ArticleNature structural & molecular biology2008
Aminoacylation of tRNA with phosphoserine for synthesis of cysteinyl-tRNA(Cys).
Article in Nature structural & molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 65 citations in OpenAlex.
- Decoding the Minimal Translation System of the Plasmodium falciparum Apicoplast: Essential tRNA-modifying Enzymes and Their Roles in Organelle Maintenance.Journal of molecular biology · 2025Article
- Investigations of Single-Subunit tRNA Methyltransferases from Yeast.Journal of fungi (Basel, Switzerland) · 2023Review
- The tRNA identity landscape for aminoacylation and beyond.Nucleic acids research · 2023Review
- Evolutionary repair reveals an unexpected role of the tRNA modification m1G37 in aminoacylation.Nucleic acids research · 2021Article
- Indirect Routes to Aminoacyl-tRNA: The Diversity of Prokaryotic Cysteine Encoding Systems.Frontiers in genetics · 2021Article
- The mammalian mitochondrial epitranscriptome.Biochimica et biophysica acta. Gene regulatory mechanisms · 2019Review
- Effects of Heterologous tRNA Modifications on the Production of Proteins Containing Noncanonical Amino Acids.Bioengineering (Basel, Switzerland) · 2018Article
- Structural basis for tRNA-dependent cysteine biosynthesis.Nature communications · 2017Article
- The central role of tRNA in genetic code expansion.Biochimica et biophysica acta. General subjects · 2017Review
- Article
- A genetically encoded fluorescent tRNA is active in live-cell protein synthesis.Nucleic acids research · 2017Article
- Trm5 and TrmD: Two Enzymes from Distinct Origins Catalyze the Identical tRNA Modification, m¹G37.Biomolecules · 2017Review
- Methyl transfer by substrate signaling from a knotted protein fold.Nature structural & molecular biology · 2016Article
- Non-canonical roles of tRNAs and tRNA mimics in bacterial cell biology.Molecular microbiology · 2016Review
- Crystallographic analysis of a subcomplex of the transsulfursome with tRNA for Cys-tRNA(Cys) synthesis.Acta crystallographica. Section F, Structural biology communications · 2016Article
- From Chemical Mutagenesis to Post-Expression Mutagenesis: A 50 Year Odyssey.Angewandte Chemie (International ed. in English) · 2016Review
- Efficient genetic encoding of phosphoserine and its nonhydrolyzable analog.Nature chemical biology · 2015Article
- Kinetic Analysis of tRNA Methyltransferases.Methods in enzymology · 2015Article
- Computational identification of a new SelD-like family that may participate in sulfur metabolism in hyperthermophilic sulfur-reducing archaea.BMC genomics · 2014Article
- Ancient translation factor is essential for tRNA-dependent cysteine biosynthesis in methanogenic archaea.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)) is required for translation and is typically synthesized by cysteinyl-tRNA synthetase (CysRS). However, Methanocaldococcus jannaschii synthesizes Cys-tRNA(Cys) by an indirect pathway, whereby O-phosphoseryl-tRNA synthetase (SepRS) acylates tRNA(Cys) with phosphoserine (Sep), and Sep-tRNA-Cys-tRNA synthase (SepCysS) converts the tRNA-bound phosphoserine to cysteine. We show here that M. jannaschii SepRS differs from CysRS by recruiting the m1G37 modification as a determinant for aminoacylation, and in showing limited discrimination against mutations of conserved nucleotides. Kinetic and binding measurements show that both SepRS and SepCysS bind the reaction intermediate Sep-tRNA(Cys) tightly, and these two enzymes form a stable binary complex that promotes conversion of the intermediate to the product and sequesters the intermediate from binding to elongation factor EF-1alpha or infiltrating into the ribosome. These results highlight the importance of the protein binary complex for efficient synthesis of Cys-tRNA(Cys).
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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.