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.
Results
Showing 1 to 20 of 22 for “"aaRSs"”.
-
FUNCTIONAL EFFECT OF ALTERATIONS TO E. coli METHIONYL-tRNA SYNTHETASE BETA-LINKER LENGTH
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that catalyze the
-
Characterization of Molecular Structure-Function Relationships of Escherichia Coli Leucyl-Trna Synthetase
… 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 idiosyncratically evolved to include various modules to optimize activity and also enhance fidelity. …
-
Characterization of Amino Acid tRNA Ligases using the Analytical Ultracentrifuge
… were used in these investigations. The aaRSs were obtained from bacteria and yeast: LysRS and ValRS from S. cerevisiae, AspRS, LysRS and SerRS from E. coli, AsnRS, LysRS, SerRS and ValRS from Bacillus stearothermophilus. The quaternary structures of ValRSs from S. cerevisiae and B. …
-
Evolution and dynamic behavior of transfer RNA in the first two steps of translation
… are still emerging. Aminoacyl-tRNA synthetases (aaRSs) are enzymes that recognize specific tRNAs and amino acids from the cellular pool and facilitate the charging of the correct amino acids on tRNAs. Following aminoacylation, tRNAs dissociate from the aaRSs and bind the elongation factor Tu …
-
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 …
-
Engineering exclusively-quadruplet codon translation in vivo
… rely upon endogenous aminoacyl-tRNA synthetases (AARSs) for charging. We find that AARSs generally tolerate quadruplet anticodons, resulting in efficient, selectively charged qtRNAs for eight of the twenty canonical amino acids, as well as candidate qtRNAs for the remaining 12 amino acids. We …
-
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 …
-
Editing by leucyl-trna synthetase: Discrimination of norvaline and isoleucine
… of amino acid attachment challenges the AARSs that need to distinguish between structurally similar amino acids. In such cases, AARSs have developed editing mechanisms to circumvent the issue of misaminoacylation. Leucyl-tRNA synthetase (LeuRS), for instance selectively edits misactivated …
-
Non-canonical functions of leucyl-tRNA synthetase: Mechanism of cell growth and skeletal myogenesis
… myogenesis among the aminoacyl-tRNA synthetases (AARSs). A few of AARSs were discovered to be negative regulators based on the knockdown phenotypes, but the majority appeared to be positive regulators of myoblast differentiation. It is intriguing, aside from LRS, that only a small number of AARSs …
-
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 …
-
Establishing new approaches to unveil regulatory functions of tRNAs and their interactors
… functions of aminoacyl tRNA synthetases (aaRSs). For example, Tyrosyl-tRNA synthetase (YARS) was seen to translocate to the nucleus upon genotoxic stress. By applying a novel method (infSILAC), it is possible to quantitatively identify direct interactors and provide a solution to the …
-
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 …
-
Experimental and Computational Dynamics of an Aminoacyl-tRNA Synthetase System
… 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 recognition and aminoacylation of tRNAMet. The …
-
Leucyl-tRNA synthetase: dynamic subcellular relocalization and drug resistance mechanism
… precise control of aminoacylation fidelity. The aaRSs have also been adapted through evolution for alternate functions that are entirely distinct from proteins synthesis. In E. coli, small fractions of LeuRS were identified outside the cytoplasm, in the periplasmic space and also associated with …
-
Identification and Evolution of New Orthogonal Aminoacyl-tRNA Synthetase/tRNA Pairs for Genetic Code Expansion
… likelihood to be recognised by the endogenous aaRSs in E. coli, our model organism. I then developed a rapid, scalable new in vitro approach, named tRNA Extension (tREX), to determine the in vivo aminoacylation status of tRNAs. Using tREX, 243 candidate tRNAs were tested in E. coli and 71 …
-
The Development and Application of Methods to Study the Evolution of Specificity, Allostery, and RNA -Protein Interactions in Translation
… that evolved as specificity emerged in the AARSs. In the second step of translation, the elongation factor Tu (EF-Tu) binds to all the standard aminoacyl-transfer RNAs and transports them to the ribosome. Combined energetic and evolutionary analyses reveal the coevolution of residues in …
-
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 …
-
Computational studies of origins of life scenarios
… are performed by amino-acyl tRNA synthetases (AARSs), and are essential for enforcing the genetic code. While studies involving the PR and code optimality apply to a more error-prone epoch of early biology, possibly forming ``statistical proteins"" whose sequence is determined probabilistically …
-
Simulation and visualization of dynamics in RNA-protein complexes in translation
… For several Class I aminoacyl-tRNA synthetases (aaRSs), the rate determining step in aminoacylation is the dissociation of the charged tRNA from the enzyme. Through molecular modeling, internal pKa calculations, and MD simulations, distinct, mechanistically relevant post-transfer states with the …
-
Evaluation of the Protein Recognition Properties of Peptide Nucleic Acids
<p>The objective is to evaluate the ability of aminoacyl-tRNA synthetases (aaRS) to recognize the non-standard nucleic acid, PNA (peptide nucleic acid). PNA has immense potential in biomedical applications due to its increased thermostability and nuclease resistance over natural nucleic acids. PNA …
Page 1 of 2