ArticleFEBS letters2012
Selenomodification of tRNA in archaea requires a bipartite rhodanese enzyme.
Article in FEBS letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- A Geranylated Natural Product Simamycin Disrupts the Allosteric Catalysis of tRNA-2-selenouridine Synthase SelU.Biochemistry · 2025Article
- Disproportionation of elemental sulfur byISME communications · 2025Article
- Article
- Naturally occurring modified ribonucleosides.Wiley interdisciplinary reviews. RNA · 2020Review
- C5-Substituted 2-Selenouridines Ensure Efficient Base Pairing with Guanosine; Consequences for Reading the NNG-3' Synonymous mRNA Codons.International journal of molecular sciences · 2020Article
- Rhodanese-Like Domain Protein UbaC and Its Role in Ubiquitin-Like Protein Modification and Sulfur Mobilization in Archaea.Journal of bacteriology · 2019Article
- Horizontal acquisition of hydrogen conversion ability and other habitat adaptations in the Hydrogenovibrio strains SP-41 and XCL-2.BMC genomics · 2019Article
- Diverse Mechanisms of Sulfur Decoration in Bacterial tRNA and Their Cellular Functions.Biomolecules · 2017Review
- Transfer RNA Bound to MnmH Protein Is Enriched with Geranylated tRNA--A Possible Intermediate in Its Selenation?PloS one · 2016Article
- Evolution of selenophosphate synthetases: emergence and relocation of function through independent duplications and recurrent subfunctionalization.Genome research · 2015Article
- Biochemical functional predictions for protein structures of unknown or uncertain function.Computational and structural biotechnology journal · 2015Review
- Objective: biochemical function.Frontiers in genetics · 2014Article
- The COMBREX project: design, methodology, and initial results.PLoS biology · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
5-Methylaminomethyl-2-selenouridine (mnm(5)Se(2)U) is found in the first position of the anticodon in certain tRNAs from bacteria, archaea and eukaryotes. This selenonucleoside is formed in Escherichia coli from the corresponding thionucleoside mnm(5)S(2)U by the monomeric enzyme YbbB. This nucleoside is present in the tRNA of Methanococcales, yet the corresponding 2-selenouridine synthase is unknown in archaea and eukaryotes. Here we report that a bipartite ybbB ortholog is present in all members of the Methanococcales. Gene deletions in Methanococcus maripaludis and in vitro activity assays confirm that the two proteins act in trans to form in tRNA a selenonucleoside, presumably mnm(5)Se(2)U. Phylogenetic data suggest a primal origin of seleno-modified tRNAs.
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