ArticleProceedings of the National Academy of Sciences of the United States of America2009
The appearance of pyrrolysine in tRNAHis guanylyltransferase by neutral evolution.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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43 citing papers in PubMed, 55 citations in OpenAlex.
- Methanogenic archaea encoding Pyrrolysine maintain ambiguous amber codon usage.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Engineering Pyrrolysine Systems for Genetic Code Expansion and Reprogramming.Chemical reviews · 2024Review
- The life and times of a tRNA.RNA (New York, N.Y.) · 2023Review
- Update of the Pyrrolysyl-tRNA Synthetase/tRNAJournal of bacteriology · 2023Review
- Towards a Cure for HARS Disease.Genes · 2023Review
- Human Thg1 displays tRNA-inducible GTPase activity.Nucleic acids research · 2022Article
- Highlighting the Unique Roles of RadicalJournal of bacteriology · 2022Review
- Metascan: METabolic Analysis, SCreening and ANnotation of Metagenomes.Frontiers in bioinformatics · 2022Article
- Recoding of stop codons expands the metabolic potential of two novel Asgardarchaeota lineages.ISME communications · 2021Article
- Improved pyrrolysine biosynthesis through phage assisted non-continuous directed evolution of the complete pathway.Nature communications · 2021Article
- Review
- Programmed Deviations of Ribosomes From Standard Decoding in Archaea.Frontiers in microbiology · 2021Review
- Engineering aminoacyl-tRNA synthetases for use in synthetic biology.The Enzymes · 2020Article
- Review
- Minimal requirements for reverse polymerization and tRNA repair by tRNARNA biology · 2018Article
- Identification of distinct biological functions for four 3'-5' RNA polymerases.Nucleic acids research · 2016Article
- Pyrrolysyl-tRNA synthetase, an aminoacyl-tRNA synthetase for genetic code expansion.Croatica chemica acta. Arhiv za kemiju · 2016Article
- Template-dependent nucleotide addition in the reverse (3'-5') direction by Thg1-like protein.Science advances · 2016Article
- Genetic code flexibility in microorganisms: novel mechanisms and impact on physiology.Nature reviews. Microbiology · 2015Review
- In vitro substrate specificities of 3'-5' polymerases correlate with biological outcomes of tRNA 5'-editing reactions.FEBS letters · 2015Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
tRNA(His) guanylyltransferase (Thg1) post-transcriptionally adds a G (position -1) to the 5'-terminus of tRNA(His). The Methanosarcina acetivorans Thg1 (MaThg1) gene contains an in-frame TAG (amber) codon. Although a UAG codon typically directs translation termination, its presence in Methanosarcina mRNA may lead to pyrrolysine (Pyl) incorporation achieved by Pyl-tRNA(Pyl), the product of pyrrolysyl-tRNA synthetase. Sequencing of the MaThg1 gene and transcript confirmed the amber codon. Translation of MaThg1 mRNA led to a full-length, Pyl-containing, active enzyme as determined by immunoblotting, mass spectrometry, and biochemical analysis. The nature of the inserted amino acid at the position specified by UAG is not critical, as Pyl or Trp insertion yields active MaThg1 variants in M. acetivorans and equal amounts of full-length protein. These data suggest that Pyl insertion is akin to natural suppression and unlike the active stop codon reassignment that is required for selenocysteine insertion. Only three Pyl-containing proteins have been characterized previously, a set of methylamine methyltransferases in which Pyl is assumed to have specifically evolved to be a key active-site constituent. In contrast, Pyl in MaThg1 is a dispensable residue that appears to confer no selective advantage. Phylogenetic analysis suggests that Thg1 is becoming dispensable in the archaea, and furthermore supports the hypothesis that Pyl appeared in MaThg1 as the result of neutral evolution. This indicates that even the most unusual amino acid can play an ordinary role in proteins.
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