ArticleJournal of bacteriology2002
Functional annotation of class I lysyl-tRNA synthetase phylogeny indicates a limited role for gene transfer.
Article in Journal of bacteriology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 39 citations in OpenAlex.
- Determining the Identity Nucleotides and the Energy of Binding of tRNAs to Their Aminoacyl-tRNA Synthetases Using a Simple Logistic Model.Life (Basel, Switzerland) · 2024Article
- Structural Computational Analysis of the Natural History of Class I aminoacyl-tRNA Synthetases Suggests their Role in Establishing the Genetic Code.Journal of molecular evolution · 2021Article
- Review
- Emergence and evolution.Topics in current chemistry · 2014Review
- Prediction and classification of aminoacyl tRNA synthetases using PROSITE domains.BMC genomics · 2010Article
- Weighted bootstrapping: a correction method for assessing the robustness of phylogenetic trees.BMC evolutionary biology · 2010Article
- Translation termination in pyrrolysine-utilizing archaea.FEBS letters · 2009Article
- Anticodon recognition and discrimination by the alpha-helix cage domain of class I lysyl-tRNA synthetase.Biochemistry · 2007Article
- The amino-terminal domain of pyrrolysyl-tRNA synthetase is dispensable in vitro but required for in vivo activity.FEBS letters · 2007Article
- Recognition of pyrrolysine tRNA by the Desulfitobacterium hafniense pyrrolysyl-tRNA synthetase.Nucleic acids research · 2007Article
- In silico detection of tRNA sequence features characteristic to aminoacyl-tRNA synthetase class membership.Nucleic acids research · 2007Article
- Pyrrolysine analogues as substrates for pyrrolysyl-tRNA synthetase.FEBS letters · 2006Article
- Complete genome sequence of the marine, chemolithoautotrophic, ammonia-oxidizing bacterium Nitrosococcus oceani ATCC 19707.Applied and environmental microbiology · 2006Article
- Discrimination of cognate and noncognate substrates at the active site of class I lysyl-tRNA synthetase.Biochemistry · 2006Article
- TFAM detects co-evolution of tRNA identity rules with lateral transfer of histidyl-tRNA synthetase.Nucleic acids research · 2006Article
- Article
- Human lysyl-tRNA synthetase is secreted to trigger proinflammatory response.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- An aminoacyl-tRNA synthetase that specifically activates pyrrolysine.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- On the evolution of structure in aminoacyl-tRNA synthetases.Microbiology and molecular biology reviews : MMBR · 2003Review
- Nonorthologous replacement of lysyl-tRNA synthetase prevents addition of lysine analogues to the genetic code.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Functional and comparative genomic studies have previously shown that the essential protein lysyl-tRNA synthetase (LysRS) exists in two unrelated forms. Most prokaryotes and all eukaryotes contain a class II LysRS, whereas most archaea and a few bacteria contain a less common class I LysRS. In bacteria the class I LysRS is only found in the alpha-proteobacteria and a scattering of other groups, including the spirochetes, while the class I protein is by far the most common form of LysRS in archaea. To investigate this unusual distribution we functionally annotated a representative phylogenetic sampling of LysRS proteins. Class I LysRS proteins from a variety of bacteria and archaea were characterized in vitro by their ability to recognize Escherichia coli tRNA(Lys) anticodon mutants. Class I LysRS proteins were found to fall into two distinct groups, those that preferentially recognize the third anticodon nucleotide of tRNA(Lys) (U36) and those that recognize both the second and third positions (U35 and U36). Strong recognition of U35 and U36 was confined to the pyrococcus-spirochete grouping within the archaeal branch of the class I LysRS phylogenetic tree, while U36 recognition was seen in other archaea and an example from the alpha-proteobacteria. Together with the corresponding phylogenetic relationships, these results suggest that despite its comparative rarity the distribution of class I LysRS conforms to the canonical archaeal-bacterial division. The only exception, suggested from both functional and phylogenetic data, appears to be the horizontal transfer of class I LysRS from a pyrococcal progenitor to a limited number of bacteria.
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