Leucyl-tRNA synthetase
Leucyl-tRNA synthetase | |||||||||||||
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Identifiers | |||||||||||||
Symbols | LARS ; HSPC192; LARS1; LEURS; LEUS; LFIS; LRS; PIG44; RNTLS; hr025Cl | ||||||||||||
External IDs | OMIM: 151350 MGI: 1913808 HomoloGene: 7083 ChEMBL: 3258 GeneCards: LARS Gene | ||||||||||||
EC number | 6.1.1.4 | ||||||||||||
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RNA expression pattern | |||||||||||||
More reference expression data | |||||||||||||
Orthologs | |||||||||||||
Species | Human | Mouse | |||||||||||
Entrez | 51520 | 107045 | |||||||||||
Ensembl | ENSG00000133706 | ENSMUSG00000024493 | |||||||||||
UniProt | Q9P2J5 | Q8BMJ2 | |||||||||||
RefSeq (mRNA) | NM_020117 | NM_134137 | |||||||||||
RefSeq (protein) | NP_064502 | NP_598898 | |||||||||||
Location (UCSC) | Chr 5: 145.49 – 145.56 Mb | Chr 18: 42.2 – 42.26 Mb | |||||||||||
PubMed search | |||||||||||||
Leucyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the LARS gene.[1][2]
Function
This gene encodes a cytosolic leucine-tRNA synthetase, a member of the class I aminoacyl-tRNA synthetase family. The encoded enzyme catalyzes the ATP-dependent ligation of L-leucine to tRNA(Leu). It is found in the cytoplasm as part of a multisynthetase complex and interacts with the arginine tRNA synthetase through its C-terminal domain. Alternatively spliced transcript variants of this gene have been found; however, their full-length nature is not known.[2]
Interactions
Leucyl-tRNA synthetase has been shown to interact with EEF1G.[3]
See also
- Leucine-tRNA ligase
References
- ↑ Giles RE, Shimizu N, Ruddle FH (Jan 1981). "Assignment of a human genetic locus to chromosome 5 which corrects the heat sensitive lesion associated with reduced leucyl-tRNA synthetase activity in ts025Cl Chinese hamster cells". Somatic Cell Genet 6 (5): 667–687. doi:10.1007/BF01538645. PMID 6933703.
- ↑ 2.0 2.1 "Entrez Gene: LARS leucyl-tRNA synthetase".
- ↑ Sang Lee J, Gyu Park S, Park H, Seol W, Lee S, Kim S (Feb 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.
Further reading
- Norcum MT (1991). "Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents.". J. Biol. Chem. 266 (23): 15398–405. PMID 1651330.
- 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. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Quevillon S, Robinson JC, Berthonneau E, Siatecka M, Mirande M (1999). "Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein.". J. Mol. Biol. 285 (1): 183–95. doi:10.1006/jmbi.1998.2316. PMID 9878398.
- Rho SB, Kim MJ, Lee JS, Seol W, Motegi H, Kim S et al. (1999). "Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex.". Proc. Natl. Acad. Sci. U.S.A. 96 (8): 4488–93. doi:10.1073/pnas.96.8.4488. PMC 16359. PMID 10200289.
- Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O (2000). "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro.". DNA Res. 7 (1): 65–73. doi:10.1093/dnares/7.1.65. PMID 10718198.
- Kang J, Kim T, Ko YG, Rho SB, Park SG, Kim MJ et al. (2000). "Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases.". J. Biol. Chem. 275 (41): 31682–8. doi:10.1074/jbc.M909965199. PMID 10913161.
- Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ et al. (2001). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells.". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
- Sang Lee J, Gyu Park S, Park H, Seol W, Lee S, Kim S (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.
- Ling C, Yao YN, Zheng YG, Wei H, Wang L, Wu XF et al. (2005). "The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex.". J. Biol. Chem. 280 (41): 34755–63. doi:10.1074/jbc.M413511200. PMID 16055448.
- Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
- Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
- Maeso E, Rueda A, Jiménez S, Del Hoyo P, Martín R, Cabello A et al. (2007). "A novel mutation in the mitochondrial DNA tRNA Leu (UUR) gene associated with late-onset ocular myopathy.". Neuromuscul. Disord. 17 (5): 415–8. doi:10.1016/j.nmd.2007.01.015. PMID 17363246. Vancouver style error (help)
- Lue SW, Kelley SO (2007). "A single residue in leucyl-tRNA synthetase affecting amino acid specificity and tRNA aminoacylation.". Biochemistry 46 (15): 4466–72. doi:10.1021/bi0618215. PMC 2518062. PMID 17378584.