<p> Several <i>Saccharomyces cerevisiae</i> mutant tRNA-<sup> Q2</sup> species (glutamine isoacceptor, CUG anticodon) were synthesized and assayed for aminoacylation activity with <i>Saccharomyces cerevisiae </i> 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 <i>Escherichia coli</i>, but with slightly relaxed specificity as revealed by comparison of <i>k</i><sub>cat</sub>/<i>K</i><sub>M</sub> values relative to wild type <i>in vitro</i> transcribed tRNA. Additionally the eukaryotic N-terminal domain appendage, as found in <i>Sce</i> 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.</p>
| Identifer | oai:union.ndltd.org:PROQUEST/oai:pqdtoai.proquest.com:1568586 |
| Date | 16 December 2014 |
| Creators | Rogers, Aaron Bethea |
| Publisher | Portland State University |
| Source Sets | ProQuest.com |
| Language | English |
| Detected Language | English |
| Type | thesis |
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