IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v479y2011i7373d10.1038_nature10536.html
   My bibliography  Save this article

Oxygen sensing in plants is mediated by an N-end rule pathway for protein destabilization

Author

Listed:
  • Francesco Licausi

    (Max Planck Institute of Molecular Plant Physiology, Am Muehlenberg 1, 14476
    PlantLab, Institute of Life Sciences, Scuola Superiore Sant’Anna, Piazza Martiri della Libertà 33)

  • Monika Kosmacz

    (Max Planck Institute of Molecular Plant Physiology, Am Muehlenberg 1, 14476)

  • Daan A. Weits

    (Max Planck Institute of Molecular Plant Physiology, Am Muehlenberg 1, 14476)

  • Beatrice Giuntoli

    (PlantLab, Institute of Life Sciences, Scuola Superiore Sant’Anna, Piazza Martiri della Libertà 33)

  • Federico M. Giorgi

    (Max Planck Institute of Molecular Plant Physiology, Am Muehlenberg 1, 14476)

  • Laurentius A. C. J. Voesenek

    (Plant Ecophysiology, Institute of Environmental Biology, Utrecht University, Padualaan 8
    Centre for Biosystems Genomics)

  • Pierdomenico Perata

    (PlantLab, Institute of Life Sciences, Scuola Superiore Sant’Anna, Piazza Martiri della Libertà 33)

  • Joost T. van Dongen

    (Max Planck Institute of Molecular Plant Physiology, Am Muehlenberg 1, 14476)

Abstract

How plants sense oxygen shortage Tolerance of plants to flooding is an important factor for food security, particularly in the developing world. When plants are submerged in water they experience hypoxia, which triggers changes in gene transcription that promote anaerobic metabolism and sustain ATP production. Two complementary studies identify the mechanism that senses reduced oxygen levels in Arabidopsis. They report that the N-end rule pathway of targeted proteolysis regulates the stability of key hypoxia-response transcription factors. Enhanced stability of these proteins under low oxygen conditions improves plant survival, suggesting a target for possible genetic improvement of flooding-tolerance in crops.

Suggested Citation

  • Francesco Licausi & Monika Kosmacz & Daan A. Weits & Beatrice Giuntoli & Federico M. Giorgi & Laurentius A. C. J. Voesenek & Pierdomenico Perata & Joost T. van Dongen, 2011. "Oxygen sensing in plants is mediated by an N-end rule pathway for protein destabilization," Nature, Nature, vol. 479(7373), pages 419-422, November.
  • Handle: RePEc:nat:nature:v:479:y:2011:i:7373:d:10.1038_nature10536
    DOI: 10.1038/nature10536
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature10536
    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/nature10536?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. Verna Van & Janae B. Brown & Corin R. O’Shea & Hannah Rosenbach & Ijaz Mohamed & Nna-Emeka Ejimogu & Toan S. Bui & Veronika A. Szalai & Kelly N. Chacón & Ingrid Span & Fangliang Zhang & Aaron T. Smith, 2023. "Iron-sulfur clusters are involved in post-translational arginylation," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Agata Zubrycka & Charlene Dambire & Laura Dalle Carbonare & Gunjan Sharma & Tinne Boeckx & Kamal Swarup & Craig J. Sturrock & Brian S. Atkinson & Ranjan Swarup & Françoise Corbineau & Neil J. Oldham &, 2023. "ERFVII action and modulation through oxygen-sensing in Arabidopsis thaliana," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    3. Karen C. Heathcote & Thomas P. Keeley & Matti Myllykoski & Malin Lundekvam & Nina McTiernan & Salma Akter & Norma Masson & Peter J. Ratcliffe & Thomas Arnesen & Emily Flashman, 2024. "N-terminal cysteine acetylation and oxidation patterns may define protein stability," Nature Communications, Nature, vol. 15(1), pages 1-15, 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:479:y:2011:i:7373:d:10.1038_nature10536. 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.