Global ETD Search
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Showing 1 to 2 of 2 for “"fidelity in protein synthesis"”.
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Characterization of the Fidelity Mechanisms of Leucyl -Trna Synthetases From Saccharomyces Cerevisiae and Escherichia Coli
We tested several mutations in yeast mitochondrial LeuRS that altered the post-transfer editing function of LeuRSs from other origins. Our results show that yeast mitochondrial LeuRS has maintained a competent editing active site for post-transfer editing of mischarged tRNA similar to other LeuRSs. …
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Characterization of leucyl-TRNA synthetase from homo sapiens and escherichia coli in aminoacylation, amino acid editing and interdomain interactions
Aminoacyl-tRNA synthetases (aaRSs) are ancient enzymes that charge tRNA with its cognate amino acid. In order to maintain fidelity during protein synthesis, editing mechanisms ensure that tRNAs are accurately charged. Leucyl-tRNA synthetase (LeuRS) has an editing active site that resides in a …