ArticleThe Journal of biological chemistry2015
Formation of a Ternary Complex for Selenocysteine Biosynthesis in Bacteria.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 25 citations in OpenAlex.
- The mycobacterial selenocysteine machinery: presence and expression.RNA biology · 2026Article
- Bacterial selenocysteine synthase structure revealed by single-particle cryoEM.Current research in structural biology · 2024Article
- Bioinformatic Prediction of an tRNAInternational journal of molecular sciences · 2021Article
- Trypanosomatid selenophosphate synthetase structure, function and interaction with selenocysteine lyase.PLoS neglected tropical diseases · 2020Article
- Why Selenocysteine Is Unique?Frontiers in molecular biosciences · 2020Article
- [A facile method for producing selenocysteine-containing proteins].Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2018Article
- A Facile Method for Producing Selenocysteine-Containing Proteins.Angewandte Chemie (International ed. in English) · 2018Article
- Biomagnetic Recovery and Bioaccumulation of Selenium Granules in Magnetotactic Bacteria.Applied and environmental microbiology · 2016Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The synthesis of selenocysteine-containing proteins (selenoproteins) involves the interaction of selenocysteine synthase (SelA), tRNA (tRNA(Sec)), selenophosphate synthetase (SelD, SPS), a specific elongation factor (SelB), and a specific mRNA sequence known as selenocysteine insertion sequence (SECIS). Because selenium compounds are highly toxic in the cellular environment, the association of selenium with proteins throughout its metabolism is essential for cell survival. In this study, we demonstrate the interaction of SPS with the SelA-tRNA(Sec) complex, resulting in a 1.3-MDa ternary complex of 27.0 ± 0.5 nm in diameter and 4.02 ± 0.05 nm in height. To assemble the ternary complex, SPS undergoes a conformational change. We demonstrated that the glycine-rich N-terminal region of SPS is crucial for the SelA-tRNA(Sec)-SPS interaction and selenoprotein biosynthesis, as revealed by functional complementation experiments. Taken together, our results provide new insights into selenoprotein biosynthesis, demonstrating for the first time the formation of the functional ternary SelA-tRNA(Sec)-SPS complex. We propose that this complex is necessary for proper selenocysteine synthesis and may be involved in avoiding the cellular toxicity of selenium compounds.
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Registered trials
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