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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|Commitee:||Lehman, Niles, Peyton, David|
|School:||Portland State University|
|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|
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