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Transfer RNA supplementation rescues HARS deficiency in a humanized yeast model of Charcot-Marie-Tooth disease.
Nucleic Acids Res
December 2024
Department of Biochemistry, The University of Western Ontario, London, Ontario N6A 5C1, Canada.
Aminoacyl-tRNA synthetases are indispensable enzymes in all cells, ensuring the correct pairing of amino acids to their cognate tRNAs to maintain translation fidelity. Autosomal dominant mutations V133F and Y330C in histidyl-tRNA synthetase (HARS) cause the genetic disorder Charcot-Marie-Tooth type 2W (CMT2W). Treatments are currently restricted to symptom relief, with no therapeutic available that targets the cause of disease.
View Article and Find Full Text PDFCorrection: G:U-Independent RNA Minihelix Aminoacylation by Nanoarchaeum equitans Alanyl-tRNA Synthetase: An Insight into the Evolution of Aminoacyl-tRNA Synthetases.
J Mol Evol
December 2024
Department of Biological Science and Technology, Tokyo University of Science, 6-3-1 Niijuku, Katsushika-Ku, Tokyo, 125-8585, Japan.
Single-Molecule Studies of Cognate and Near-Cognate Elongation in an Eukaryotic Translation System.
bioRxiv
August 2024
Department of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA.
The ribosome plays a central role in translation of the genetic code into amino acid sequences during synthesis of polypeptides. During each cycle of peptide elongation, the ribosome must discriminate between correct and incorrect aminoacyl-tRNAs according to the codon present in its A-site. Ribosomes rely on a complex sequence of proofreading mechanisms to minimize erroneous selection of incorrect aminoacyl-tRNAs that would lead to mistakes in translation.
View Article and Find Full Text PDFThe central role of transfer RNAs in mistranslation.
J Biol Chem
September 2024
Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, Connecticut, USA. Electronic address:
Transfer RNAs (tRNA) are essential small non-coding RNAs that enable the translation of genomic information into proteins in all life forms. The principal function of tRNAs is to bring amino acid building blocks to the ribosomes for protein synthesis. In the ribosome, tRNAs interact with messenger RNA (mRNA) to mediate the incorporation of amino acids into a growing polypeptide chain following the rules of the genetic code.
View Article and Find Full Text PDFThe role of tRNA identity elements in aminoacyl-tRNA editing.
Front Microbiol
July 2024
Department of Molecular Biology and Biophysics, University of Connecticut School of Medicine, Farmington, CT, United States.
The rules of the genetic code are implemented by the unique features that define the amino acid identity of each transfer RNA (tRNA). These features, known as "identity elements," mark tRNAs for recognition by aminoacyl-tRNA synthetases (ARSs), the enzymes responsible for ligating amino acids to tRNAs. While tRNA identity elements enable stringent substrate selectivity of ARSs, these enzymes are prone to errors during amino acid selection, leading to the synthesis of incorrect aminoacyl-tRNAs that jeopardize the fidelity of protein synthesis.
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