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Showing 1 to 10 of 10 for “"amino acid editing"”.
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CP1 domain of leucyl-tRNA synthetase: dissecting its dual roles in amino acid editing and RNA splicing
Item marked as restricted to the 'Administrator' Group (id=1) by William Ingram (wingram2@illinois.edu) on 2012-06-27T21:32:36Z Item is restricted until 2014-06-27T21:32:23Z
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Characterization of Leucyl -Trna Synthetase From Homo Sapiens and Escherichia Coli in Aminoacylation, Amino Acid Editing and Interdomain Interactions
… hscLeuRS possesses a secondary function beyond aminoacylation reliant on a doubly charged Leu-Leu-tRNALeu. Further biochemical analysis of the hscLeuRS focused on its editing pocket. The editing site of hscLeuRS includes a highly conserved threonine discriminator and universally conserved …
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Characterization of Leucyl -Trna Synthetase From Saccharomyces Cerevisiae and Escherichia Coli in Aminoacylation, Amino Acid Editing and Enzyme Inhibition
Because they are essential to protein synthesis, aaRSs offer a promising target for the development of novel drugs. Leucyl-adenylate analogs were tested for inhibition activity against LeuRS from different sources. These analogs efficiently inhibited the E. coli and Saccharomyces cerevisiae …
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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 …
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Characterization of Leucyl -Trna Synthetase From Escherichia Coli and Saccharomyces Cerevisiae in Aminoacylation, Amino Acid Editing, and Protein-Dependent RNA Splicing
… domain has uniquely adapted to accommodate aminoacylation, amino acid editing, and RNA-protein interactions.
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Characterization of the Fidelity Mechanisms of Leucyl -Trna Synthetases From Saccharomyces Cerevisiae and Escherichia Coli
… 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. However, unlike other origins, when …
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Dissection of Connective Beta -Strand Linkers and Their Role in Enzymatic Activities of Escherichia Coli Leucyl -Trna Synthetase
… glycine residues, when mutated to proline, misaminoacylate tRNALeu in spite of retaining efficient amino acid editing activities. It is possible that these mutant LeuRSs may have impaired the translocation of editing substrates between the aminoacylation and editing active sites. An additional …
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Characterization of Molecular Structure-Function Relationships of Escherichia Coli Leucyl-Trna Synthetase
The accurate covalent linkage of amino acid to tRNA for protein synthesis is catalyzed by a family of aminoacyl-tRNA synthetases (aaRS). Some aaRSs have the potential to make mistakes during aminoacylation due to the nature of their amino acid substrate. However, the synthetases have …
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Biochemical Analysis of the Molecular Factors of Leucyl-Trna Synthetase That Ensure Aminoacylation Fidelity
The tRNA synthetases catalyze aminoacylation of transfer RNA (tRNA) with specific amino acids. Accurate aminoacylation is critical to the fidelity of protein synthesis. Leucyl-tRNA synthetase (LeuRS) can misactivate a broad scope of non-leucine amino acids. In these cases, mischarged tRNA products …
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Mechanisms of leucyl-tRNA synthetase dependent group I intron splicing
… mutations have been isolated within the amino acid editing CP1 domain and restore native RNA splicing activity in the presence of an inactive maturase. Mutational analysis of these sites and the regions that surround them demonstrated that certain substitutions can also inactivate …