HARS

From Wikipedia, the free encyclopedia

Histidyl-tRNA synthetase

PDB rendering based on 1x59.

Available structures: 1x59

Identifiers

Symbol(s)

HARS; FLJ20491; HRS

External IDs

OMIM: 142810 MGI: 108087 HomoloGene: 1592

Gene ontology
Molecular Function:	• nucleotide binding • histidine-tRNA ligase activity • ATP binding • ligase activity
Cellular Component:	• cytoplasm
Biological Process:	• histidyl-tRNA aminoacylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002109 (mRNA)
NP_002100 (protein)

NM_008214 (mRNA)
NP_032240 (protein)

Location

Chr 5: 140.03 - 140.05 Mb

Chr 18: 36.89 - 36.91 Mb

Pubmed search

[1]

[2]

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

Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl-tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.^[1]

[edit] References

^ ^a ^b Entrez Gene: HARS histidyl-tRNA synthetase.

[edit] Further reading

Raben N, Borriello F, Amin J, et al. (1992). "Human histidyl-tRNA synthetase: recognition of amino acid signature regions in class 2a aminoacyl-tRNA synthetases.". Nucleic Acids Res. 20 (5): 1075–81. PMID 1549469.
Shi MH, Tsui FW, Rubin LA (1991). "Cellular localization of the target structures recognized by the anti-Jo-1 antibody: immunofluorescence studies on cultured human myoblasts.". J. Rheumatol. 18 (2): 252–8. PMID 2023220.
Carlock LR, Skarecky D, Dana SL, Wasmuth JJ (1985). "Deletion mapping of human chromosome 5 using chromosome-specific DNA probes.". Am. J. Hum. Genet. 37 (5): 839–52. PMID 2996334.
Wasmuth JJ, Carlock LR (1986). "Chromosomal localization of human gene for histidyl-tRNA synthetase: clustering of genes encoding aminoacyl-tRNA synthetases on human chromosome 5.". Somat. Cell Mol. Genet. 12 (5): 513–7. PMID 3464104.
Tsui FW, Siminovitch L (1987). "Isolation, structure and expression of mammalian genes for histidyl-tRNA synthetase.". Nucleic Acids Res. 15 (8): 3349–67. PMID 3554142.
O'Hanlon TP, Raben N, Miller FW (1995). "A novel gene oriented in a head-to-head configuration with the human histidyl-tRNA synthetase (HRS) gene encodes an mRNA that predicts a polypeptide homologous to HRS.". Biochem. Biophys. Res. Commun. 210 (2): 556–66. PMID 7755634.
Ogata K, Kurahashi A, Nishiyama C, Terao K (1994). "Presence of role of the 5SrRNA-L5 protein complex (5SRNP) in the threonyl- and histidyl-tRNA synthetase complex in rat liver cytosol.". Biochim. Biophys. Acta 1218 (3): 388–400. PMID 8049265.
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.
Tsui HW, Mok S, de Souza L, et al. (1993). "Transcriptional analyses of the gene region that encodes human histidyl-tRNA synthetase: identification of a novel bidirectional regulatory element.". Gene 131 (2): 201–8. PMID 8406012.
Vázquez-Abad D, Carson JH, Rothfield N (1997). "Localization of histidyl-tRNA synthetase (Jo-1) in human laryngeal epithelial carcinoma cell line (HEp-2 cells).". Cell Tissue Res. 286 (3): 487–91. PMID 8929351.
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.
Sang Lee J, Gyu Park S, Park H, et al. (2002). "Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex.". Biochem. Biophys. Res. Commun. 291 (1): 158–64. doi:10.1006/bbrc.2002.6398. PMID 11829477.
O'Hanlon TP, Miller FW (2002). "Genomic organization, transcriptional mapping, and evolutionary implications of the human bi-directional histidyl-tRNA synthetase locus (HARS/HARSL).". Biochem. Biophys. Res. Commun. 294 (3): 609–14. doi:10.1016/S0006-291X(02)00525-9. PMID 12056811.
Ascherman DP, Oriss TB, Oddis CV, Wright TM (2003). "Critical requirement for professional APCs in eliciting T cell responses to novel fragments of histidyl-tRNA synthetase (Jo-1) in Jo-1 antibody-positive polymyositis.". J. Immunol. 169 (12): 7127–34. PMID 12471150.
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.
Lu Q, Hope LW, Brasch M, et al. (2003). "TSG101 interaction with HRS mediates endosomal trafficking and receptor down-regulation.". Proc. Natl. Acad. Sci. U.S.A. 100 (13): 7626–31. doi:10.1073/pnas.0932599100. PMID 12802020.
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.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Levine SM, Raben N, Xie D, et al. (2007). "Novel conformation of histidyl-transfer RNA synthetase in the lung: the target tissue in Jo-1 autoantibody-associated myositis.". Arthritis Rheum. 56 (8): 2729–39. doi:10.1002/art.22790. PMID 17665459.