Arginyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the RARSgene.[5][6]
Aminoacyl-tRNA synthetases catalyze the aminoacylation of 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. Arginyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family.[6]
McCune SA, Yu PL, Nance WE (1977). "A genetic study of erythrocyte arginine-tRNA synthetase activity in man". Acta Geneticae Medicae et Gemellologiae. 26 (1): 21–7. doi:10.1017/S0001566000010151. PMID562050.
Norcum MT (August 1991). "Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents". The Journal of Biological Chemistry. 266 (23): 15398–405. PMID1651330.
Wang HY, Pan F (1985). "Kinetic mechanism of arginyl-tRNA synthetase from human placenta". The International Journal of Biochemistry. 16 (12): 1379–85. doi:10.1016/0020-711X(84)90244-1. PMID6530022.
Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 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.
Quevillon S, Robinson JC, Berthonneau E, Siatecka M, Mirande M (January 1999). "Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein". Journal of Molecular Biology. 285 (1): 183–95. doi:10.1006/jmbi.1998.2316. PMID9878398.
Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. doi:10.1038/nbt810. PMID12665801. S2CID23783563.
Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC1847948. PMID17353931.
Bottoni A, Vignali C, Piccin D, Tagliati F, Luchin A, Zatelli MC, Uberti EC (August 2007). "Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell lines". Journal of Cellular Physiology. 212 (2): 293–7. doi:10.1002/jcp.21083. PMID17443684. S2CID27371659.
External links
Overview of all the structural information available in the PDB for UniProt: P54136 (Human Arginine--tRNA ligase, cytoplasmic) at the PDBe-KB.