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Title:
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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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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