Tyrosine–tRNA ligase, cytoplasmic, also called
Tyrosyl-tRNA synthetase 1, is an enzyme that in humans is encoded by the YARS1gene (previously YARS).[5][6][7] Like the mitochondrial variety, YARS2, this enzyme functions as a Tyrosine–tRNA ligase,[8] meaning it functions to attach the amino acid tyrosine to its corresponding transfer RNA (tRNATyr) as part of RNA-to-protein translation.[9]
Living cells translate DNA sequences into RNA sequences and then into protein sequences. Proteins are chains of amino acids, such as tyrosine. As the protein grows, each amino acid is added to the end with the help of an adapator molecule called transfer RNA (tRNA). Each amino acid has its own tRNA (called tRNATyr in the case of tyrosine), and tyrosyl-tRNA synthetase is an enzyme that attaches tyrosine to tRNATyr, so that it can be then used in this translation process.[9]
Aminoacyl-tRNA synthetases catalyze the aminoacylation of transfer RNA (tRNA) by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Tyrosyl-tRNA synthetase belongs to the class I tRNA synthetase family. Cytokine activities have also been observed for the human tyrosyl-tRNA synthetase, after it is split into two parts, an N-terminal fragment that harbors the catalytic site and a C-terminal fragment found only in the mammalian enzyme. The N-terminal fragment is an interleukin-8-like cytokine, whereas the released C-terminal fragment is an EMAP II-like cytokine.[7][10]
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