QARS1

QARS1
Identifiers
AliasesQARS1, GLNRS, MSCCA, PRO2195, glutaminyl-tRNA synthetase, glutaminyl-tRNA synthetase 1, QARS
External IDsOMIM: 603727; MGI: 1915851; GeneCards: QARS1
Available structures
PDBOrtholog search: PDBe RCSB
Enzyme activity
EC #BRENDAExPASyKEGGMetaCyc
6.1.1.18
Orthologs
DatabasesNCBI: entry; OMA: entry
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

Glutaminyl-tRNA ligase is an enzyme that in humans is encoded by the QARS1 gene (previously QARS).[5][6][7] More broadly, Glutamate–tRNA ligase (EC 6.1.1.18) can also refer to the type of enzyme activity that the QARS1 protein performs, namely catalyzing the attachment of the amino acid glutamine to transfer RNA using ATP.[8]

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.[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.[9]

Interactions

QARS has been shown to interact with RARS.[10]

References

  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. ^ "P47897 · SYQ_HUMAN". uniprot.org. UniProt consortium. Retrieved 2026-08-11.
  9. ^ 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.
  10. ^ 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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