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Two oligomeric types of glycyl-tRNA synthetase (GlyRS) are found in nature: a α 2  type and a α 2 β 2  type. The former has been identified in all three kingdoms of life and often pairs with tRNA Gly  that carries an A73 discriminator base, while the latter is found only in bacteria and chloroplasts and is almost always coupled with tRNA Gly  that contains U73. In the yeast  Saccharomyces cerevisiae , a single GlyRS gene,  GRS1 , provides both the cytoplasmic and mitochondrial functions, and tRNA Gly  isoacceptors in both compartments possess A73. We showed herein that  Homo sapiens  and  Arabidopsis thaliana  cytoplasmic GlyRSs (both α 2 -type enzymes) can rescue both the cytoplasmic and mitochondrial defects of a yeast  grs1   -  strain, while  Escherichia coli  GlyRS (a α 2 β 2 -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 α 2 -type eukaryotic GlyRS may be functionally substituted with a α 2 β 2 -type bacterial cognate enzyme despite their remote evolutionary relationships.

Functional Substitution of a Eukaryotic Glycyl-tRNA Synthetase with an Evolutionarily Unrelated Bacterial Cognate Enzyme