Dissociating quaternary structure regulates cell-signaling functions of a secreted human tRNA synthetase.

@article{Vo2011DissociatingQS,
  title={Dissociating quaternary structure regulates cell-signaling functions of a secreted human tRNA synthetase.},
  author={M Y Vo and Xiang-Lei Yang and Paul R. Schimmel},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 13},
  pages={11563-8}
}
Many tRNA synthetases are homodimers that are catalytically inactive as monomers. An example is the 528-amino acid human tyrosyl-tRNA synthetase, which is made up of an N-terminal catalytic unit (TyrRS(Mini)) and a 164-amino acid C-domain. Although native TyrRS has no known cytokine functions, natural proteolysis of secreted TyrRS releases TyrRS(Mini), which not only has the same aminoacylation activity as native TyrRS but also has strong activity for stimulating migration of polymorphonuclear… CONTINUE READING

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