Glutaminyl-tRNA synthetase is an enzyme that in humans is encoded by the QARS gene.[5][6][7]

QARS1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesQARS1, GLNRS, MSCCA, PRO2195, glutaminyl-tRNA synthetase, glutaminyl-tRNA synthetase 1, QARS
External IDsOMIM: 603727; MGI: 1915851; HomoloGene: 3704; GeneCards: QARS1; OMA:QARS1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001272073
NM_005051

NM_001168270
NM_133794

RefSeq (protein)

NP_001259002
NP_005042

NP_598555

Location (UCSC)Chr 3: 49.1 – 49.11 MbChr 9: 108.38 – 108.39 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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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.[7] 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.[8]

Interactions

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QARS has been shown to interact with RARS.[9]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000172053Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032604Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Lamour V, Quevillon S, Diriong S, N'Guyen VC, Lipinski M, Mirande M (Aug 1994). "Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer". Proceedings of the National Academy of Sciences of the United States of America. 91 (18): 8670–4. Bibcode:1994PNAS...91.8670L. doi:10.1073/pnas.91.18.8670. PMC 44668. PMID 8078941.
  6. ^ Durkin ME, Jäger AC, Khurana TS, Nielsen FC, Albrechtsen R, Wewer UM (July 1999). "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)". Cytogenetics and Cell Genetics. 84 (3–4): 173–8. doi:10.1159/000015249. PMID 10393422. S2CID 36315977.
  7. ^ a b "Entrez Gene: QARS glutaminyl-tRNA synthetase".
  8. ^ Hadd A, Perona JJ (Oct 2014). "Coevolution of specificity determinants in eukaryotic glutamyl- and glutaminyl-tRNA synthetases". Journal of Molecular Biology. 426 (21): 3619–33. doi:10.1016/j.jmb.2014.08.006. PMID 25149203.
  9. ^ Kim T, Park SG, Kim JE, Seol W, Ko YG, Kim S (Jul 2000). "Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex". The Journal of Biological Chemistry. 275 (28): 21768–72. doi:10.1074/jbc.M002404200. PMID 10801842.

Further reading

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