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Title[redir]:
Agmatine-conjugated cytidine in a tRNA anticodon is essential for AUA decoding in archaea | Nature Chemical Biology
Description:
Ribosomal decoding is dependent on wobble base pairing, which frequently involves modified nucleotides in the tRNA anticodon loop. The discovery of a new guanidine-modified base, 2-agmatinylcytidine, in the tRNAIle of archaea uncovers the mechanism for AUA decoding in these organisms. A modified base at the first (wobble) position of some tRNA anticodons is critical for deciphering the genetic code. In eukaryotes and eubacteria, AUA codons are decoded by tRNAsIle with modified bases pseudouridine (and/or inosine) and lysidine, respectively. The mechanism by which archaeal species translate AUA codons is unclear. We describe a polyamine-conjugated modified base, 2-agmatinylcytidine (agm2C or agmatidine), at the wobble position of archaeal tRNAIle that decodes AUA codons specifically. We demonstrate that archaeal cells use agmatine to synthesize agm2C of tRNAIle. We also identified a new enzyme, tRNAIle-agm2C synthetase (TiaS), that catalyzes agm2C formation in the presence of agmatine and ATP. Although agm2C is chemically similar to lysidine, TiaS constitutes a distinct class of enzyme from tRNAIle-lysidine synthetase (TilS), suggesting that the decoding systems evolved convergently across domains.
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Keywords {🔍}
article, google, scholar, cas, nature, trna, suzuki, japan, access, content, biology, agmc, science, chemical, aua, decoding, ikeuchi, tsutomu, lysidine, synthetase, biosynthesis, cookies, archaea, modified, wobble, trnas, biol, cell, privacy, function, structural, modification, codon, mol, chem, rna, identification, research, technology, essential, data, information, numata, mechanism, archaeal, trnaile, enzyme, tias, insights, isoleucine,
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nature portfolio scientific research permissions reprints privacy policy advertising ef-tu–isoleucine trna elucidate social media open thermo fischer scientific nature 336 nature 461 nature author information authors single post-transcriptional modification sulfur-oxidizing bacteria living author correspondence polyamine-conjugated modified base personal data springerlink instant access data protection supported chemical synthesis permissions takeo suzuki performed tsutomu suzuki designed privacy competing financial interests rna modification genes takashi yokogawa halobacterium volcanii trnas agmatine-conjugated cytidine rna-modifying enzymes european economic area issue learn institutional subscriptions read lysine-substituted nucleoside translational fidelity ensured de crecy-lagard japanese junior scientists medical genome sciences probing conformational transitions mutagenic watson–crick modified bases pseudouridine hyper-modified nucleoside accepting optional cookies chemical structure tsutomu suzuki archaea yoshiho ikeuchi minor isoleucine trna performed biochemical studies isoleucyl-trna synthetase
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headline:Agmatine-conjugated cytidine in a tRNA anticodon is essential for AUA decoding in archaea
description:Ribosomal decoding is dependent on wobble base pairing, which frequently involves modified nucleotides in the tRNA anticodon loop. The discovery of a new guanidine-modified base, 2-agmatinylcytidine, in the tRNAIle of archaea uncovers the mechanism for AUA decoding in these organisms.
A modified base at the first (wobble) position of some tRNA anticodons is critical for deciphering the genetic code. In eukaryotes and eubacteria, AUA codons are decoded by tRNAsIle with modified bases pseudouridine (and/or inosine) and lysidine, respectively. The mechanism by which archaeal species translate AUA codons is unclear. We describe a polyamine-conjugated modified base, 2-agmatinylcytidine (agm2C or agmatidine), at the wobble position of archaeal tRNAIle that decodes AUA codons specifically. We demonstrate that archaeal cells use agmatine to synthesize agm2C of tRNAIle. We also identified a new enzyme, tRNAIle-agm2C synthetase (TiaS), that catalyzes agm2C formation in the presence of agmatine and ATP. Although agm2C is chemically similar to lysidine, TiaS constitutes a distinct class of enzyme from tRNAIle-lysidine synthetase (TilS), suggesting that the decoding systems evolved convergently across domains.
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description:Ribosomal decoding is dependent on wobble base pairing, which frequently involves modified nucleotides in the tRNA anticodon loop. The discovery of a new guanidine-modified base, 2-agmatinylcytidine, in the tRNAIle of archaea uncovers the mechanism for AUA decoding in these organisms.
A modified base at the first (wobble) position of some tRNA anticodons is critical for deciphering the genetic code. In eukaryotes and eubacteria, AUA codons are decoded by tRNAsIle with modified bases pseudouridine (and/or inosine) and lysidine, respectively. The mechanism by which archaeal species translate AUA codons is unclear. We describe a polyamine-conjugated modified base, 2-agmatinylcytidine (agm2C or agmatidine), at the wobble position of archaeal tRNAIle that decodes AUA codons specifically. We demonstrate that archaeal cells use agmatine to synthesize agm2C of tRNAIle. We also identified a new enzyme, tRNAIle-agm2C synthetase (TiaS), that catalyzes agm2C formation in the presence of agmatine and ATP. Although agm2C is chemically similar to lysidine, TiaS constitutes a distinct class of enzyme from tRNAIle-lysidine synthetase (TilS), suggesting that the decoding systems evolved convergently across domains.
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