Portland State University. Department of Chemistry
Date of Publication
Master of Science (M.S.) in Chemistry
Aminoacyl-tRNA synthetases, RNA-protein interactions
1 online resource (vi, 74 pages)
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 its role in the assembly of the multiple aminoacyl-tRNA synthetase complex.
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Rogers, Aaron Bethea, "Translational Fidelity of a Eukaryotic Glutaminyl-tRNA Synthetase with an N-terminal Domain Appendage" (2014). Dissertations and Theses. Paper 2006.
FASTA sequences of Eukaryotic and Bacterial QRS sequences used for Figure S1
303099_supp_E04D2FAA-120A-11E4-B40B-C642EF8616FA.fasta (50 kB)
FASTA sequences of Sce tRNA
303099_supp_D2759D86-120A-11E4-88A2-4A632E1BA5B1.fasta (14 kB)
FASTA sequences of Eco tRNA
303099_supp_EB592AD4-120A-11E4-9A75-0C642E1BA5B1.fasta (98 kB)
FASTA sequences of Hsa tRNA
303099_supp_87A8E258-120B-11E4-8A45-6A43EF8616FA.zip (289387 kB)
Zip file of raw kinetic data
303099_supp_9C9F4C74-120B-11E4-9922-3945EF8616FA.xml (67 kB)
Spreadsheet (.xml) legend to eukaryotic QRS sequences in SD1