Global ETD Search
Search theses and dissertations gathered from participating repositories worldwide. Every result links back to the library that holds it. No account is needed.
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Showing 1 to 20 of 77 for “"tRNA synthetase"”.
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Tumor Suppression by a TRNA Synthetase
… 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 mammary …
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STUDIES OF THE PYRROLYSYL-TRNA SYNTHETASE
… amino acid encoded by the UAG codon. Pyrrolysyl-tRNA synthetase (PylS) is the specific enzyme that can attach Pyl to its cognate tRNA, the amber suppressor tRNAPyl. The biosynthesis of pyrrolysine required the function of three genes, pylC, pylB, pylD, which were identified in the same apparent …
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Modelling neuronal mitochondrial aminoacyl-tRNA synthetase defects
… muscle. Mutations in mitochondrial aminoacyl-tRNA synthetase (MT-ARS) genes, which are crucial for mitochondrial protein synthesis and energy production via oxidative phosphorylation, are implicated in a variety of severe neurological and multisystemic diseases. Among these, mutations in …
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Characterizing CMT-causing variants in tryptophanyl- tRNA synthetase
Aminoacyl-tRNA synthetases (aaRSs) are essential enzymes that link amino acids to their cognate tRNAs. Neurological conditions, such as Charcot-Marie-Tooth (CMT) disease, have been linked to variants identified in these enzymes. I created a humanized yeast model to assess the underlying …
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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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Functional analysis of a class II aminoacyl-tRNA synthetase
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 1994.
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Amino acid recognition by a Class I tRNA synthetase
Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 1996.
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Reactions of isoleucyl-tRNA synthetase from Escherichia coli B.
Thesis: Ph. D., Massachusetts Institute of Technology, Department of Chemistry, 1972
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Experimental and Computational Dynamics of an Aminoacyl-tRNA Synthetase System
… recognition and aminoacylation of transfer RNA (tRNA) by their cognate aminoacyl-tRNA synthetases (AARSs). Methionine is the amino acid that acts as the start codon for every protein and can also be found within a protein message. Methionyl-tRNA synthetase (MetRS) is responsible for the correct …
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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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tRNA-dependent amino acid discrimination by Escherichia coli valyl-tRNA synthetase
<p>Valyl-tRNA synthetase (ValRS) has difficulty discriminating between its cognate amino acid, valine, and structurally similar amino acids, particularly threonine. To minimize translational errors, the enzyme catalyzes a tRNA-dependent editing reaction that prevents accumulation of misacylated …
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NMR studies of RNA binding domains of human lysyl aminoacyl tRNA synthetase
<p>Human lysyl aminoacyl tRNA synthetase (hLysRS) is a multi-functional aminoacyl tRNA synthetase which is primarily involved in protein biosynthesis as well as crucial processes ranging from proinflammatory response to signal transduction. One important, non-canonical function of hLysRS is to …
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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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Characterizing the landscape of aminoacyl-tRNA synthetase protein production in Bacillus subtilis
… Here I use a model enzyme family, the aminoacyl tRNA synthetases (aaRS), to explore how sensitive Bacillus subtilis are to changes in aaRS production from the molecular to phenotypic level. This culmination of protein levels, functional output, and fitness, leads to a complete "fitness landscape" …
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FUNCTIONAL EFFECT OF ALTERATIONS TO E. coli METHIONYL-tRNA SYNTHETASE BETA-LINKER LENGTH
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that catalyze the
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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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