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. Recently, tyrosyl-tRNA synthetase has been demonstrated as the biologically and functionally significant target for resveratrol
For a comparison of cytoplasmic human tyrosyl-tRNA synthetase with its mitochondrial counterpart and with tyrosyl-tRNA synthetases of other biological kingdoms and organisms, see the Wikipedia page on Tyrosine-tRNA ligase and a general review on their structures and functions.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Wakasugi K, Schimmel P (1999). "Highly differentiated motifs responsible for two cytokine activities of a split human tRNA synthetase". J. Biol. Chem. 274 (33): 23155–9. doi:10.1074/jbc.274.33.23155. PMID10438485.
Austin J, First EA (2002). "Potassium functionally replaces the second lysine of the KMSKS signature sequence in human tyrosyl-tRNA synthetase". J. Biol. Chem. 277 (23): 20243–8. doi:10.1074/jbc.M201923200. PMID11927599.
Wakasugi K, Slike BM, Hood J, et al. (2002). "Induction of angiogenesis by a fragment of human tyrosyl-tRNA synthetase". J. Biol. Chem. 277 (23): 20124–6. doi:10.1074/jbc.C200126200. PMID11956181.
Austin J, First EA (2002). "Comparison of the catalytic roles played by the KMSKS motif in the human and Bacillus stearothermophilus trosyl-tRNA synthetases". J. Biol. Chem. 277 (32): 28394–9. doi:10.1074/jbc.M204404200. PMID12016229.
Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID12665801.