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QARS

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{about||the radio enthusiasts of Qatar|Qatar Amateur Radio Society|the village in Azerbaijan|Qars}}

{{Infobox_gene}}

Glutaminyl-tRNA synthetase is an enzyme that in humans is encoded by the QARS gene.{{cite journal | vauthors = Lamour V, Quevillon S, Diriong S, N'Guyen VC, Lipinski M, Mirande M | title = Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 91 | issue = 18 | pages = 8670–4 | date = Aug 1994 | pmid = 8078941 | pmc = 44668 | doi = 10.1073/pnas.91.18.8670 | bibcode = 1994PNAS...91.8670L | doi-access = free }}{{cite journal | vauthors = Durkin ME, Jäger AC, Khurana TS, Nielsen FC, Albrechtsen R, Wewer UM | title = Characterization of the human laminin beta2 chain locus (LAMB2): linkage to a gene containing a nonprocessed, transcribed LAMB2-like pseudogene (LAMB2L) and to the gene encoding glutaminyl tRNA synthetase (QARS) | journal = Cytogenetics and Cell Genetics | volume = 84 | issue = 3–4 | pages = 173–8 | date = July 1999 | pmid = 10393422 | doi = 10.1159/000015249 | s2cid = 36315977 }}{{cite web | title = Entrez Gene: QARS glutaminyl-tRNA synthetase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5859}}

Function

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. In metazoans, 9 aminoacyl-tRNA synthetases specific for glutamine (gln), glutamic acid (glu), and 7 other amino acids are associated within a multienzyme complex. Although present in eukaryotes, glutaminyl-tRNA synthetase (QARS) is absent from many prokaryotes, mitochondria, and chloroplasts, in which Gln-tRNA(Gln) is formed by transamidation of the misacylated Glu-tRNA(Gln). Glutaminyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family. Almost all eukaryotic GlnRS enzymes possess a YqeY domain at the N-terminus, which affects affinity for the tRNA; in some bacterial species, such as Deinococcus radiodurans, YqeY is present as a C-terminal domain with similar function.{{cite journal | vauthors = Hadd A, Perona JJ | title = Coevolution of specificity determinants in eukaryotic glutamyl- and glutaminyl-tRNA synthetases | journal = Journal of Molecular Biology | volume = 426 | issue = 21 | pages = 3619–33 | date = Oct 2014 | pmid = 25149203 | doi = 10.1016/j.jmb.2014.08.006 }}

Interactions

QARS has been shown to interact with RARS.{{cite journal | vauthors = Kim T, Park SG, Kim JE, Seol W, Ko YG, Kim S | title = Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex | journal = The Journal of Biological Chemistry | volume = 275 | issue = 28 | pages = 21768–72 | date = Jul 2000 | pmid = 10801842 | doi = 10.1074/jbc.M002404200 | doi-access = free }}

References

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Further reading

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  • {{cite journal | vauthors = Norcum MT | title = Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents | journal = The Journal of Biological Chemistry | volume = 266 | issue = 23 | pages = 15398–405 | date = Aug 1991 | doi = 10.1016/S0021-9258(18)98629-1 | pmid = 1651330 | doi-access = free }}
  • {{cite journal | vauthors = Maruyama K, Sugano S | title = Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides | journal = Gene | volume = 138 | issue = 1–2 | pages = 171–4 | date = Jan 1994 | pmid = 8125298 | doi = 10.1016/0378-1119(94)90802-8 }}
  • {{cite journal | vauthors = Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S | title = Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library | journal = Gene | volume = 200 | issue = 1–2 | pages = 149–56 | date = Oct 1997 | pmid = 9373149 | doi = 10.1016/S0378-1119(97)00411-3 }}
  • {{cite journal | vauthors = Quevillon S, Robinson JC, Berthonneau E, Siatecka M, Mirande M | title = Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein | journal = Journal of Molecular Biology | volume = 285 | issue = 1 | pages = 183–95 | date = Jan 1999 | pmid = 9878398 | doi = 10.1006/jmbi.1998.2316 }}
  • {{cite journal | vauthors = Ko YG, Kang YS, Kim EK, Park SG, Kim S | title = Nucleolar localization of human methionyl-tRNA synthetase and its role in ribosomal RNA synthesis | journal = The Journal of Cell Biology | volume = 149 | issue = 3 | pages = 567–74 | date = May 2000 | pmid = 10791971 | pmc = 2174846 | doi = 10.1083/jcb.149.3.567 }}
  • {{cite journal | vauthors = Kim T, Park SG, Kim JE, Seol W, Ko YG, Kim S | title = Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex | journal = The Journal of Biological Chemistry | volume = 275 | issue = 28 | pages = 21768–72 | date = Jul 2000 | pmid = 10801842 | doi = 10.1074/jbc.M002404200 | doi-access = free }}
  • {{cite journal | vauthors = Kang J, Kim T, Ko YG, Rho SB, Park SG, Kim MJ, Kwon HJ, Kim S | title = Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases | journal = The Journal of Biological Chemistry | volume = 275 | issue = 41 | pages = 31682–8 | date = Oct 2000 | pmid = 10913161 | doi = 10.1074/jbc.M909965199 | doi-access = free }}
  • {{cite journal | vauthors = Ko YG, Kim EY, Kim T, Park H, Park HS, Choi EJ, Kim S | title = Glutamine-dependent antiapoptotic interaction of human glutaminyl-tRNA synthetase with apoptosis signal-regulating kinase 1 | journal = The Journal of Biological Chemistry | volume = 276 | issue = 8 | pages = 6030–6 | date = Feb 2001 | pmid = 11096076 | doi = 10.1074/jbc.M006189200 | doi-access = free }}
  • {{cite journal | vauthors = Lehner B, Semple JI, Brown SE, Counsell D, Campbell RD, Sanderson CM | title = Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region | journal = Genomics | volume = 83 | issue = 1 | pages = 153–67 | date = Jan 2004 | pmid = 14667819 | doi = 10.1016/S0888-7543(03)00235-0 }}
  • {{cite journal | vauthors = Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM | title = Functional proteomics mapping of a human signaling pathway | journal = Genome Research | volume = 14 | issue = 7 | pages = 1324–32 | date = Jul 2004 | pmid = 15231748 | pmc = 442148 | doi = 10.1101/gr.2334104 }}
  • {{cite journal | vauthors = Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ | title = Immunoaffinity profiling of tyrosine phosphorylation in cancer cells | journal = Nature Biotechnology | volume = 23 | issue = 1 | pages = 94–101 | date = Jan 2005 | pmid = 15592455 | doi = 10.1038/nbt1046 | s2cid = 7200157 }}
  • {{cite journal | vauthors = Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–8 | date = Oct 2005 | pmid = 16189514 | doi = 10.1038/nature04209 | bibcode = 2005Natur.437.1173R | s2cid = 4427026 }}

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