Dissertation/Thesis Abstract

Translational Fidelity of a Eukaryotic Glutaminyl-tRNA Synthetase with an N-terminal Domain Appendage
by Rogers, Aaron Bethea, M.S., Portland State University, 2014, 82; 1568586
Abstract (Summary)

Several Saccharomyces cerevisiae mutant tRNA- Q2 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 its role in the assembly of the multiple aminoacyl-tRNA synthetase complex.

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Indexing (document details)
Advisor: Perona, John
Commitee: Lehman, Niles, Peyton, David
School: Portland State University
Department: Chemistry
School Location: United States -- Oregon
Source: MAI 54/01M(E), Masters Abstracts International
Subjects: Molecular biology, Biochemistry
Keywords: Aminoacyl-tRNA synthetase, Glutaminyl-tRNA synthetase, Mars, Translation, tRNA
Publication Number: 1568586
ISBN: 978-1-321-31805-0
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