IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v480y2011i7377d10.1038_nature10623.html
   My bibliography  Save this article

HIV-1 restriction factor SAMHD1 is a deoxynucleoside triphosphate triphosphohydrolase

Author

Listed:
  • David C. Goldstone

    (MRC National Institute for Medical Research, the Ridgeway, Mill Hill)

  • Valerie Ennis-Adeniran

    (MRC National Institute for Medical Research, the Ridgeway, Mill Hill)

  • Joseph J. Hedden

    (MRC National Institute for Medical Research, the Ridgeway, Mill Hill)

  • Harriet C. T. Groom

    (MRC National Institute for Medical Research, the Ridgeway, Mill Hill)

  • Gillian I. Rice

    (Genetic Medicine, University of Manchester, Manchester Academic Heath Science Centre, Central Manchester Foundation Trust University Hospitals)

  • Evangelos Christodoulou

    (MRC National Institute for Medical Research, the Ridgeway, Mill Hill)

  • Philip A. Walker

    (MRC National Institute for Medical Research, the Ridgeway, Mill Hill)

  • Geoff Kelly

    (MRC Biomedical NMR Centre, National Institute for Medical Research, the Ridgeway, Mill Hill)

  • Lesley F. Haire

    (MRC National Institute for Medical Research, the Ridgeway, Mill Hill)

  • Melvyn W. Yap

    (MRC National Institute for Medical Research, the Ridgeway, Mill Hill)

  • Luiz Pedro S. de Carvalho

    (MRC National Institute for Medical Research, the Ridgeway, Mill Hill)

  • Jonathan P. Stoye

    (MRC National Institute for Medical Research, the Ridgeway, Mill Hill)

  • Yanick J. Crow

    (Genetic Medicine, University of Manchester, Manchester Academic Heath Science Centre, Central Manchester Foundation Trust University Hospitals)

  • Ian A. Taylor

    (MRC National Institute for Medical Research, the Ridgeway, Mill Hill)

  • Michelle Webb

    (Genetic Medicine, University of Manchester, Manchester Academic Heath Science Centre, Central Manchester Foundation Trust University Hospitals)

Abstract

Antiretroviral role for SAMHD1 protein Mutations in SAMHD1 protein are associated with the human autoimmune disease Aicardi–Goutières syndrome, and SAMHD1 was recently shown to be responsible for restriction of HIV-1 replication in myeloid cells. Ian Taylor and colleagues reveal a previously unknown function of SAMHD1 that could explain its antivirus role. They provide a crystal structure of the catalytic core of SAMHD1 and show that it is a dGTP-stimulated triphosphohydrolase that hydrolyses dNTPs, the building blocks of DNA. This activity may prevent reverse transcription and viral synthesis of complementary DNA by keeping the concentration of cellular dNTPs at a low level.

Suggested Citation

  • David C. Goldstone & Valerie Ennis-Adeniran & Joseph J. Hedden & Harriet C. T. Groom & Gillian I. Rice & Evangelos Christodoulou & Philip A. Walker & Geoff Kelly & Lesley F. Haire & Melvyn W. Yap & Lu, 2011. "HIV-1 restriction factor SAMHD1 is a deoxynucleoside triphosphate triphosphohydrolase," Nature, Nature, vol. 480(7377), pages 379-382, December.
    • Handle: RePEc:nat:nature:v:480:y:2011:i:7377:d:10.1038_nature10623
    DOI: 10.1038/nature10623
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature10623
    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/nature10623?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. Priya Kapoor-Vazirani & Sandip K. Rath & Xu Liu & Zhen Shu & Nicole E. Bowen & Yitong Chen & Ramona Haji-Seyed-Javadi & Waaqo Daddacha & Elizabeth V. Minten & Diana Danelia & Daniela Farchi & Duc M. D, 2022. "SAMHD1 deacetylation by SIRT1 promotes DNA end resection by facilitating DNA binding at double-strand breaks," Nature Communications, Nature, vol. 13(1), pages 1-18, December.
    2. Oliver J. Acton & Devon Sheppard & Simone Kunzelmann & Sarah J. Caswell & Andrea Nans & Ailidh J. O. Burgess & Geoff Kelly & Elizabeth R. Morris & Peter B. Rosenthal & Ian A. Taylor, 2024. "Platform-directed allostery and quaternary structure dynamics of SAMHD1 catalysis," Nature Communications, Nature, vol. 15(1), pages 1-16, 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:480:y:2011:i:7377:d:10.1038_nature10623. 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.