title: Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex.
abstract: Aminoacyl-tRNA synthetases (ARSs) ligate amino acids to their cognate tRNAs. It has been suggested that mammalian ARSs are linked to the EF-1 complex for efficient channeling of aminoacyl tRNAs to ribosome. Here we systemically investigated possible interactions between human ARSs and the subunits of EF-1 (alpha, beta, gamma, and delta) using a yeast two-hybrid assay. Among the 80 tested pairs, leucyl- and histidyl-tRNA synthetases were found to make strong and specific interaction with the EF-1gamma and beta while glu-proly-, glutaminyl-, alanyl-, aspartyl-, lysyl-, phenylalanyl-, glycyl-, and tryptophanyl-tRNA synthetases showed moderate interactions with the different EF-1 subunits. The interactions of leucyl- and histidyl-tRNA synthetase with the EF-1 complex were confirmed by immunoprecipitation and in vitro pull-down experiments. Interestingly, the aminoacylation activities of these two enzymes, but not other ARSs, were stimulated by the cofactor of EF-1, GTP. These data suggest that a systematic interaction network may exist between mammalian ARSs and EF-1 subunits probably to enhance the efficiency of in vivo protein synthesis.
authors.affiliation: National Creative Research Initiatives Center for ARS Network, College of Pharmacy, Seoul National University, Shinlim-Dong, Kwanak-Ku, Seoul, 157-742, Korea.
authors.forename: Jong
authors.initials: J
authors.lastname: Sang Lee
authors.forename: Sang
authors.initials: S
authors.lastname: Gyu Park
authors.forename: Heonyong
authors.initials: H
authors.lastname: Park
authors.forename: Wongi
authors.initials: W
authors.lastname: Seol
authors.forename: Sangwon
authors.initials: S
authors.lastname: Lee
authors.forename: Sunghoon
authors.initials: S
authors.lastname: Kim
mesh_terms: D000604:Amino Acyl-tRNA Synthetases / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics; D004789:Enzyme Activation / Q000187:drug effects; D006160:Guanosine Triphosphate / Q000494:pharmacology; D006643:Histidine-tRNA Ligase / Q000235:genetics / Q000378:metabolism; D006801:Humans; D007935:Leucine-tRNA Ligase / Q000235:genetics / Q000378:metabolism; D046911:Macromolecular Substances; D020648:Peptide Elongation Factor 1 / Q000235:genetics / Q000378:metabolism*; D011233:Precipitin Tests; D011485:Protein Binding / Q000502:physiology; D021122:Protein Subunits; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D012697:Serine Endopeptidases / Q000235:genetics; D013379:Substrate Specificity; D020798:Two-Hybrid System Techniques; D000099160:LexA Repressor Protein
chemical_list: D000604:Amino Acyl-tRNA Synthetases; D001426:Bacterial Proteins; D006160:Guanosine Triphosphate; D006643:Histidine-tRNA Ligase; D007935:Leucine-tRNA Ligase; D046911:Macromolecular Substances; D020648:Peptide Elongation Factor 1; D021122:Protein Subunits; D011993:Recombinant Fusion Proteins; D012697:Serine Endopeptidases; D000099160:LexA Repressor Protein