Beyond building proteins: tRNA synthetases outside of translation

Beyond building proteins: tRNA synthetases outside of translation

Nature Medicine 22452–453 (2016) doi:10.1038/nm0516-452 Published online 05 May 2016


BSIP SA / Alamy Stock Photo

In the 1990s, biochemist Eric First came upon unusual similarities in parts of the amino acid sequences of a key molecule involved in protein synthesis and a cytokine called endothelial monocyte-activating polypeptide II1. At the time, the general reaction to these findings was surprise. Why would this protein-building enzyme look so similar to a cytokine that suppresses blood vessel growth and promotes inflammation?

Paul Schimmel, a molecular biologist with laboratories at both the California and Florida campuses of the Scripps Research Institute, was similarly skeptical when a postdoctoral scientist in his lab, Keisuke Wakasugi, showed him that this same enzyme—called tyrosyl-tRNA synthetase—could exit the cell and split into two chunks as the cell dies. Each chunk acted like a cytokine, inducing immune cells to move from one compartment of a cell migration assay to another.



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