IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v5y2014i1d10.1038_ncomms4425.html
   My bibliography  Save this article

Plant cysteine oxidases control the oxygen-dependent branch of the N-end-rule pathway

Author

Listed:
  • Daan A. Weits

    (Institute of Life Sciences, Scuola Superiore Sant’Anna
    Max Planck Institute of Molecular Plant Physiology)

  • Beatrice Giuntoli

    (Institute of Life Sciences, Scuola Superiore Sant’Anna)

  • Monika Kosmacz

    (Max Planck Institute of Molecular Plant Physiology)

  • Sandro Parlanti

    (Institute of Life Sciences, Scuola Superiore Sant’Anna)

  • Hans-Michael Hubberten

    (Max Planck Institute of Molecular Plant Physiology)

  • Heike Riegler

    (Max Planck Institute of Molecular Plant Physiology)

  • Rainer Hoefgen

    (Max Planck Institute of Molecular Plant Physiology)

  • Pierdomenico Perata

    (Institute of Life Sciences, Scuola Superiore Sant’Anna)

  • Joost T. van Dongen

    (Max Planck Institute of Molecular Plant Physiology
    Institute of Biology, RWTH Aachen University)

  • Francesco Licausi

    (Institute of Life Sciences, Scuola Superiore Sant’Anna)

Abstract

In plant and animal cells, amino-terminal cysteine oxidation controls selective proteolysis via an oxygen-dependent branch of the N-end rule pathway. It remains unknown how the N-terminal cysteine is specifically oxidized. Here we identify plant cysteine oxidase (PCO) enzymes that oxidize the penultimate cysteine of ERF-VII transcription factors by using oxygen as a co-substrate, thereby controlling the lifetime of these proteins. Consequently, ERF-VII proteins are stabilized under hypoxia and activate the molecular response to low oxygen while the expression of anaerobic genes is repressed in air. Members of the PCO family are themselves targets of ERF-VII transcription factors, generating a feedback loop that adapts the stress response according to the extent of the hypoxic condition. Our results reveal that PCOs act as sensor proteins for oxygen in plants and provide an example of how proactive regulation of the N-end rule pathway balances stress response to optimal growth and development in plants.

Suggested Citation

  • Daan A. Weits & Beatrice Giuntoli & Monika Kosmacz & Sandro Parlanti & Hans-Michael Hubberten & Heike Riegler & Rainer Hoefgen & Pierdomenico Perata & Joost T. van Dongen & Francesco Licausi, 2014. "Plant cysteine oxidases control the oxygen-dependent branch of the N-end-rule pathway," Nature Communications, Nature, vol. 5(1), pages 1-10, May.
  • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4425
    DOI: 10.1038/ncomms4425
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/ncomms4425
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/ncomms4425?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
    ---><---

    Citations

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


    Cited by:

    1. 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.
    2. 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:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4425. 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.