Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex.

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.
Mesh Terms:
Amino Acyl-tRNA Synthetases, Bacterial Proteins, Enzyme Activation, Guanosine Triphosphate, Histidine-tRNA Ligase, Humans, Leucine-tRNA Ligase, Macromolecular Substances, Peptide Elongation Factor 1, Precipitin Tests, Protein Binding, Protein Subunits, Recombinant Fusion Proteins, Serine Endopeptidases, Substrate Specificity, Two-Hybrid System Techniques
Biochem. Biophys. Res. Commun.
Date: Feb. 15, 2002
Download Curated Data For This Publication
2844
Switch View:
  • Interactions 9