hepatocarcinogenesis. Expand
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DNA polymerase (POL) λ plays an important role during DNA repair and DNA nonhomologous recombination processes. A novel POL λ variant was cloned from a human liver cDNA library and named POL λ2Expand
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TLDR
The results indicate that the average single-base deletion error rate of Pol λ is higher than those of other mammalian polymerases, and this ability, together with an ability to fill short gaps in DNA at low dNTP concentrations, is consistent with a role for mammalian Polλ in non-homologous end-joining. Expand
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TLDR
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TLDR
It is demonstrated that the non-enzymatic proline-rich domain confers the increase in fidelity of DNA polymerase λ by significantly lowering incorporation rate constants of incorrect nucleotides, illustrating a novel mechanism, in which theDNA polymerase fidelity is controlled not by an accessory protein or a proofreading exonuclease domain but by an internal regulatory domain. Expand
POLN, a Nuclear PolA Family DNA Polymerase Homologous to the DNA Cross-link Sensitivity Protein Mus308*
TLDR
The identification, cloning, and characterization of POLN and its gene product, a new mammalian DNA polymerase also related to Mus308, are reported on. Expand
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TLDR
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TLDR
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TLDR
A new approach is developed for determining the relative contributions of SP- and LP-BER pathways, exploiting mass-labeled nucleotides to distinguish single- and multinucleotide repair patches, and it is found that uracil repair in wild-type and in Polβ-deficient cell extracts supplemented with Polλ was ∼80% SP-BER. Expand
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