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In vitro lesion bypass by human PrimPol.

Alena V Makarova1, Elizaveta O Boldinova1, Ekaterina A Belousova2

  • 1Institute of Molecular Genetics, Russian Academy of Sciences, Kurchatov sq. 2, Moscow, 123182, Russia.

DNA Repair
|August 12, 2018
PubMed
Summary

Human PrimPol (translesion synthesis polymerase) efficiently bypasses DNA damage like 8-oxoguanine with Mg2+ ions. Mn2+ ions enhance its activity on more complex lesions, though with increased errors.

Keywords:
DNADNA damagePrimPolTranslesion synthesis

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Area of Science:

  • Molecular Biology
  • DNA Repair Mechanisms
  • Enzymology

Background:

  • DNA damage poses a threat to genome stability.
  • Translesion synthesis (TLS) polymerases are crucial for bypassing DNA lesions.
  • Human PrimPol possesses both primase and polymerase activities, aiding replication fork progression.

Purpose of the Study:

  • To investigate the TLS properties of human PrimPol in vitro.
  • To determine the effect of different metal ions (Mg2+ and Mn2+) on PrimPol's TLS activity and fidelity.
  • To assess PrimPol's ability to bypass various DNA lesions.

Main Methods:

  • In vitro biochemical assays using purified human PrimPol.
  • Testing PrimPol's DNA synthesis activity on templates containing specific DNA lesions (8-oxoguanine, 5-formyluracil, abasic site, O6-methylguanine, thymine glycol, 1,N6-ethenoadenine).
  • Evaluating the impact of Mg2+ and Mn2+ ions on synthesis efficiency and accuracy.

Main Results:

  • PrimPol efficiently and accurately synthesizes DNA past 8-oxoguanine and 5-formyluracil in the presence of Mg2+.
  • Mg2+-dependent bypass is blocked by thymine glycol and 1,N6-ethenoadenine.
  • Mn2+ significantly enhances PrimPol's TLS activity, enabling bypass of all tested lesions, but with reduced fidelity (error-prone synthesis).

Conclusions:

  • Human PrimPol exhibits metal ion-dependent translesion synthesis capabilities.
  • The choice of metal ion influences PrimPol's efficiency and accuracy in bypassing DNA damage.
  • PrimPol's dual primase and polymerase activities may play a significant role in replicating DNA with clustered damage in vivo.