Arginyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the RARSgene.[1][2]
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.[2]
↑Wolf, N. I.; Salomons, G. S.; Rodenburg, R. J.; Pouwels, P. J.; Schieving, J. H.; Derks, T. G.; Fock, J. M.; Rump, P; Van Beek, D. M.; Van Der Knaap, M. S.; Waisfisz, Q (2014). "Mutations in RARS cause hypomyelination". Annals of Neurology. 76 (1): 134–9. doi:10.1002/ana.24167. PMID24777941.
↑Kim, T; Park S G; Kim J E; Seol W; Ko Y G; Kim S (July 2000). "Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex". J. Biol. Chem. UNITED STATES. 275 (28): 21768–72. doi:10.1074/jbc.M002404200. ISSN0021-9258. PMID10801842.
Further reading
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. PMID562050.
Norcum MT (1991). "Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents". J. Biol. Chem. 266 (23): 15398–405. PMID1651330.
Wang HY, Pan F (1985). "Kinetic mechanism of arginyl-tRNA synthetase from human placenta". Int. J. Biochem. 16 (12): 1379–85. doi:10.1016/0020-711X(84)90244-1. PMID6530022.
Maruyama K, Sugano S (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.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID8889548.
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.
Rho SB, Lee JS, Jeong EJ, et al. (1998). "A multifunctional repeated motif is present in human bifunctional tRNA synthetase". J. Biol. Chem. 273 (18): 11267–73. doi:10.1074/jbc.273.18.11267. PMID9556618.
Quevillon S, Robinson JC, Berthonneau E, et al. (1999). "Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein". J. Mol. Biol. 285 (1): 183–95. doi:10.1006/jmbi.1998.2316. PMID9878398.
Park SG, Jung KH, Lee JS, et al. (1999). "Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase". J. Biol. Chem. 274 (24): 16673–6. doi:10.1074/jbc.274.24.16673. PMID10358004.
Kim T, Park SG, Kim JE, et al. (2000). "Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex". J. Biol. Chem. 275 (28): 21768–72. doi:10.1074/jbc.M002404200. PMID10801842.
Kang J, Kim T, Ko YG, et al. (2000). "Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases". J. Biol. Chem. 275 (41): 31682–8. doi:10.1074/jbc.M909965199. PMID10913161.
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.
Ling C, Yao YN, Zheng YG, et al. (2005). "The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex". J. Biol. Chem. 280 (41): 34755–63. doi:10.1074/jbc.M413511200. PMID16055448.
Bottoni A, Vignali C, Piccin D, et al. (2007). "Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell lines". J. Cell. Physiol. 212 (2): 293–7. doi:10.1002/jcp.21083. PMID17443684.