RARS (gene)

From Wikipedia, the free encyclopedia


Arginyl-tRNA synthetase
Identifiers
Symbol(s) RARS; ArgRS; DALRD1; MGC8641
External IDs OMIM: 107820 MGI1914297 HomoloGene68281
Orthologs
Human Mouse
Entrez 5917 104458
Ensembl ENSG00000113643 ENSMUSG00000018848
Uniprot P54136 Q3THP2
Refseq NM_002887 (mRNA)
NP_002878 (protein)
NM_025936 (mRNA)
NP_080212 (protein)
Location Chr 5: 167.85 - 167.88 Mb Chr 11: 35.65 - 35.68 Mb
Pubmed search [1] [2]

Arginyl-tRNA synthetase, also known as RARS, is a human gene.[1]

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.[1]

[edit] References

[edit] 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. PMID 562050. 
  • 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. PMID 1651330. 
  • Wang HY, Pan F (1985). "Kinetic mechanism of arginyl-tRNA synthetase from human placenta.". Int. J. Biochem. 16 (12): 1379–85. PMID 6530022. 
  • Girjes AA, Hobson K, Chen P, Lavin MF (1995). "Cloning and characterization of cDNA encoding a human arginyl-tRNA synthetase.". Gene 164 (2): 347–50. PMID 7590355. 
  • 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. PMID 8125298. 
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548. 
  • 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. PMID 9373149. 
  • 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. PMID 9556618. 
  • 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. PMID 9878398. 
  • 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. PMID 10358004. 
  • 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. PMID 10801842. 
  • 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. PMID 10913161. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • 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. PMID 12665801. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334. 
  • 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. PMID 16055448. 
  • Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMID 16344560. 
  • Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931. 
  • 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. PMID 17443684.