YARS

YARS1
Identifiers
AliasesYARS1, CMTDIC, TYRRS, YRS, YTS, tyrosyl-tRNA synthetase, tyrosyl-tRNA synthetase 1, YARS, IMNEPD2
External IDsOMIM: 603623; MGI: 2147627; GeneCards: YARS1
Available structures
PDBOrtholog search: PDBe RCSB
Enzyme activity
EC #BRENDAExPASyKEGGMetaCyc
6.1.1.1↗↗↗↗
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez

8565

107271

Ensembl

ENSG00000134684

ENSMUSG00000028811

UniProt

P54577

Q91WQ3

RefSeq (mRNA)

NM_003680

NM_134151

RefSeq (protein)

NP_003671

NP_598912

Location (UCSC)Chr 1: 32.78 – 32.82 MbChr 4: 129.08 – 129.11 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Tyrosyl-tRNA synthetase, cytoplasmic, also known as tyrosine-tRNA ligase, is an enzyme that in humans is encoded by the YARS gene.[5][6][7]

Function

Living cells translate DNA sequences into RNA sequences and then into protein sequences. Proteins are chains of amino acids, such as tyrosine. As the protein grows, each amino acid is added to the end by an enzyme called transfer RNA (tRNA). Each amino acid has its own tRNA, and tyrosyl-tRNA synthetase is the tRNA that adds tyrosine to the end of a growing protein.

Aminoacyl-tRNA synthetases catalyze the aminoacylation of transfer RNA (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. Tyrosyl-tRNA synthetase belongs to the class I tRNA synthetase family. Cytokine activities have also been observed for the human tyrosyl-tRNA synthetase, after it is split into two parts, an N-terminal fragment that harbors the catalytic site and a C-terminal fragment found only in the mammalian enzyme. The N-terminal fragment is an interleukin-8-like cytokine, whereas the released C-terminal fragment is an EMAP II-like cytokine.[7][8]

Clinical significance

Recently, tyrosyl-tRNA synthetase has been demonstrated as the biologically and functionally significant target for resveratrol.[9]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000134684 – Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028811 – Ensembl, 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. ↑ Ribas de Pouplana L, Frugier M, Quinn CL, Schimmel P (February 1996). "Evidence that two present-day components needed for the genetic code appeared after nucleated cells separated from eubacteria". Proceedings of the National Academy of Sciences of the United States of America. 93 (1): 166–170. Bibcode:1996PNAS...93..166R. doi:10.1073/pnas.93.1.166. PMC 40199. PMID 8552597.
  6. ↑ Kleeman TA, Wei D, Simpson KL, First EA (June 1997). "Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine". The Journal of Biological Chemistry. 272 (22): 14420–14425. doi:10.1074/jbc.272.22.14420. PMID 9162081.
  7. 1 2 "Entrez Gene: YARS tyrosyl-tRNA synthetase".
  8. ↑ Bedouelle H (2013). "Tyrosyl-tRNA Synthetases". Madame Curie Bioscience Database. Austin (TX): Landes Bioscience. NBK6553.
  9. ↑ Sajish M, Schimmel P (March 2015). "A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol". Nature. 519 (7543): 370–373. Bibcode:2015Natur.519..370S. doi:10.1038/nature14028. PMC 4368482. PMID 25533949.

Further reading

  • Overview of all the structural information available in the PDB for UniProt: P54577 (Tyrosine--tRNA ligase, cytoplasmic) at the PDBe-KB.
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