IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v13y2022i1d10.1038_s41467-022-28644-7.html
   My bibliography  Save this article

Cryo-EM structure of translesion DNA synthesis polymerase ζ with a base pair mismatch

Author

Listed:
  • Radhika Malik

    (Icahn School of Medicine at Mount Sinai, New York)

  • Robert E. Johnson

    (301 University Blvd. University of Texas Medical Branch)

  • Louise Prakash

    (301 University Blvd. University of Texas Medical Branch)

  • Satya Prakash

    (301 University Blvd. University of Texas Medical Branch)

  • Iban Ubarretxena-Belandia

    (Icahn School of Medicine at Mount Sinai, New York
    University of the Basque Country
    Ikerbasque, Basque Foundation for Science)

  • Aneel K. Aggarwal

    (Icahn School of Medicine at Mount Sinai, New York)

Abstract

The B-family multi-subunit DNA polymerase ζ (Polζ) is important for translesion DNA synthesis (TLS) during replication, due to its ability to extend synthesis past nucleotides opposite DNA lesions and mismatched base pairs. We present a cryo-EM structure of Saccharomyces cerevisiae Polζ with an A:C mismatch at the primer terminus. The structure shows how the Polζ active site responds to the mismatched duplex DNA distortion, including the loosening of key protein-DNA interactions and a fingers domain in an “open” conformation, while the incoming dCTP is still able to bind for the extension reaction. The structure of the mismatched DNA-Polζ ternary complex reveals insights into mechanisms that either stall or favor continued DNA synthesis in eukaryotes.

Suggested Citation

  • Radhika Malik & Robert E. Johnson & Louise Prakash & Satya Prakash & Iban Ubarretxena-Belandia & Aneel K. Aggarwal, 2022. "Cryo-EM structure of translesion DNA synthesis polymerase ζ with a base pair mismatch," Nature Communications, Nature, vol. 13(1), pages 1-6, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-28644-7
    DOI: 10.1038/s41467-022-28644-7
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-022-28644-7
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-022-28644-7?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-28644-7. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.