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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 R, Shimizu N, Ruddle F (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.
^ ^a ^b "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 M (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 J, 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 S, Kim M, Lee J, 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 K, 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 Y, Rho S, Park S, Kim M 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 Q, Ye M, Wu X, Ren S, Zhao M, Zhao C 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 Y, Zheng Y, Wei H, Wang L, Wu X 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 R, 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.
Lue S, Kelley S (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.

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English Journal

Kinetic partitioning between synthetic and editing pathways in class I aminoacyl-tRNA synthetases occurs at both pre-transfer and post-transfer hydrolytic steps.

Cvetesic N, Perona JJ, Gruic-Sovulj I.SourceDepartment of Chemistry, Faculty of Science, University of Zagreb, Croatia;
The Journal of biological chemistry.J Biol Chem.2012 May 30. [Epub ahead of print]
Comprehensive steady-state and transient kinetic studies of the synthetic and editing activities of Escherichia coli leucyl-tRNA synthetase (LeuRS) demonstrate that the enzyme depends almost entirely on post-transfer editing to endow the cell with specificity against incorporation of norvaline into
PMID 22648413

Expanding the Genetic Code of Caenorhabditis elegans Using Bacterial Aminoacyl-tRNA Synthetase/tRNA Pairs.

Parrish AR, She X, Xiang Z, Coin I, Shen Z, Briggs SP, Dillin A, Wang L.SourceJack H. Skirball Center for Chemical Biology and Proteomics and ‡Howard Hughes Medical Institute, Glenn Center for Aging Research, The Salk Institute for Biological Studies , 10010 N. Torrey Pines Road, La Jolla, California 92037, United States.
ACS chemical biology.ACS Chem Biol.2012 May 11. [Epub ahead of print]
The genetic code specifies 20 common amino acids and is largely preserved in both single and multicellular organisms. Unnatural amino acids (Uaas) have been genetically incorporated into proteins by using engineered orthogonal tRNA/aminoacyl-tRNA synthetase (RS) pairs, enabling new research capabili
PMID 22554080

Japanese Journal

3P-093 Leucyl-tRNA合成酵素における酵素機能発現の計算科学的解析(核酸結合蛋白質,第47回日本生物物理学会年会)

Hagiwara Yohsuke,Nureki Osamu,Tateno Masaru
生物物理 49(SUPPLEMENT_1), S166-S167, 2009-09-20
NAID 110008101947

Identification of the nucleophilic factors and the productive complex for the editing reaction by leucyl-tRNA synthetase

Hagiwara Yohsuke,Nureki Osamu,Tateno Masaru,舘野賢
FEBS letters 583(12), 1901-1908, 2009-06
… To ensure fidelity of translation, several aminoacyl-tRNA synthetases (aaRSs) possess editing capability to hydrolyse mis-aminoacylated tRNAs. … In this report, based on our previously-modelled structure of leucyl-tRNA synthetase (LeuRS) complexed with valyl-tRNALeu, further structural modelling has been performed along with molecular dynamics simulations. …
NAID 120001468404

「ロイシルtRNA合成酵素」

Leucyl-tRNA synthetase
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	2WFD
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
Gene ontology
Molecular function	• aminoacyl-tRNA editing activity; • leucine-tRNA ligase activity; • protein binding; • ATP binding;
Cellular component	• nucleus; • cytoplasm; • cytosol;
Biological process	• tRNA aminoacylation for protein translation; • leucyl-tRNA aminoacylation; • regulation of translational fidelity; • gene expression;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	This box: view; talk; edit;

　　[★]

英: leucyl-tRNA synthetase
関: ロイシルtRNAシンテターゼ

「ロイシルtRNAシンテターゼ」

　　[★]

英: leucyl-tRNA synthetase
関: ロイシルtRNA合成酵素

「isoleucyl-tRNA synthetase」

　　[★]

イソロイシルtRNA合成酵素、イソロイシルtRNAシンテターゼ

関: isoleucine-tRNA ligase

「synthetase」

　　[★]

n.

(ATPやNADを必要とする2分子連結酵素リガーゼの別名)シンテターゼ、シンセターゼ、連結酵素、合成酵素

関: ligase、synthase

「tRNA」

　　[★] トランスファーRNA, transfer RNA, 転位RNA

「tRNAs」

　　[★] トランスファーRNA transfer RNAs

[pmid6933703-1] Giles R, Shimizu N, Ruddle F (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.

[entrez-2] "Entrez Gene: LARS leucyl-tRNA synthetase".

[pmid11829477-3] 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.

リンク元	「ロイシルtRNA合成酵素」「ロイシルtRNAシンテターゼ」
拡張検索	「isoleucyl-tRNA synthetase」
関連記事	「synthetase」「tRNA」「tRNAs」

匿名

検索

案内

案内

leucyl-tRNA synthetase