Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase

The Journal of Biological Chemistry
Anand Minajigi, Christopher Francklyn

Abstract

Aminoacyl-tRNA synthetases hydrolyze aminoacyl adenylates and aminoacyl-tRNAs formed from near-cognate amino acids, thereby increasing translational fidelity. The contributions of pre- and post-transfer editing pathways to the fidelity of Escherichia coli threonyl-tRNA synthetase (ThrRS) were investigated by rapid kinetics. In the pre-steady state, asymmetric activation of cognate threonine and noncognate serine was observed in the active sites of dimeric ThrRS, with similar rates of activation. In the absence of tRNA, seryl-adenylate was hydrolyzed 29-fold faster by the ThrRS catalytic domain than threonyl-adenylate. The rate of seryl transfer to cognate tRNA was only 2-fold slower than threonine. Experiments comparing the rate of ATP consumption to the rate of aminoacyl-tRNA(AA) formation demonstrated that pre-transfer hydrolysis contributes to proofreading only when the rate of transfer is slowed significantly. Thus, the relative contributions of pre- and post-transfer editing in ThrRS are subject to modulation by the rate of aminoacyl transfer.

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Related Concepts

Biochemical Pathway
Alkalescens-Dispar Group
Amino Acids, I.V. solution additive
MT-TA gene
Triplet Codon-amino Acid Adaptor Activity
Transfer RNA
RNA Editing
Threonine-tRNA Ligase
Adenylate
Solvents

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