Genomes and Genes
arginine trna ligase
Summary: An enzyme that activates arginine with its specific transfer RNA. EC 188.8.131.52.
- Liu M, Huang Y, Wu J, Wang E, Wang Y. Effect of cysteine residues on the activity of arginyl-tRNA synthetase from Escherichia coli. Biochemistry. 1999;38:11006-11 pubmed..Our study suggested that inactivation of E. coli ArgRS by sulfhydryl reagents is a result of steric hindrance in the enzyme. ..
- Cavarelli J, Delagoutte B, Eriani G, Gangloff J, Moras D. L-arginine recognition by yeast arginyl-tRNA synthetase. EMBO J. 1998;17:5438-48 pubmed..This tyrosine is also conserved in other class I aaRS active sites but plays several functional roles. The ArgRS structure allows the definition of a new framework for sequence alignments and subclass definition in class I aaRSs. ..
- Zhang Q, Shen L, Wang E, Wang Y. Biosynthesis and characterization of 4-fluorotryptophan-labeled Escherichia coli arginyl-tRNA synthetase. J Protein Chem. 1999;18:187-92 pubmed..Finally, a preliminary study of 19F nuclear magnetic resonance spectroscopy of the fluorinated enzyme has shown promising prospect for further investigation of its structure and function with NMR. ..
- Zhou M, Azzi A, Xia X, Wang E, Lin S. Crystallization and preliminary X-ray diffraction analysis of E. coli arginyl-tRNA synthetase in complex form with a tRNAArg. Amino Acids. 2007;32:479-82 pubmed..Such complex structure also provides a wide opening for inhibitor search using bioinformatics. ..
- Popenko V, Ivanova J, Cherny N, Filonenko V, Beresten S, Wolfson A, et al. Compartmentalization of certain components of the protein synthesis apparatus in mammalian cells. Eur J Cell Biol. 1994;65:60-9 pubmed..At the same time, the detection of some ARS in the diffuse chromatin regions in the nucleus implies that these enzymes may exhibit some non-canonical functions in addition to their role in protein synthesis. ..
- Aggarwal A, Schneider S, Houlden H, Silverdale M, Paudel R, Paisan Ruiz C, et al. Indian-subcontinent NBIA: unusual phenotypes, novel PANK2 mutations, and undetermined genetic forms. Mov Disord. 2010;25:1424-31 pubmed publisher..In conclusion, genetically determined NBIA cases from the Indian subcontinent suggest presence of unusual phenotypes of PANK2 and novel mutations. The phenotype of NBIA of unknown cause includes a PD-like presentation. ..
- Sivaram P, Vellekamp G, Deutscher M. A role for lipids in the functional and structural properties of the rat liver aminoacyl-tRNA synthetase complex. J Biol Chem. 1988;263:18891-6 pubmed..The significance of these findings for the intracellular location of aminoacyl-tRNA synthetases and for the study of purified complexes are discussed. ..
- Norcum M, Boisset N. Three-dimensional architecture of the eukaryotic multisynthetase complex determined from negatively stained and cryoelectron micrographs. FEBS Lett. 2002;512:298-302 pubmed..The structures have openings or indentations on most sides. Maximum dimensions are ca. 19x16x10 nm. The central cavity is 4 nm in diameter and extends two-thirds of the length of the particle. ..
- Berbec H, Paszkowska A. Comparison of the thermolability and hydrophobic properties of high- and low-molecular-weight forms of rabbit liver arginyl-tRNA synthetase. Mol Cell Biochem. 1989;86:125-33 pubmed..It was found that the complexed arginyl-tRNA synthetase is more stable than the free enzyme. A role of hydrophobic interactions in the maintenance of the complexed enzyme stability is suggested. ..
- Wang H, Pan F. Kinetic mechanism of arginyl-tRNA synthetase from human placenta. Int J Biochem. 1984;16:1379-85 pubmed..The kinetic patterns obtained are consistent with a random Ter Ter sequential mechanism, instead of the common Bi Uni Uni Bi ping-pong mechanism for all other human aminoacyl-tRNA synthetases so far investigated in this respect. ..
- Cheng X, Lin S, Shi J, Wang Y. Arginyl-tRNA synthetase from Escherichia coli affinity labeling with 3'-oxidized tRNA(Arg). Sci China B. 1991;34:297-305 pubmed..During the whole process of labeling and RNase treatment, the two activities of the enzyme were closely associated. ..
- Schulman L, Pelka H. The anticodon contains a major element of the identity of arginine transfer RNAs. Science. 1989;246:1595-7 pubmed..The combined anticodon and dihydrouridine loop mutations yield a tRNA(mMet) derivative that is aminoacylated with near-normal kinetics by the Arg-tRNA synthetase. ..
- Eriani G, Dirheimer G, Gangloff J. Structure-function relationship of arginyl-tRNA synthetase from Escherichia coli: isolation and characterization of the argS mutation MA5002. Nucleic Acids Res. 1990;18:1475-9 pubmed..The position of this mutation and its effect on enzymatic properties suggest the implication of arginine 134 in ATP binding as well as in the activation catalytic process. ..
- Berg B. Autophosphorylation of degradation products of arginyl-tRNA synthetase protein, isolated from Bom:NMRI mouse liver. Biochem Mol Biol Int. 1993;31:229-37 pubmed..9 kDa molecule. In some cases higher molecular weight phosphorylated proteins were also detected. Properties of the 60 kDa species are described. ..
- Sissler M, Eriani G, Martin F, Giege R, Florentz C. Mirror image alternative interaction patterns of the same tRNA with either class I arginyl-tRNA synthetase or class II aspartyl-tRNA synthetase. Nucleic Acids Res. 1997;25:4899-906 pubmed..This study indicates that complex formation between unmodified tRNAAspand either ArgRS and AspRS is solely governed by the proteins. ..
- Lin S, Wang Q, Wang Y. Interactions between Escherichia coli arginyl-tRNA synthetase and its substrates. Biochemistry. 1988;27:6348-53 pubmed..Periodate oxidation did not alter the tRNA binding to the enzyme. The oxidized tRNA still afforded protection against heat inactivation of the enzyme. ..
- Lee S, Cho B, Park S, Kim S. Aminoacyl-tRNA synthetase complexes: beyond translation. J Cell Sci. 2004;117:3725-34 pubmed..They may thus have joined the ARS community to coordinate protein synthesis with other biological processes. ..
- Sissler M, Giege R, Florentz C. The RNA sequence context defines the mechanistic routes by which yeast arginyl-tRNA synthetase charges tRNA. RNA. 1998;4:647-57 pubmed..This confers biological advantages to the arginine aminoacylation system and sheds light on its evolutionary relationship with the aspartate system. ..
- Liao T, Call G, Guptan P, Cespedes A, Marshall J, Yackle K, et al. An efficient genetic screen in Drosophila to identify nuclear-encoded genes with mitochondrial function. Genetics. 2006;174:525-33 pubmed..We have molecularly characterized six complementation groups and, surprisingly, each encodes a mitochondrial protein. Therefore, we believe our screen to be an efficient method for identifying genes with mitochondrial function. ..
- Hogg J, Schiefermayr E, Schiltz E, Igloi G. Expression and properties of arginyl-tRNA synthetase from jack bean (Canavalia ensiformis). Protein Expr Purif. 2008;61:163-7 pubmed publisher..2 kDa compared to the native arginyl-tRNA synthetase. Both full-length fusion and thrombin-treated products proved to be active in aminoacylation, with similar kinetic parameters. ..
- Anderson L, Mao X, Scott B, Crowder C. Survival from hypoxia in C. elegans by inactivation of aminoacyl-tRNA synthetases. Science. 2009;323:630-3 pubmed publisher..Thus, translational suppression produces hypoxia resistance, in part by reducing unfolded protein toxicity. ..
- Teichmann S, Mitchison G. Is there a phylogenetic signal in prokaryote proteins?. J Mol Evol. 1999;49:98-107 pubmed
- Eriani G, Dirheimer G, Gangloff J. Isolation and characterization of the gene coding for Escherichia coli arginyl-tRNA synthetase. Nucleic Acids Res. 1989;17:5725-36 pubmed..coli genes. With the exception of the presence of a HVGH sequence similar to the HIGH consensus element, ArgRS has no relevant sequence homologies with other aminoacyl-tRNA synthetases. ..
- Shimada A, Nureki O, Goto M, Takahashi S, Yokoyama S. Structural and mutational studies of the recognition of the arginine tRNA-specific major identity element, A20, by arginyl-tRNA synthetase. Proc Natl Acad Sci U S A. 2001;98:13537-42 pubmed publisher..Other mutants of Asn(79) also exhibited broader specificity for the nucleotide at position 20 of tRNA(Arg). We propose a model of A20 recognition by the ArgRS that is consistent with the present results of the mutational analyses...
- Airas R. Analysis of the kinetic mechanism of arginyl-tRNA synthetase. Biochim Biophys Acta. 2006;1764:307-19 pubmed..When all free tRNA(Arg) had been used from the reaction mixture, the aminoacylation reaction stopped, but the ATP-PP(i) exchange continued at a lowered rate. ..
- Bence A, Crooks P. The mechanism of L-canavanine cytotoxicity: arginyl tRNA synthetase as a novel target for anticancer drug discovery. J Enzyme Inhib Med Chem. 2003;18:383-94 pubmed..This novel mechanism of cytotoxicity forms the basis for the anticancer activity of L-canavanine and thus, arginyl tRNA synthetase may represent a novel target for the development of such therapeutic agents. ..
- Yao Y, Zhang Q, Yan X, Zhu G, Wang E. Escherichia coli tRNA(4)(Arg)(UCU) induces a constrained conformation of the crucial Omega-loop of arginyl-tRNA synthetase. Biochem Biophys Res Commun. 2004;313:129-34 pubmed..Our 19F NMR and catalytic assay results suggest that the tRNA(Arg)-induced conformational changes of Omega-loop little contribute to the productive conformation of ArgRS catalytic core. ..
- Yao Y, Zhang Q, Yan X, Zhu G, Wang E. Substrate-induced conformational changes in Escherichia coli arginyl-tRNA synthetase observed by 19F NMR spectroscopy. FEBS Lett. 2003;547:197-200 pubmed..The local conformational changes of E. coli ArgRS induced by its substrates observed herein by 19F NMR are similar to those of crystalline yeast homologous enzyme. ..
- Nafisinia M, Sobreira N, Riley L, Gold W, Uhlenberg B, Weiß C, et al. Mutations in RARS cause a hypomyelination disorder akin to Pelizaeus-Merzbacher disease. Eur J Hum Genet. 2017;25:1134-1141 pubmed publisher..001) compared to control cells, suggestive of inefficiency of protein synthesis in the patient cells. Our functional studies provide further evidence that RARS is a PMD-causing gene. ..
- Sivaram P, Deutscher M. Free fatty acids associated with the high molecular weight aminoacyl-tRNA synthetase complex influence its structure and function. J Biol Chem. 1990;265:5774-9 pubmed..These results indicate that the free fatty acids co-purifying with the synthetase complex bind to the synthetases and affect their structure and function. ..
- Airas R. Differences in the magnesium dependences of the class I and class II aminoacyl-tRNA synthetases from Escherichia coli. Eur J Biochem. 1996;240:223-31 pubmed..The binding of ATP to the E. aminoacyl-tRNA complex also speeds up the dissociation of the aminoacyl-tRNA from most of these enzymes. ..
- Guigou L, Mirande M. Determinants in tRNA for activation of arginyl-tRNA synthetase: evidence that tRNA flexibility is required for the induced-fit mechanism. Biochemistry. 2005;44:16540-8 pubmed
- Bottoni A, Vignali C, Piccin D, Tagliati F, Luchin A, Zatelli M, et al. Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell lines. J Cell Physiol. 2007;212:293-7 pubmed..These data indicate that RARS over-expression associates with a reduced AIMP1 secretion and that the multicatalytic protease is involved in the generation of the mature cytokine, EMAP II. ..
- Sharp P, Mitchell K. Corynebacterium glutamicum arginyl-tRNA synthetase. Mol Microbiol. 1993;8:200 pubmed
- Ribeiro S, Golding G. The mosaic nature of the eukaryotic nucleus. Mol Biol Evol. 1998;15:779-88 pubmed..A chimeric origin of eukaryotes or an ancient, massive horizontal transfer of genes from Gram-negative bacteria to eucarya can explain many of the observed phylogenies. ..
- Edvardson S, Shaag A, Kolesnikova O, Gomori J, Tarassov I, Einbinder T, et al. Deleterious mutation in the mitochondrial arginyl-transfer RNA synthetase gene is associated with pontocerebellar hypoplasia. Am J Hum Genet. 2007;81:857-62 pubmed..We speculate that missplicing mutations in mitochondrial aminoacyl-tRNA synthethase genes preferentially affect the brain because of a tissue-specific vulnerability of the splicing machinery. ..
- Shimada A, Nureki O, Dohmae N, Takio K, Yokoyama S. Gene cloning, expression, crystallization and preliminary X-ray analysis of Thermus thermophilus arginyl-tRNA synthetase. Acta Crystallogr D Biol Crystallogr. 2001;57:272-5 pubmed..The flash-frozen crystals diffracted beyond 2.3 A resolution using synchrotron radiation from the beamline 41XU at SPring-8 (Harima). ..
- McCune S, Yu P, Nance W. A genetic study of erythrocyte arginine-tRNA synthetase activity in man. Acta Genet Med Gemellol (Roma). 1977;26:21-7 pubmed..Higher enzyme activity was observed in newborn DZ unlike-sexed twins than in like-sexed twins for either zygosity. Possible explanations for this observation are discussed. ..
- Zhou M, Wang E, Campbell R, Wang Y, Lin S. Crystallization and preliminary X-ray diffraction analysis of arginyl-tRNA synthetase from Escherichia coli. Protein Sci. 1997;6:2636-8 pubmed..They have an orthorhombic space group P2(1)2(1)2 with unit cell parameters of a = 251.51 A, b = 53.12 A, and c = 52.35 A. A complete native data set has been collected at 3.1 A resolution for these crystals. ..
- Huang S, Deutscher M. The NH2-terminal extension of rat liver arginyl-tRNA synthetase is responsible for its hydrophobic properties. Biochem Biophys Res Commun. 1991;180:702-8 pubmed..These findings support the proposed model for synthetase association within the multienzyme complex. ..
- Lazard M, Mirande M. Cloning and analysis of a cDNA encoding mammalian arginyl-tRNA synthetase, a component of the multisynthetase complex with a hydrophobic N-terminal extension. Gene. 1993;132:237-45 pubmed..By using the isolated cDNA, a Northern blot analysis showed a single mRNA species. Thus, there is a possibility that the free and complexed forms of ArgRS are encoded by the same gene. ..
- Sakamoto K, Ishimaru S, Kobayashi T, Walker J, Yokoyama S. The Escherichia coli argU10(Ts) phenotype is caused by a reduction in the cellular level of the argU tRNA for the rare codons AGA and AGG. J Bacteriol. 2004;186:5899-905 pubmed
- Perret V, Florentz C, Giege R. Efficient aminoacylation of a yeast tRNA(Asp) transcript with a 5' extension. FEBS Lett. 1990;270:4-8 pubmed
- Girjes A, Hobson K, Chen P, Lavin M. Cloning and characterization of cDNA encoding a human arginyl-tRNA synthetase. Gene. 1995;164:347-50 pubmed..2.2 kb. The results described here demonstrate that ArgRS is highly conserved in mammalian cells and confirm the presence of a hydrophobic N-terminal region in the higher-molecular-weight complexed form of ArgRS. ..
- Barbarese E, Koppel D, Deutscher M, Smith C, Ainger K, Morgan F, et al. Protein translation components are colocalized in granules in oligodendrocytes. J Cell Sci. 1995;108 ( Pt 8):2781-90 pubmed..This spatial organization may increase the efficiency of protein synthesis and may also provide a vehicle for transport and localization of specific mRNAs within the cell. ..
- Freist W, Sternbach H, Cramer F. Arginyl-tRNA synthetase from yeast. Discrimination between 20 amino acids in aminoacylation of tRNA(Arg)-C-C-A and tRNA(Arg)-C-C-A(3'NH2). Eur J Biochem. 1989;186:535-41 pubmed..They can be related to hydrophobic interaction forces and hydrogen bonds that are especially formed by the arginine side chain. A hypothetical 'stopper' model of the amino acid recognition site is discussed. ..
- Ling C, Yao Y, Zheng Y, Wei H, Wang L, Wu X, et al. 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. 2005;280:34755-63 pubmed..Our results also indicate that the two molecules interact with each other only through their appended domains. ..
- Perret V, Garcia A, Grosjean H, Ebel J, Florentz C, Giege R. Relaxation of a transfer RNA specificity by removal of modified nucleotides. Nature. 1990;344:787-9 pubmed..Our results indicate that post-transcriptional modification of tRNAs introduces structural 'anti-determinants', restricting the efficiency with which the tRNAs are charged with inappropriate amino acids. ..
- Lin S, Shi J, Cheng X, Wang Y. Arginyl-tRNA synthetase from Escherichia coli, purification by affinity chromatography, properties, and steady-state kinetics. Biochemistry. 1988;27:6343-8 pubmed..9 mM, and 0.5 mM for arginine, ATP, and PPi, respectively, with a turnover number of 40 s-1. The pH dependence shows that the reaction is favored toward slightly acidic conditions where the aminoacylation is relatively depressed. ..
- Geslain R, Bey G, Cavarelli J, Eriani G. Limited set of amino acid residues in a class Ia aminoacyl-tRNA synthetase is crucial for tRNA binding. Biochemistry. 2003;42:15092-101 pubmed..Mutations in this domain have no effects on tRNA(Arg) aminoacylation, thus confirming that Saccharomyces cerevisiae and other fungi belong to a distinct class of ArgRS. ..
- Nathanson L, Deutscher M. Active aminoacyl-tRNA synthetases are present in nuclei as a high molecular weight multienzyme complex. J Biol Chem. 2000;275:31559-62 pubmed..Moreover, their unexpected structural organization raises important questions about the functional significance of these multienzyme complexes and whether they might play a more direct role in nuclear to cytoplasmic transport of tRNAs. ..
- Shen Y, Zhao H, Wang H, Wang W, Zhang L, Fu R. Ischemic preconditioning inhibits over-expression of arginyl-tRNA synthetase gene Rars in ischemia-injured neurons. J Huazhong Univ Sci Technolog Med Sci. 2016;36:554-557 pubmed publisher..IPC can inhibit the increased Rars activity and down-regulate ArgRS expression of ischemia-insulted neurons. This mechanism may confer ischemic tolerance on neurons. ..