Iron-sensing and redox properties of the hemerythrin-like domains of Arabidopsis BRUTUS and BRUTUS-LIKE2 proteins
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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 O 2 and H 2 O 2 , resulting in a di-Fe 3+ form that is non-labile. In the reduced state, a proportion of the iron becomes labile, based on accessibility to Fe 2+ 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.
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Control of iron homeostasis by an iron-regulated ubiquitin ligase
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- Authors
- Pullin, J., Rodríguez-Celma, J., Franceschetti, M., Mundy, J. E. A., Svistunenko, D. A., Bradley, J. M., Le Brun, N. E., & Balk, J.
- Affiliations
- John Innes Centre (GB)
- Estación Experimental de Aula Dei (ES)
- University of Essex (GB)
- University of East Anglia (GB)
- Corresponding author
- Balk, Janneke
- ORCID
- Venue
- Nature Communications
- Published
- 2025-04-24
- Volume
- 16
- Issue
- 1
- Pages
- 3865-3865
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC12022348
- OpenAlex
- W4409735919
- Cited by
- 18
- References
- 3
- Citations by year
- 2026: 11 · 2025: 7
- FWCI
- 9.73
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- UEA Digital Repository (University of East Anglia) (submittedVersion, cc-by)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- RCUK | Biotechnology and Biological Sciences Research Council (BB/N001079/1, BB/V015095/1, BB/R013578/1, BB/V014625/1)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Micronutrient Interactions and Effects
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Keywords
- Brutus, iron uptake regulation, E3 ubiquitin ligase, redox properties, iron binding, Arabidopsis thaliana, iron chelators
- MeSH terms
- Protein Domains, Hemerythrin, Hydrogen Peroxide, Iron, Oxidation-Reduction, Signal Transduction, Arabidopsis, Arabidopsis Proteins, Ubiquitin-Protein Ligases
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