title: Functional substitution of a eukaryotic glycyl-tRNA synthetase with an evolutionarily unrelated bacterial cognate enzyme.
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.
authors.affiliation: Department of Life Sciences, National Central University, Jung-li, Taiwan.
authors.forename: Chin-I
authors.initials: CI
authors.lastname: Chien
authors.affiliation: Department of Neurology, Landseed Hospital, Ping-jen, Taiwan.
authors.forename: Yu-Wei
authors.initials: YW
authors.lastname: Chen
authors.affiliation: Department of Life Sciences, National Central University, Jung-li, Taiwan.
authors.forename: Yi-Hua
authors.initials: YH
authors.lastname: Wu
authors.affiliation: Department of Life Sciences, National Central University, Jung-li, Taiwan.
authors.forename: Chih-Yao
authors.initials: CY
authors.lastname: Chang
authors.affiliation: Graduate Institute of Mathematics and Science Education, National Hsinchu University of Education, Hsinchu, Taiwan.
authors.forename: Tzu-Ling
authors.initials: TL
authors.lastname: Wang
authors.affiliation: Department of Life Sciences, National Central University, Jung-li, Taiwan.
authors.forename: Chien-Chia
authors.initials: CC
authors.lastname: Wang
mesh_terms: D049148:Aminoacylation; D000818:Animals; D001419:Bacteria / Q000201:enzymology; D001483:Base Sequence; D003001:Cloning, Molecular; D056890:Eukaryota / Q000201:enzymology*; D019143:Evolution, Molecular; D055786:Gene Knockout Techniques; D006032:Glycine-tRNA Ligase / Q000737:chemistry / Q000172:deficiency / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008928:Mitochondria / Q000235:genetics / Q000378:metabolism; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D021381:Protein Transport
chemical_list: D006032:Glycine-tRNA Ligase
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