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Showing 1 to 8 of 8 for “"Leucyl-tRNA synthetase (LeuRS)"”.
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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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Regulation of mTORC1 by homocysteine and its effects on autophagy in human and mouse neuronal tissues
… by a constitutive protein complex composed of leucyl-tRNA-synthetase (LeuRS) and folliculin (Flcn), which regulates mTOR tethering to lysosomal membranes. In hyper-homocysteinemic human cells and cystathionine [beta]-synthase-deficient mouse brains, an acute and chronic inhibition of autophagy, …
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Editing by leucyl-trna synthetase: Discrimination of norvaline and isoleucine
Aminoacyl tRNA-synthetases (AARS) are housekeeping enzymes that are tasked with accurate synthesis of aminoacylated tRNA for protein synthesis and other cellular functions. The specificity of amino acid attachment challenges the AARSs that need to distinguish between structurally similar amino …
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Leucyl-tRNA synthetase: dynamic subcellular relocalization and drug resistance mechanism
"The family of aminoacyl-tRNA synthetases (aaRS) are essential to all living cells. They are fundamental to setting the genetic code during protein synthesis by charging tRNA with a specific amino acid. As such, they have been selected by the pharmaceutical industries as optimal targets. A new …
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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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Mechanisms of leucyl-tRNA synthetase dependent group I intron splicing
Leucyl-tRNA synthetase (LeuRS) plays dual roles within the yeast mitochondria. In addition to protein synthesis, it is also essential to RNA splicing of critical respiratory genes. The LeuRS collaborates with a maturase to excise the bI4 and aI4α introns from the cob and cox1α genes respectively. …
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On the fidelity of translation
Aminoacyl-tRNA synthetases (aaRSs) set up the genetic code by covalently attaching the amino acids to their cognate tRNAs with a high specificity. For several aaRSs, mismatched products are cleared by hydrolytic editing mechanisms, which are essential to maintain the fidelity of translation. These …
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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