IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v16y2025i1d10.1038_s41467-025-58853-9.html
   My bibliography  Save this article

Iron-sensing and redox properties of the hemerythrin-like domains of Arabidopsis BRUTUS and BRUTUS-LIKE2 proteins

Author

Listed:
  • Jacob Pullin

    (John Innes Centre)

  • Jorge Rodríguez-Celma

    (CSIC)

  • Marina Franceschetti

    (John Innes Centre)

  • Julia E. A. Mundy

    (John Innes Centre)

  • Dimitri A. Svistunenko

    (University of Essex)

  • Justin M. Bradley

    (University of East Anglia)

  • Nick E. Brun

    (University of East Anglia)

  • Janneke Balk

    (John Innes Centre
    University of East Anglia)

Abstract

Iron uptake in plants is negatively regulated by highly conserved hemerythrin (Hr) E3 ubiquitin ligases exemplified by Arabidopsis thaliana BRUTUS (BTS). Physiological studies suggest these are the elusive plant iron sensors, but biochemical evidence is lacking. Here we demonstrate that the N-terminal domains of BTS and BTS-LIKE2 (BTSL2) respectively bind three and two diiron centres within three closely packed Hr-like subdomains. The centres can be reversibly oxidized by O2 and H2O2, resulting in a di-Fe3+ form that is non-labile. In the reduced state, a proportion of the iron becomes labile, based on accessibility to Fe2+ chelators and reconstitution experiments, consistent with dynamic iron binding. Impaired iron binding and altered redox properties in the BTS dgl variant correlate with diminished capacity to suppress the downstream signalling cascade. These data provide the biochemical foundation for a mechanistic model of how BTS/Ls function as iron sensors that are unique to the plant kingdom.

Suggested Citation

  • Jacob Pullin & Jorge Rodríguez-Celma & Marina Franceschetti & Julia E. A. Mundy & Dimitri A. Svistunenko & Justin M. Bradley & Nick E. Brun & Janneke Balk, 2025. "Iron-sensing and redox properties of the hemerythrin-like domains of Arabidopsis BRUTUS and BRUTUS-LIKE2 proteins," Nature Communications, Nature, vol. 16(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-58853-9
    DOI: 10.1038/s41467-025-58853-9
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-025-58853-9
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-025-58853-9?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:16:y:2025:i:1:d:10.1038_s41467-025-58853-9. 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.