ArticleNucleic acids research2015
SerRS-tRNASec complex structures reveal mechanism of the first step in selenocysteine biosynthesis.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 41 citations in OpenAlex.
- Targeting the HPGDS-PGDSignal transduction and targeted therapy · 2026Article
- Exploring the Antioxidant Roles of Cysteine and Selenocysteine in Cellular Aging and Redox Regulation.Biomolecules · 2025Review
- Human selenocysteine synthase, SEPSECS, has evolved to optimize binding of a tRNA-based substrate.Nucleic acids research · 2024Article
- Structural basis of tRNA recognition by the mNature structural & molecular biology · 2024Article
- Interplay between mistranslation and oxidative stress inArhiv za higijenu rada i toksikologiju · 2024Article
- Protein-Protein Interactions of Seryl-tRNA Synthetases with Emphasis on Human Counterparts and Their Connection to Health and Disease.Life (Basel, Switzerland) · 2024Review
- Selenoproteins and tRNA-Sec: regulators of cancer redox homeostasis.Trends in cancer · 2023Review
- Seryl-tRNA synthetase promotes translational readthrough by mRNA binding and involvement of the selenocysteine incorporation machinery.Nucleic acids research · 2023Article
- Recoding UAG to selenocysteine inRNA (New York, N.Y.) · 2023Article
- Structural basis for the tRNA-dependent activation of the terminal complex of selenocysteine synthesis in humans.Nucleic acids research · 2023Article
- Selenium and Selenoproteins in Health.Biomolecules · 2023Review
- Drug repurposing screens identify compounds that inhibit α-synuclein oligomers' membrane disruption and block antibody interactions.Chemical science · 2023Article
- The tRNA identity landscape for aminoacylation and beyond.Nucleic acids research · 2023Review
- Loss of seryl-tRNA synthetase (Journal of medical genetics · 2022Article
- Bladder Cancer-Derived Small Extracellular Vesicles Promote Tumor Angiogenesis by Inducing HBP-Related Metabolic Reprogramming and SerRS O-GlcNAcylation in Endothelial Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Personalized Medicine in Mitochondrial Health and Disease: Molecular Basis of Therapeutic Approaches Based on Nutritional Supplements and Their Analogs.Molecules (Basel, Switzerland) · 2022Review
- Mutually exclusive substrate selection strategy by human m3C RNA transferases METTL2A and METTL6.Nucleic acids research · 2021Article
- Transfer RNAs: diversity in form and function.RNA biology · 2021Review
- On the Track of the Missing tRNA Genes: A Source of Non-Canonical Functions?Frontiers in molecular biosciences · 2021Review
- Rational Design of Aptamer-Tagged tRNAs.International journal of molecular sciences · 2020Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Selenocysteine (Sec) is found in the catalytic centers of many selenoproteins and plays important roles in living organisms. Malfunctions of selenoproteins lead to various human disorders including cancer. Known as the 21st amino acid, the biosynthesis of Sec involves unusual pathways consisting of several stages. While the later stages of the pathways are well elucidated, the molecular basis of the first stage-the serylation of Sec-specific tRNA (tRNA(Sec)) catalyzed by seryl-tRNA synthetase (SerRS)-is unclear. Here we present two cocrystal structures of human SerRS bound with tRNA(Sec) in different stoichiometry and confirm the formation of both complexes in solution by various characterization techniques. We discovered that the enzyme mainly recognizes the backbone of the long variable arm of tRNA(Sec) with few base-specific contacts. The N-terminal coiled-coil region works like a long-range lever to precisely direct tRNA 3' end to the other protein subunit for aminoacylation in a conformation-dependent manner. Restraints of the flexibility of the coiled-coil greatly reduce serylation efficiencies. Lastly, modeling studies suggest that the local differences present in the D- and T-regions as well as the characteristic U20:G19:C56 base triple in tRNA(Sec) may allow SerRS to distinguish tRNA(Sec) from closely related tRNA(Ser) substrate.
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