ArticlePlant signaling & behavior2016
Further insight into BRUTUS domain composition and functionality.
Article in Plant signaling & behavior, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 41 citations in OpenAlex.
- Iron-sensing and redox properties of the hemerythrin-like domains of Arabidopsis BRUTUS and BRUTUS-LIKE2 proteins.Nature communications · 2025Article
- Genome-wide analysis of CHYR gene family and BnA03.CHYR.1 functional verification under salt stress in Brassica napus L.BMC plant biology · 2025Article
- Cellular clarity: a logistic regression approach to identify root epidermal regulators of iron deficiency response.BMC genomics · 2023Article
- Transcriptional and Post-Translational Regulation of Plant bHLH Transcription Factors during the Response to Environmental Stresses.Plants (Basel, Switzerland) · 2023Review
- Genome-wide analysis and functional characterization of CHYR gene family associated with abiotic stress tolerance in bread wheat (Triticum aestivum L.).BMC plant biology · 2022Article
- Primary nutrient sensors in plants.iScience · 2022Review
- Genome-Wide Identification, Characterization and Expression Analysis of SoybeanInternational journal of molecular sciences · 2021Article
- Basic Helix-Loop-Helix (bHLH) Transcription Factors Regulate a Wide Range of Functions in Arabidopsis.International journal of molecular sciences · 2021Review
- Transcriptome Analysis ofGenes · 2020Article
- The Transcription Factor bHLH121 Interacts with bHLH105 (ILR3) and Its Closest Homologs to Regulate Iron Homeostasis in Arabidopsis.The Plant cell · 2020Article
- Article
- OsbHLH058 and OsbHLH059 transcription factors positively regulate iron deficiency responses in rice.Plant molecular biology · 2019Article
- Arabidopsis BRUTUS-LIKE E3 ligases negatively regulate iron uptake by targeting transcription factor FIT for recycling.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Hemerythrin E3 Ubiquitin Ligases as Negative Regulators of Iron Homeostasis in Plants.Frontiers in plant science · 2019Review
- Structure, function and evolution of the hemerythrin-like domain superfamily.Protein science : a publication of the Protein Society · 2018Article
- BRUTUS and its paralogs, BTS LIKE1 and BTS LIKE2, encode important negative regulators of the iron deficiency response in Arabidopsis thaliana.Metallomics : integrated biometal science · 2017Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
BRUTUS (BTS) is a hemerythrin (HHE) domain containing E3 ligase that facilitates the degradation of POPEYE-like (PYEL) proteins in a proteasomal-dependent manner. Deletion of BTS HHE domains enhances BTS stability in the presence of iron and also complements loss of BTS function, suggesting that the HHE domains are critical for protein stability but not for enzymatic function. The RING E3 domain plays an essential role in BTS' capacity to both interact with PYEL proteins and to act as an E3 ligase. Here we show that removal of the RING domain does not complement loss of BTS function. We conclude that enzymatic activity of BTS via the RING domain is essential for response to iron deficiency in plants. Further, we analyze possible BTS domain structure evolution and predict that the combination of domains found in BTS is specific to photosynthetic organisms, potentially indicative of a role for BTS and its orthologs in mitigating the iron-related challenges presented by photosynthesis.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.