ArticleNucleic acids research2012
Trans-kingdom rescue of Gln-tRNAGln synthesis in yeast cytoplasm and mitochondria.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- Adaptation of a eukaryote-like ProRS to a prokaryote-like tRNAPro.Nucleic acids research · 2024Article
- Modulating the Structure and Function of an Aminoacyl-tRNA Synthetase Cofactor by Biotinylation.The Journal of biological chemistry · 2016Article
- A WHEP Domain Regulates the Dynamic Structure and Activity of Caenorhabditis elegans Glycyl-tRNA Synthetase.The Journal of biological chemistry · 2016Article
- Divergent Alanyl-tRNA Synthetase Genes of Vanderwaltozyma polyspora Descended from a Common Ancestor through Whole-Genome Duplication Followed by Asymmetric Evolution.Molecular and cellular biology · 2015Article
- Functional substitution of a eukaryotic glycyl-tRNA synthetase with an evolutionarily unrelated bacterial cognate enzyme.PloS one · 2014Article
- An insertion peptide in yeast glycyl-tRNA synthetase facilitates both productive docking and catalysis of cognate tRNAs.Molecular and cellular biology · 2013Article
- Unusual domain architecture of aminoacyl tRNA synthetases and their paralogs from Leishmania major.BMC genomics · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aminoacylation of transfer RNA(Gln) (tRNA(Gln)) is performed by distinct mechanisms in different kingdoms and represents the most diverged route of aminoacyl-tRNA synthesis found in nature. In Saccharomyces cerevisiae, cytosolic Gln-tRNA(Gln) is generated by direct glutaminylation of tRNA(Gln) by glutaminyl-tRNA synthetase (GlnRS), whereas mitochondrial Gln-tRNA(Gln) is formed by an indirect pathway involving charging by a non-discriminating glutamyl-tRNA synthetase and the subsequent transamidation by a specific Glu-tRNA(Gln) amidotransferase. Previous studies showed that fusion of a yeast non-specific tRNA-binding cofactor, Arc1p, to Escherichia coli GlnRS enables the bacterial enzyme to substitute for its yeast homologue in vivo. We report herein that the same fusion enzyme, upon being imported into mitochondria, substituted the indirect pathway for Gln-tRNA(Gln) synthesis as well, despite significant differences in the identity determinants of E. coli and yeast cytosolic and mitochondrial tRNA(Gln) isoacceptors. Fusion of Arc1p to the bacterial enzyme significantly enhanced its aminoacylation activity towards yeast tRNA(Gln) isoacceptors in vitro. Our study provides a mechanism by which trans-kingdom rescue of distinct pathways of Gln-tRNA(Gln) synthesis can be conferred by a single enzyme.
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