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Related Experiment Videos

Damage repair DNA polymerases Y.

Wei Yang1

  • 1Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. Wei.Yang@nih.gov

Current Opinion in Structural Biology
|February 13, 2003
PubMed
Summary

Newly discovered Y-family DNA polymerases perform low-fidelity replication and translesion synthesis. Their unique structure, including a small active site and a "little finger" domain, allows them to handle DNA damage and interact with cellular factors.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Y-family DNA polymerases are crucial for DNA repair and replication fidelity.
  • These enzymes are known for their ability to synthesize DNA across damaged templates, a process called translesion synthesis.
  • Their low fidelity on undamaged templates suggests specialized roles in genome maintenance.

Purpose of the Study:

  • To elucidate the structural basis for the unique functions of Y-family DNA polymerases.
  • To understand how their structure facilitates translesion DNA synthesis and interaction with DNA lesions.
  • To investigate the role of specific domains in DNA binding and catalytic activity.

Main Methods:

  • X-ray crystallography was used to determine the structures of three Y-family polymerases.

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  • Structures were analyzed both alone and in complex with DNA and nucleotide substrates.
  • Comparative structural analysis focused on the catalytic core, active site accessibility, and unique domains.

    • Main Results:

    • Y-family polymerases possess a conserved right-hand-like catalytic core (finger, thumb, palm domains).
    • Unusually small finger and thumb domains create an open, spacious active site accommodating mismatched bases and DNA lesions.
    • A unique 'little finger' domain enhances DNA binding, catalytic efficiency, and auxiliary factor interactions.
    • These polymerases lack 3' to 5' exonuclease activity.

    Conclusions:

    • The open active site and specialized domains of Y-family polymerases are key to their translesion synthesis capabilities.
    • The 'little finger' domain is critical for DNA polymerase function and interactions within the replication machinery.
    • Expression and recruitment of these polymerases are regulated by DNA damage and protein interactions (e.g., beta-clamp, PCNA).