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• W2014863886 endingPage "164" @default.
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• W2014863886 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." @default.
• W2014863886 created "2016-06-24" @default.
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• W2014863886 date "2002-02-01" @default.
• W2014863886 modified "2023-10-12" @default.
• W2014863886 title "Interaction Network of Human Aminoacyl-tRNA Synthetases and Subunits of Elongation Factor 1 Complex" @default.
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• W2014863886 doi "https://doi.org/10.1006/bbrc.2002.6398" @default.
• W2014863886 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11829477" @default.
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