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Copyright © 1999 Cell Press. All rights reserved.
Molecular Cell, Volume 4, Issue 4, 519-528, 1 October 1999
doi:10.1016/S1097-2765(00)80203-8
Article
Transfer RNA–Dependent Translocation of Misactivated Amino Acids to Prevent Errors in Protein Synthesis
Tyzoon K. Nomanbhoy1, Tamara L. Hendrickson1 and Paul Schimmel1, *, *, 
Corresponding author: Paul Schimmel, 858 784 8970 (phone), 858 784 8990 (fax)Summary
Misactivation of amino acids by aminoacyl-tRNA synthetases can lead to significant errors in protein synthesis that are prevented by editing reactions. As an example, discrete sites in isoleucyl-tRNA synthetase for amino acid activation and editing are about 25 Å apart. The details of how misactivated valine is translocated from one site to the other are unknown. Here, we present a kinetic study in which a fluorescent probe is used to monitor translocation of misactivated valine from the active site to the editing site. Isoleucine-specific tRNA, and not other tRNAs, is essential for translocation of misactivated valine. Misactivation and translocation occur on the same enzyme molecule, with translocation being rate limiting for editing. These results illustrate a remarkable capacity for a specific tRNA to enhance amino acid fine structure recognition by triggering a unimolecular translocation event.
