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Showing 1 to 20 of 21 for “"leucyl-tRNA synthetase"”.
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Exogenous leucyl-tRNA synthetase inhibits mouse skeletal muscle differentiation
Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2024-05-01
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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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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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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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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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A novel regulatory role of leucyl-tRNA synthetase in supporting human cancer growth
Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2026-12-01
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Biochemical Analysis of the Molecular Factors of Leucyl -Trna Synthetase That Ensure Aminoacylation Fidelity
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2009.
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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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Novel and critical function of leucyl-tRNA synthetase in maintaining gastric carcinoma cell homeostasis
Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2025-05-01
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Non-canonical functions of leucyl-tRNA synthetase: Mechanism of cell growth and skeletal myogenesis
… work I have investigated the role of leucyl-tRNA synthetase (LRS) as a leucine sensor regulating mTORC1 activity in cell growth, myogenic differentiation, and skeletal muscle regeneration. Amino acid availability activates signaling by mTORC1. The class III PI-3-kinase Vps34 mediates …
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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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Dissection of Connective Beta -Strand Linkers and Their Role in Enzymatic Activities of Escherichia Coli Leucyl -Trna Synthetase
… 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 T252A …
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Characterization of Leucyl -Trna Synthetase From Homo Sapiens and Escherichia Coli in Aminoacylation, Amino Acid Editing and Interdomain Interactions
… that it attaches a second leucine to Leu-tRNALeu. Liquid chromatography and mass spectrometry methods were used in an attempt to isolate this hypothesized ""doubly charged"" tRNA species and it is possible that hscLeuRS possesses a secondary function beyond aminoacylation reliant on a …
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Characterization of Leucyl -Trna Synthetase From Saccharomyces Cerevisiae and Escherichia Coli in Aminoacylation, Amino Acid Editing and Enzyme Inhibition
… 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 mitochondrial LeuRS enzymes with low nanomolar K I's, but had no …
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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
Using extensive deletion and site-directed mutagenesis, we characterized the C-terminal domain of LeuRSs from different origins to understand its role. The results demonstrated that the native environment of the enzyme influenced the functional role of the unique C-terminal domain of both LeuRSs. …
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Enzymatic and Splicing Activity of Class I Leucyl -Trna Synthetases From Escherichia Coli and Saccharomyces Cerevisiae
Leucyl-tRNA synthetase from yeast mitochondria is also required for splicing of the mitochondrial bI4 and al4a introns. Splicing of these introns is dependent on coordination between ymLeuRS and bI4 maturase. An in vitro splicing assay has been established that is based on assembly of proteins into …
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The C-terminal domains of leucyl-tRNA synthetases
The mitochondrial Leucyl-tRNA synthetase (mtLeuRS) of certain Caenorhabditis species contains an idiosyncratic C-terminal addition. Bioinformatic analyses identified this domain in the mtLeuRS and also four putative nuclear localization sequences (NLSs) encoded within the domain (Ezak, Hong, …
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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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Tumor Suppression by a TRNA Synthetase
… thesis, we report the surprising finding that leucyl-tRNA synthetase (LARS), a tRNA synthetase responsible for ligating leucine to corresponding leucyl-tRNAs, becomes strongly repressed during mammary cell transformation and in breast cancer. Monoallelic genetic inactivation of LARS in mouse …
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