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Visualizing Rev1 catalyze protein-template DNA synthesis.

Tyler M Weaver1,2, Luis M Cortez1,2, Thu H Khoang1,2

  • 1Department of Biochemistry and Molecular Biology, University of Kansas Medical Center, Kansas City, KS 66160.

Proceedings of the National Academy of Sciences of the United States of America
|October 1, 2020
PubMed
Summary

Specialized translesion synthesis (TLS) polymerases like Rev1 bypass DNA lesions using a unique protein-template mechanism. Rev1 evicts the DNA base before nucleotide incorporation and prevents mutagenic synthesis by modifying the pyrophosphate product.

Keywords:
DNA polymeraseDNA repairtranslesion synthesis

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • DNA replication can stall at DNA lesions, necessitating specialized repair mechanisms.
  • Translesion synthesis (TLS) polymerases bypass DNA lesions, preventing replication fork stalling.
  • Rev1 is a TLS polymerase that handles abasic sites and guanine adducts via a protein-template mechanism.

Purpose of the Study:

  • To elucidate the atomic-level details of the Rev1 protein-template mechanism.
  • To understand how Rev1 bypasses DNA lesions and incorporates nucleotides.

Main Methods:

  • Time-lapse X-ray crystallography
  • Molecular dynamics simulations
  • DNA enzymology
  • Studied Saccharomyces cerevisiae Rev1 protein

Main Results:

  • Rev1 evicts the templating base before nucleotide binding.
  • Nucleotide binding induces DNA substrate conformational changes for nucleotidyl transfer.
  • Rev1 converts pyrophosphate to monophosphates, preventing pyrophosphorolysis.
  • Post-incorporation changes prevent mutagenic synthesis and facilitate product dissociation.

Conclusions:

  • Rev1 utilizes a unique protein-template mechanism for DNA lesion bypass.
  • The enzyme's mechanism prevents potentially mutagenic processive synthesis.
  • Rev1's actions ensure efficient and accurate DNA damage tolerance.