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Updated: Aug 9, 2026

Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses
Published on: February 26, 2011
Relationship of two human tRNA synthetases used in cell signaling
Xiang-Lei Yang1, Paul Schimmel, Karla L Ewalt
1The Skaggs Institute for Chemical Biology, The Scripps Research Institute, BCC379, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Abstract:
Human tyrosyl-tRNA synthetase (TyrRS) and tryptophanyl-tRNA synthetase (TrpRS) are closely related, dual function enzymes that act in protein biosynthesis and angiogenesis. The recent crystallographic structures of these two enzymes show that they adopt remarkably similar three-dimensional (3D) architectures, being more like each other than like their respective prokaryotic orthologs. In particular, adaptations to the anticodon recognition domain of TyrRS cause distinct appended domains in TyrRS and TrpRS to occupy the same 3D space and thus to mask a common surface on each synthetase. Thought to be important for cell-signaling activity, this surface is made accessible by proteolytic cleavage, thereby activating the cell-signaling function of these enzymes.
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