Leucyl-tRNA synthetase

Leucyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the LARS gene.

LARS1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2WFD
Identifiers
Aliases	LARS1, Leucyl-tRNA synthetase, ILFS1, HSPC192, LARS, leucyl-tRNA synthetase 1, LRS, LEUS, LFIS, PIG44, hr025Cl, LEURS, RNTLS
External IDs	OMIM: 151350; MGI: 1913808; HomoloGene: 7083; GeneCards: LARS1; OMA:LARS1 - orthologs
Gene location (Human) Chr. Chromosome 5 (human) Band 5q32 Start 146,110,566 bp End 146,182,696 bp
Gene location (Mouse) Chr. Chromosome 18 (mouse) Band 18|18 B3 Start 42,335,363 bp End 42,395,259 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Brodmann area 23 endothelial cell ventricular zone middle temporal gyrus body of pancreas right uterine tube ganglionic eminence primary visual cortex cartilage tissue islet of Langerhans Top expressed in medullary collecting duct basilar part of occipital bone lacrimal gland yolk sac primitive streak renal corpuscle calvaria seminal vesicula ureter salivary gland More reference expression data BioGPS More reference expression data
Gene ontology Molecular function aminoacyl-tRNA ligase activity nucleotide binding leucine-tRNA ligase activity ligase activity protein binding ATP binding aminoacyl-tRNA editing activity valine-tRNA ligase activity GTPase activator activity glutamine-tRNA ligase activity Cellular component cytosol nuclear body cytoplasm lysosome endoplasmic reticulum endomembrane system aminoacyl-tRNA synthetase multienzyme complex Biological process tRNA aminoacylation for protein translation protein biosynthesis leucyl-tRNA aminoacylation valyl-tRNA aminoacylation protein targeting to lysosome regulation of cell size negative regulation of autophagy cellular response to amino acid starvation positive regulation of GTPase activity cellular response to amino acid stimulus cellular response to leucine positive regulation of TORC1 signaling cellular response to leucine starvation glutaminyl-tRNA aminoacylation aminoacyl-tRNA metabolism involved in translational fidelity Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 51520 107045 Ensembl ENSG00000133706 ENSMUSG00000024493 UniProt Q9P2J5 Q8BMJ2 RefSeq (mRNA) NM_020117 NM_001317964 NM_001317965 NM_016460 NM_134137 RefSeq (protein) NP_001304893 NP_001304894 NP_057544 NP_064502 NP_598898 Location (UCSC) Chr 5: 146.11 – 146.18 Mb Chr 18: 42.34 – 42.4 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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 arginyl-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.

Interactions

Leucyl-tRNA synthetase has been shown to interact with EEF1G.

Inhibitors

• BC-LI-0186
• Tavaborole

See also

• Leucine-tRNA ligase

Further reading

• Norcum MT (August 1991). "Structural analysis of the high molecular mass aminoacyl-tRNA synthetase complex. Effects of neutral salts and detergents". The Journal of Biological Chemistry. 266 (23): 15398–15405. doi:10.1016/S0021-9258(18)98629-1. PMID 1651330.
• Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Quevillon S, Robinson JC, Berthonneau E, Siatecka M, Mirande M (January 1999). "Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core protein". Journal of Molecular Biology. 285 (1): 183–195. doi:10.1006/jmbi.1998.2316. PMID 9878398.
• Rho SB, Kim MJ, Lee JS, Seol W, Motegi H, Kim S, Shiba K (April 1999). "Genetic dissection of protein-protein interactions in multi-tRNA synthetase complex". Proceedings of the National Academy of Sciences of the United States of America. 96 (8): 4488–4493. Bibcode:1999PNAS...96.4488R. doi:10.1073/pnas.96.8.4488. PMC 16359. PMID 10200289.
• Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O (February 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 Research. 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. (October 2000). "Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases". The Journal of Biological Chemistry. 275 (41): 31682–31688. doi:10.1074/jbc.M909965199. PMID 10913161.
• Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, et al. (October 2000). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Research. 10 (10): 1546–1560. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
• Sang Lee J, Gyu Park S, Park H, Seol W, Lee S, Kim S (February 2002). "Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex". Biochemical and Biophysical Research Communications. 291 (1): 158–164. doi:10.1006/bbrc.2002.6398. PMID 11829477.
• Ling C, Yao YN, Zheng YG, Wei H, Wang L, Wu XF, Wang ED (October 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". The Journal of Biological Chemistry. 280 (41): 34755–34763. doi:10.1074/jbc.M413511200. PMID 16055448.
• Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, et al. (January 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 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". Molecular Systems Biology. 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. (May 2007). "A novel mutation in the mitochondrial DNA tRNA Leu (UUR) gene associated with late-onset ocular myopathy". Neuromuscular Disorders. 17 (5): 415–418. doi:10.1016/j.nmd.2007.01.015. PMID 17363246. S2CID 26750219.
• Lue SW, Kelley SO (April 2007). "A single residue in leucyl-tRNA synthetase affecting amino acid specificity and tRNA aminoacylation". Biochemistry. 46 (15): 4466–4472. doi:10.1021/bi0618215. PMC 2518062. PMID 17378584.