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Showing 1 to 13 of 13 for “"Aminoacyl-tRNA synthetases (AARSs)"”.
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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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BIOCHEMICAL ANALYSIS OF TWO DISTINCT METHIONYL-TRNA SYNTHETASES
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that catalyze the attachment of amino acids to their cognate tRNAs for protein biosynthesis at the ribosome. The long term objective of this project is to investigate catalytic features of methionyl-tRNA synthetase (MetRS) from two different …
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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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Engineering exclusively-quadruplet codon translation in vivo
… the task of assembling enough quadruplet-tRNAs (qtRNAs) to implement an all-quadruplet code remains a major hurdle. Here, we create qtRNAs that decode canonical amino acids by modifying E. coli tRNAs that continue to rely upon endogenous aminoacyl-tRNA synthetases (AARSs) for charging. We …
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Experimental and Computational Dynamics of an Aminoacyl-tRNA Synthetase System
… is dependent upon correct 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) …
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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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Establishing new approaches to unveil regulatory functions of tRNAs and their interactors
… study living systems. However, once the role of tRNAs was established in protein synthesis, the field moved on to other areas of the RNA world. With the mainstream application of systems-wide approaches, tRNAs have emerged as implicated in multiple regulatory networks beyond translation. These …
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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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Evolution and dynamic behavior of transfer RNA in the first two steps of translation
… of the cellular machinery is transfer RNA (tRNA). This small nucleic acid is crucial to the maintenance of the genetic code because it discriminately binds the messenger RNA codon at the ribosome and adds the cognate amino acid to the growing polypeptide chain. The role of tRNA as an adaptor …
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Simulation and visualization of dynamics in RNA-protein complexes in translation
… the molecular instantiation of the genetic code, tRNA plays a central role in the translational machinery where it interacts with several proteins and other RNAs during the course of protein synthesis. We use molecular dynamics (MD) simulations informed by evolutionary analysis to investigate the …
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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 amino …
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Assembly And Function Of Macromolecular Complexes For Accurate Trna Aminoacylation In Helicobacter Pylori
… OF MACROMOLECULAR COMPLEXES FOR ACCURATE TRNA AMINOACYLATION IN <i>HELICOBACTER PYLORI</i> </strong> </p> <p>by</p> <p> <strong>GAYATHRI SILVA</strong> </p> <p>January 2014</p> <p>Advisor: Dr. Tamara L. Hendrickson</p> <p>Major: Chemistry (Biochemistry)</p> <p>Degree: Doctor of …
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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