Transfer RNA Identity Contributes to Transition State Stabilization During Aminoacyl-tRNA Synthesis
Document Type
Article
Publication Date
9-1-1999
Abstract
Sequence-specific interactions between aminoacyl-tRNA synthetases and their cognate tRNAs ensure both accurate RNA recognition and the efficient catalysis of aminoacylation. The effects of tRNATrP variants on the aminoacylation reaction catalyzed by wild-type Escherichia coli tryptophanyl-tRNA synthe-tase (TrpRS) have now been investigated by stopped-flow fluorimetry, which allowed a pre-steady-state analysis to be undertaken. This showed that tRNATrP identity has some effect on the ability of tRNA to bind the reaction intermediate TrpRS-tryptophanyl-adenylate, but predominantly affects the rate at which trypto-phan is transferred from TrpRS-tryptophanyl ade-nylate to tRNA. Use of the binding (KtRNA) and rate constants (k4) to determine the energetic levels of the various species in the aminoacylation reaction showed a difference of ∼2 kcal mol-1 in the barrier to transition state formation compared to wild-type for both tRNATrP A→C73 and
Recommended Citation
Ibba, M., Sever, S., Prætorius-Ibba, M. and Söll, D. (1999) Transfer RNA identity contributes to transition state stabilization during aminoacyl-tRNA synthesis. Nucleic Acids Res. 27, 3631-3637. https://doi.org/10.1093/nar/27.18.3631
Copyright
Oxford University Press
Comments
This article was originally published in Nucleic Acids Research, volume 27, in 1999. https://doi.org/10.1093/nar/27.18.3631