ArticleThe Journal of biological chemistry2014
Biochemical and biophysical characterization of the selenium-binding and reducing site in Arabidopsis thaliana homologue to mammals selenium-binding protein 1.
Article in The Journal of biological chemistry, 2014. 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, 37 citations in OpenAlex.
- The mechanism and application of the selenium hyperaccumulator Cardamine hupingshanensis: status and challenges.Annals of botany · 2026Review
- Time-dependent application strategies of selenium Nanofertilizer to enhance biofortification in rice and wheat.Food chemistry: X · 2025Article
- Selenium-Binding Protein 1 (SBP1): A New Putative Player of Stress Sensing in Plants.International journal of molecular sciences · 2024Review
- Overexpression of Wheat Selenium-Binding Protein GeneInternational journal of molecular sciences · 2024Article
- Methanethiol: A Scent Mark of Dysregulated Sulfur Metabolism in Cancer.Antioxidants (Basel, Switzerland) · 2023Review
- Evolutionary Aspects of Selenium Binding Protein (SBP).Journal of molecular evolution · 2023Article
- The SAH7 Homologue of the Allergen Ole e 1 Interacts with the Putative Stress Sensor SBP1 (Selenium-Binding Protein 1) inInternational journal of molecular sciences · 2023Article
- Illumina RNA and SMRT Sequencing Reveals the Mechanism of Uptake and Transformation of Selenium Nanoparticles in Soybean Seedlings.Plants (Basel, Switzerland) · 2023Article
- Wheat Selenium-binding protein TaSBP-A enhances cadmium tolerance by decreasing free CdFrontiers in plant science · 2023Article
- Selenium-binding Protein 1 (SBD1): A stress response regulator in Chlamydomonas reinhardtii.Plant physiology · 2022Article
- Metabolic Response of the YeastInternational journal of molecular sciences · 2020Article
- A Caenorhabditis elegans ortholog of human selenium-binding protein 1 is a pro-aging factor protecting against selenite toxicity.Redox biology · 2020Article
- Selenium-binding protein 1 (SELENBP1) is a marker of mature adipocytes.Redox biology · 2019Article
- Determination of Proteinaceous Selenocysteine in Selenized Yeast.International journal of molecular sciences · 2018Article
- A Role for Barley Calcium-Dependent Protein Kinase CPK2a in the Response to Drought.Frontiers in plant science · 2016Article
- A Critical Role for Cysteine 57 in the Biological Functions of Selenium Binding Protein-1.International journal of molecular sciences · 2015Article
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Authors and funding
12 authors at 7 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The function of selenium-binding protein 1 (SBP1), present in almost all organisms, has not yet been established. In mammals, SBP1 is known to bind the essential element selenium but the binding site has not been identified. In addition, the SBP family has numerous potential metal-binding sites that may play a role in detoxification pathways in plants. In Arabidopsis thaliana, AtSBP1 over-expression increases tolerance to two toxic compounds for plants, selenium and cadmium, often found as soil pollutants. For a better understanding of AtSBP1 function in detoxification mechanisms, we investigated the chelating properties of the protein toward different ligands with a focus on selenium using biochemical and biophysical techniques. Thermal shift assays together with inductively coupled plasma mass spectrometry revealed that AtSBP1 binds selenium after incubation with selenite (SeO3(2-)) with a ligand to protein molar ratio of 1:1. Isothermal titration calorimetry confirmed the 1:1 stoichiometry and revealed an unexpectedly large value of binding enthalpy suggesting a covalent bond between selenium and AtSBP1. Titration of reduced Cys residues and comparative mass spectrometry on AtSBP1 and the purified selenium-AtSBP1 complex identified Cys(21) and Cys(22) as being responsible for the binding of one selenium. These results were validated by site-directed mutagenesis. Selenium K-edge x-ray absorption near edge spectroscopy performed on the selenium-AtSBP1 complex demonstrated that AtSBP1 reduced SeO3(2-) to form a R-S-Se(II)-S-R-type complex. The capacity of AtSBP1 to bind different metals and selenium is discussed with respect to the potential function of AtSBP1 in detoxification mechanisms and selenium metabolism.
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