YARS

From Wikipedia, the free encyclopedia

Tyrosyl-tRNA synthetase

PDB rendering based on 1n3l.

Available structures: 1n3l, 1ntg, 1q11

Identifiers

Symbol(s)

YARS; CMTDIC; TYRRS; YRS; YTS

External IDs

OMIM: 603623 MGI: 2147627 HomoloGene: 2730

Gene ontology
Molecular Function:	• tRNA binding • nucleotide binding • tyrosine-tRNA ligase activity • signal transducer activity • interleukin-8 receptor binding • ATP binding • ligase activity
Cellular Component:	• extracellular space • soluble fraction • cytoplasm
Biological Process:	• tyrosyl-tRNA aminoacylation • apoptosis • cell motility

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003680 (mRNA)
NP_003671 (protein)

XM_622904 (mRNA)
XP_622904 (protein)

Location

Chr 1: 33.01 - 33.06 Mb

Chr 4: 128.69 - 128.72 Mb

Pubmed search

[1]

[2]

Tyrosyl-tRNA synthetase, also known as YARS, is a human gene.^[1]

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. 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.^[1]

[edit] References

^ ^a ^b Entrez Gene: YARS tyrosyl-tRNA synthetase.

[edit] Further reading

Ewalt KL, Schimmel P (2002). "Activation of angiogenic signaling pathways by two human tRNA synthetases.". Biochemistry 41 (45): 13344-9. PMID 12416978.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171-4. PMID 8125298.
Ribas de Pouplana L, Frugier M, Quinn CL, Schimmel P (1996). "Evidence that two present-day components needed for the genetic code appeared after nucleated cells separated from eubacteria.". Proc. Natl. Acad. Sci. U.S.A. 93 (1): 166-70. PMID 8552597.
Kleeman TA, Wei D, Simpson KL, First EA (1997). "Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine.". J. Biol. Chem. 272 (22): 14420-5. PMID 9162081.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149-56. PMID 9373149.
Wakasugi K, Quinn CL, Tao N, Schimmel P (1998). "Genetic code in evolution: switching species-specific aminoacylation with a peptide transplant.". EMBO J. 17 (1): 297-305. doi:10.1093/emboj/17.1.297. PMID 9427763.
Wakasugi K, Schimmel P (1999). "Two distinct cytokines released from a human aminoacyl-tRNA synthetase.". Science 284 (5411): 147-51. PMID 10102815.
Wakasugi K, Schimmel P (1999). "Highly differentiated motifs responsible for two cytokine activities of a split human tRNA synthetase.". J. Biol. Chem. 274 (33): 23155-9. PMID 10438485.
Austin J, First EA (2002). "Catalysis of tyrosyl-adenylate formation by the human tyrosyl-tRNA synthetase.". J. Biol. Chem. 277 (17): 14812-20. doi:10.1074/jbc.M103396200. PMID 11856731.
Austin J, First EA (2002). "Potassium functionally replaces the second lysine of the KMSKS signature sequence in human tyrosyl-tRNA synthetase.". J. Biol. Chem. 277 (23): 20243-8. doi:10.1074/jbc.M201923200. PMID 11927599.
Wakasugi K, Slike BM, Hood J, et al. (2002). "Induction of angiogenesis by a fragment of human tyrosyl-tRNA synthetase.". J. Biol. Chem. 277 (23): 20124-6. doi:10.1074/jbc.C200126200. PMID 11956181.
Austin J, First EA (2002). "Comparison of the catalytic roles played by the KMSKS motif in the human and Bacillus stearothermophilus trosyl-tRNA synthetases.". J. Biol. Chem. 277 (32): 28394-9. doi:10.1074/jbc.M204404200. PMID 12016229.
Yang XL, Skene RJ, McRee DE, Schimmel P (2003). "Crystal structure of a human aminoacyl-tRNA synthetase cytokine.". Proc. Natl. Acad. Sci. U.S.A. 99 (24): 15369-74. doi:10.1073/pnas.242611799. PMID 12427973.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Jia J, Li B, Jin Y, Wang D (2003). "Expression, purification, and characterization of human tyrosyl-tRNA synthetase.". Protein Expr. Purif. 27 (1): 104-8. PMID 12509991.
Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566-9. doi:10.1038/nbt810. PMID 12665801.
Jordanova A, Thomas FP, Guergueltcheva V, et al. (2004). "Dominant intermediate Charcot-Marie-Tooth type C maps to chromosome 1p34-p35.". Am. J. Hum. Genet. 73 (6): 1423-30. PMID 14606043.
Yang XL, Otero FJ, Skene RJ, et al. (2004). "Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains.". Proc. Natl. Acad. Sci. U.S.A. 100 (26): 15376-80. doi:10.1073/pnas.2136794100. PMID 14671330.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039.