Recombinant Human Tyrosine--tRNA ligase, Cytoplasmic domain (YARS1)

1. conclusion is further supported by a positive correlation across brain regions between TyrRS expression and arginine-accelerated KTP production. PMID: 29289698
2. Platelet replenishment by YRS(ACT) is independent of thrombopoietin (TPO), as evidenced by expansion of the megakaryocytes from induced pluripotent stem cell-derived hematopoietic stem cells from a patient deficient in TPO signaling. PMID: 30104364
3. These YARS variants occur in the catalytic domain and the C-terminal domain, respectively. Mutations in YARS have been previously associated with an autosomal dominant form of Charcot-Marie-Tooth (CMT); our findings suggest the disease spectrum associated with YARS dysregulation is broader than peripheral neuropathy. PMID: 27633801
4. Studied the structural effect of three Charcot-Marie-Tooth disease-causing mutations in tyrosyl-tRNA synthetase. The mutations do not induce changes in protein secondary structures, or shared effects on oligomerization state and stability. However, all mutations provide access to a surface masked in the wild-type enzyme, and that access correlates with protein misinteraction. PMID: 28531329
5. Data show that the internal deletion of tyrosyl-tRNA synthetase TyrRSDeltaE2-4 splice variants (SVs) gave an alternative, neomorphic dimer interface 'orthogonal' to that of native TyrRS. PMID: 26773056
6. Expression of CMT-mutant tyrosyl-tRNA synthetase in Drosophila impairs protein translation. PMID: 26138142
7. Computational modeling of molecular dynamics of G41R mutant form of human tyrosyl-tRNA synthetase, assosiated with Charcot-Marie-Tooth neuropathy has been presented. PMID: 27025069
8. the association of rare YARS variant with late-onset autosomal dominant Charcot-Marie-Tooth neuropathy PMID: 24354524
9. This study presents genetic evidence for common mutant-specific interactions between two CMT-associated aminoacyl-tRNA synthetases, lending support for a shared mechanism responsible for the synthetase-induced peripheral neuropathies. PMID: 24807208
10. rhTyrRS promotes migration and aggregation of megakaryocytes to the bone marrow niche PMID: 24907514
11. nuclear-localized TyrRS activates transcription factor E2F1 to upregulate the expression of DNA damage repair genes such as BRCA1 and RAD51. PMID: 25284223
12. A major difference between the first- and second-generation tRNA synthetases (RSs) is that the second-generation RSs have an active site more compatible with tyrosine binding. PMID: 24611875
13. The full length tyrosyl-tRNA synthetase lacks its cytokine activity because of the interactions between N-terminal and the C-terminal modules, which protect the ELR cytokine motif. PMID: 23334919
14. Nuclear import of TyrRS is regulated by tRNA(Tyr). PMID: 22291016
15. Dominant Intermediate Charcot-Marie-Tooth disorder is not due to a catalytic defect in tyrosyl-tRNA synthetase. PMID: 21732632
16. Expression of tyrosyl-tRNA synthetase (YARS) DI-CMTC associated mutations (G41R, E196K,153-156delVKQV)in Drosophila leads to neuronal dysfunction. PMID: 19561293
17. role in catalyzing tyrosyl-adenylate formation PMID: 11856731
18. replacement of second lysine in KMSKS signature sequence by potassium PMID: 11927599
19. role in inducing angiogenesis PMID: 11956181
20. the KMSSS sequence in human tyrosyl-tRNA synthetase stabilizes the transition state for the tyrosine activation reaction by interacting with the pyrophosphate moiety of ATP PMID: 12016229
21. The recently discovered proangiogenic role of a tyrosyl-tRNA synthetase fragment that stimulates immune cells and links translation to a major cell-signaling pathway is discussed in this review. PMID: 12416978
22. The structure of human mini-TyrRS containing both the catalytic & the anticodon recognition domains, is reported to a resolution of 1.18 A. The spatial disposition of the anticodon recognition domain relative to the catalytic domain is unique. PMID: 12427973
23. identification of two heterozygous missense mutations (G41R and E196K) and one de novo deletion (153-156delVKQV) in tyrosyl-tRNA synthetase (YARS) in three unrelated families affected with dominant intermediate Charcot-Marie-Tooth neuropathy PMID: 16429158
24. Mutating a conserved tyrosine (Y341) that tethers a critical ELR motif in TyrRS resulted in subtle opening of the structure, and activation of cytokine functions, proving the possibility of constitutive gain-of-function mutations in tRNA ligases. PMID: 18096501
25. Human tyrosyl-tRNA synthetase, where a catalytic-domain surface helix, next to the active site, was recruited for interleukin-8-like cytokine signaling. PMID: 19477417

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HGNC: 12840

OMIM: 603623

KEGG: hsa:8565

STRING: 9606.ENSP00000362576

UniGene: Hs.213264