ArticlePloS one2014
Functional substitution of a eukaryotic glycyl-tRNA synthetase with an evolutionarily unrelated bacterial cognate enzyme.
Article in PloS one, 2014. 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, 25 citations in OpenAlex.
- Atypical Presentation ofJIMD reports · 2025Article
- Yeast models for Charcot-Marie-Tooth disease-causing aminoacyl-tRNA synthetase alleles reveal the cellular basis of disease.IUBMB life · 2025Review
- Loss-of-Function CARS1 Variants in a Patient With Microcephaly, Developmental Delay, and a Brittle Hair Phenotype.Molecular genetics & genomic medicine · 2025Article
- A model organism pipeline provides insight into the clinical heterogeneity of TARS1 loss-of-function variants.HGG advances · 2024Article
- Predictive modeling provides insight into the clinical heterogeneity associated withbioRxiv : the preprint server for biology · 2024Article
- DominantBrain communications · 2024Article
- Distinct localization of chiral proofreaders resolves organellar translation conflict in plants.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structural basis of a two-step tRNA recognition mechanism for plastid glycyl-tRNA synthetase.Nucleic acids research · 2023Article
- Gain of C-Ala enables AlaRS to target the L-shaped tRNAAla.Nucleic acids research · 2022Article
- Mitochondrial Aminoacyl-tRNA Synthetase and Disease: The Yeast Contribution for Functional Analysis of Novel Variants.International journal of molecular sciences · 2021Review
- Associations between Neurological Diseases and Mutations in the Human Glycyl-tRNA Synthetase.Biochemistry. Biokhimiia · 2021Review
- A Yeast-Based Model for Hereditary Motor and Sensory Neuropathies: A Simple System for Complex, Heterogeneous Diseases.International journal of molecular sciences · 2020Review
- GARS-related disease in infantile spinal muscular atrophy: Implications for diagnosis and treatment.American journal of medical genetics. Part A · 2020Article
- Alanyl-tRNA Synthetase 2 (AARS2)-Related Ataxia Without Leukoencephalopathy.Cerebellum (London, England) · 2020Article
- A recurrent GARS mutation causes distal hereditary motor neuropathy.Journal of the peripheral nervous system : JPNS · 2019Article
- Article
- A Novel Mutation in MARS in a Patient with Charcot-Marie-Tooth Disease, Axonal, Type 2U with Congenital Onset.Journal of neuromuscular diseases · 2019Article
- Hypermorphic and hypomorphic AARS alleles in patients with CMT2N expand clinical and molecular heterogeneities.Human molecular genetics · 2018Article
- MARS variant associated with both recessive interstitial lung and liver disease and dominant Charcot-Marie-Tooth disease.European journal of medical genetics · 2018Article
- Compound heterozygosity for loss-of-function GARS variants results in a multisystem developmental syndrome that includes severe growth retardation.Human mutation · 2017Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two oligomeric types of glycyl-tRNA synthetase (GlyRS) are found in nature: a α2 type and a α2β2 type. The former has been identified in all three kingdoms of life and often pairs with tRNAGly that carries an A73 discriminator base, while the latter is found only in bacteria and chloroplasts and is almost always coupled with tRNAGly that contains U73. In the yeast Saccharomyces cerevisiae, a single GlyRS gene, GRS1, provides both the cytoplasmic and mitochondrial functions, and tRNAGly isoacceptors in both compartments possess A73. We showed herein that Homo sapiens and Arabidopsis thaliana cytoplasmic GlyRSs (both α2-type enzymes) can rescue both the cytoplasmic and mitochondrial defects of a yeast grs1- strain, while Escherichia coli GlyRS (a α2β2-type enzyme) and A. thaliana organellar GlyRS (a (αβ)2-type enzyme) failed to rescue either defect of the yeast mull allele. However, a head-to-tail αβ fusion of E. coli GlyRS effectively supported the mitochondrial function. Our study suggests that a α2-type eukaryotic GlyRS may be functionally substituted with a α2β2-type bacterial cognate enzyme despite their remote evolutionary relationships.
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