ArticleProceedings of the National Academy of Sciences of the United States of America2003
A noncognate aminoacyl-tRNA synthetase that may resolve a missing link in protein evolution.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
44 citing papers in PubMed, 75 citations in OpenAlex.
- Architecture ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- AARS Online: A collaborative database on the structure, function, and evolution of the aminoacyl-tRNA synthetases.IUBMB life · 2024Article
- Enzymic recognition of amino acids drove the evolution of primordial genetic codes.Nucleic acids research · 2024Article
- Genetically stable kill-switch using "demon and angel" expression construct of essential genes.Frontiers in bioengineering and biotechnology · 2024Article
- Aminoacyl-tRNA synthetases.RNA (New York, N.Y.) · 2020Review
- Article
- Old enzymesThe Journal of biological chemistry · 2018Article
- An unexpected vestigial protein complex reveals the evolutionary origins of anThe Journal of biological chemistry · 2018Article
- Crystal structure of the N-terminal anticodon-binding domain of the nondiscriminating aspartyl-tRNA synthetase from Helicobacter pylori.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- Plasmodium Apicoplast Gln-tRNAGln Biosynthesis Utilizes a Unique GatAB Amidotransferase Essential for Erythrocytic Stage Parasites.The Journal of biological chemistry · 2015Article
- Trans-oligomerization of duplicated aminoacyl-tRNA synthetases maintains genetic code fidelity under stress.Nucleic acids research · 2015Article
- Identification of Chemical Compounds That Inhibit the Function of Glutamyl-tRNA Synthetase from Pseudomonas aeruginosa.Journal of biomolecular screening · 2015Article
- Structure of the Pseudomonas aeruginosa transamidosome reveals unique aspects of bacterial tRNA-dependent asparagine biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Evolutionary insights about bacterial GlxRS from whole genome analyses: is GluRS2 a chimera?BMC evolutionary biology · 2014Article
- A tRNA-independent mechanism for transamidosome assembly promotes aminoacyl-tRNA transamidation.The Journal of biological chemistry · 2013Article
- Expression of Shigella flexneri gluQ-rs gene is linked to dksA and controlled by a transcriptional terminator.BMC microbiology · 2012Article
- Rational design and directed evolution of a bacterial-type glutaminyl-tRNA synthetase precursor.Nucleic acids research · 2012Article
- Riboswitch (T-box)-mediated control of tRNA-dependent amidation in Clostridium acetobutylicum rationalizes gene and pathway redundancy for asparagine and asparaginyl-trnaasn synthesis.The Journal of biological chemistry · 2012Article
- The asparagine-transamidosome from Helicobacter pylori: a dual-kinetic mode in non-discriminating aspartyl-tRNA synthetase safeguards the genetic code.Nucleic acids research · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Efforts to delineate the advent of many enzymes essential to protein translation are often limited by the fact that the modern genetic code evolved before divergence of the tree of life. Glutaminyl-tRNA synthetase (GlnRS) is one noteworthy exception to the universality of the translation apparatus. In eukaryotes and some bacteria, this enzyme is essential for the biosynthesis of Gln-tRNAGln, an obligate intermediate in translation. GlnRS is absent, however, in archaea, and most bacteria, organelles, and chloroplasts. Phylogenetic analyses predict that GlnRS arose from glutamyl-tRNA synthetase (GluRS), via gene duplication with subsequent evolution of specificity. A pertinent question to ask is whether, in the advent of GlnRS, a transient GluRS-like intermediate could have been retained in an extant organism. Here, we report the discovery of an essential GluRS-like enzyme (GluRS2), which coexists with another GluRS (GluRS1) in Helicobacter pylori. We show that GluRS2's primary role is to generate Glu-tRNAGln, not Glu-tRNAGlu. Thus, GluRS2 appears to be a transient GluRS-like ancestor of GlnRS and can be defined as a GluGlnRS.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.