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Showing 1 to 20 of 31 for “"aminoacyl-tRNA synthetases"”.
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The Hydroxamate Reaction of Aminoacyl-tRNA Synthetases
<p>Amino acids are activated as aminoacyladenylates which remain bound to the aminoacyl-tRNA synthetases that catalyze their formation. The activated amino acids are then esterified to specific transfer RNA molecules. By this reaction sequence, the specificity and energetics necessary for …
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Interactions Between Aminoacyl-Trna Synthetases and Transfer-Rnas From Escherichia Coli
Made available in DSpace on 2014-12-09T18:53:06Z (GMT). No. of bitstreams: 1 6901483.pdf: 1925547 bytes, checksum: 1341f16b04a547adb4610578659ace00 (MD5) Previous issue date: 1968
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Regulated alternative splicing separates canonical and cell signaling functions of aminoacyl-tRNA synthetases
Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2024-05-01
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Localization of tRNAs and aminoacyl-tRNA synthetases in cytoplasm, chloroplast and mitochondria of Glycine max, L.
Dept. of Biological Sciences. Paper copy at Leddy Library: Theses & Major Papers - Basement, West Bldg. / Call Number: Thesis1980 .S553. Source: Masters Abstracts International, Volume: 40-07, page: . Thesis (M.Sc.)--University of Windsor (Canada), 1981.
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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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Evolution of Protein Structure
The aminoacyl-tRNA synthetases are one of the major protein components in the translation machinery. These essential proteins are found in all forms of life, and are responsible for charging their cognate tRNAs with the correct amino acid. The evolution of the tRNA synthetases is of fundamental …
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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 …
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Kinetic and mutational studies of two RNA-interacting enzymes
… which disrupt RNA secondary structure, and aminoacyl-tRNA synthetases, which catalyze the attachment of an amino acid to its cognate tRNA.
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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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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
… all cases. 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 …
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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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The Invariant Arginine In Motif 2 of ESCHERICHIA COLI Alanyl-tRNA Synthetase : Is Important For Catalysis But Not For Substrate Binding
… 2 and 3, located in the active site of class II aminoacyl-tRNA synthetases, each contain an invariant arginine thought to participate in interactions with ATP. For <em>Escherichia coli</em> alanyl-tRNA synthetase (AlaRS), sequence comparisons indicate that Arg69 should be aligned with the …
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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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PTEN-5-HT2CR Complex: An Ideal Target for Developing Treatment to Restore the Functioning of 5-HT2CR; An Attempt to Minimize the Development of Antimicrobial Resistance
… cause common health problems and infections. Aminoacyl-tRNA synthetases (AsRSs) which use a unique two-step mechanism of aminoacylation reaction are ideal targets for antibacterials. AN2690, a benzoxaborole derivative, shows great antibiotic activity by trapping tRNALeu in the editing domain. …
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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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Creating CRISPR-Cas9 genome edited iPSC lines to model a patient-specific mutation in mitochondrial disease
Mitochondrial aminoacyl tRNA-synthetases (mt-aaRS) catalyse the charging of tRNAs with their cognate amino acids in mitochondria. Mutations in mt-aaRS cause tissue-specific mitochondrial diseases, especially affecting tissues with high energy expenditure like the nervous system, heart, and kidneys. …
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Chemical Reporters for Bacterial Pathogenesis and Beyond
… when used in combination with mutant aminoacyl-tRNA-synthetases. This technology allows the visualization of bacterial protein synthesis during infection as well as the enrichment, identification and proteomic analysis of bacterial proteins from infected host cells. Additionally, I …
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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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