IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v391y1998i6664d10.1038_34542.html
   My bibliography  Save this article

A mechanism for all polymerases

Author

Listed:
  • Thomas A. Steitz

    (Yale University)

Abstract

Replication of the genome is one of the most fundamental of biological activities, hence the interest in the mechanism by which the enzymes concerned -- the polynucleotide polymerases -- carry out the process. The co-crystal structures of the DNA polymerase that replicates bacteriophage T7, and of theBacillus stearothermophilusDNA polymerase large fragment, provide significant insights into the catalytic mechanism, fidelity and processivity of DNA polymerases.

Suggested Citation

  • Thomas A. Steitz, 1998. "A mechanism for all polymerases," Nature, Nature, vol. 391(6664), pages 231-232, January.
    • Handle: RePEc:nat:nature:v:391:y:1998:i:6664:d:10.1038_34542
    DOI: 10.1038/34542
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/34542
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/34542?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
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Alec Fraser & Maria L. Sokolova & Arina V. Drobysheva & Julia V. Gordeeva & Sergei Borukhov & John Jumper & Konstantin V. Severinov & Petr G. Leiman, 2022. "Structural basis of template strand deoxyuridine promoter recognition by a viral RNA polymerase," Nature Communications, Nature, vol. 13(1), pages 1-18, December.
    2. Longfu Xu & Matthew T. J. Halma & Gijs J. L. Wuite, 2024. "Mapping fast DNA polymerase exchange during replication," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    3. Chia-Shin Yang & Tzu-Ping Ko & Chao-Jung Chen & Mei-Hui Hou & Yu-Chuan Wang & Yeh Chen, 2023. "Crystal structure and functional implications of cyclic di-pyrimidine-synthesizing cGAS/DncV-like nucleotidyltransferases," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

    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:nature:v:391:y:1998:i:6664:d:10.1038_34542. 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.