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Translational Fidelity Of A Eukaryotic Glutaminyl-Trna Synthetase With An N-Terminal Domain Appendage, Aaron Bethea Rogers
Translational Fidelity Of A Eukaryotic Glutaminyl-Trna Synthetase With An N-Terminal Domain Appendage, Aaron Bethea Rogers
Dissertations and Theses
Several Saccharomyces cerevisiae mutant tRNAQ2 species (glutamine isoacceptor, CUG anticodon) were synthesized and assayed for aminoacylation activity with Saccharomyces cerevisiae glutaminyl-tRNA synthetase. The derived steady state parameters were compared to similar datasets from the literature. The mutants behaved analogously to similar mutant species based on tRNA from Escherichia coli, but with slightly relaxed specificity as revealed by comparison of kcat/KM values relative to wild type in vitro transcribed tRNA. Additionally the eukaryotic N-terminal domain appendage, as found in Sce glutaminyl-tRNA synthetase, is considered in light of the discovery of non-canonical aminoacyl-tRNA synthetase functions, including …