Mapping the human translation elongation factor eEF1H complex using the yeast two-hybrid system.

@article{Mansilla2002MappingTH,
  title={Mapping the human translation elongation factor eEF1H complex using the yeast two-hybrid system.},
  author={Francisco Mansilla and Irene Friis and Mandana Jadidi and Karen Margrethe Nielsen and Brian F. C. Clark and Charlotte Rohde Knudsen},
  journal={The Biochemical journal},
  year={2002},
  volume={365 Pt 3},
  pages={669-76}
}
In eukaryotes, the eukaryotic translation elongation factor eEF1A responsible for transporting amino-acylated tRNA to the ribosome forms a higher-order complex, eEF1H, with its guanine-nucleotide-exchange factor eEF1B. In metazoans, eEF1B consists of three subunits: eEF1B alpha, eEF1B eta and eEF1B gamma. The first two subunits possess the nucleotide-exchange activity, whereas the role of the last remains poorly defined. In mammals, two active tissue-specific isoforms of eEF1A have been… CONTINUE READING
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