arginine trna ligase

Summary

Summary: An enzyme that activates arginine with its specific transfer RNA. EC 6.1.1.19.

Top Publications

  1. Vinella D, D Ari R, Jaffe A, Bouloc P. Penicillin binding protein 2 is dispensable in Escherichia coli when ppGpp synthesis is induced. EMBO J. 1992;11:1493-501 pubmed
    ..We conclude that ppGpp regulates the transcription of a gene whose product is involved in mecillinam sensitivity, possibly as part of a chain of interacting elements which coordinate ribosomal activity with that of the PBPs. ..
  2. Delagoutte B, Keith G, Moras D, Cavarelli J. Crystallization and preliminary X-ray crystallographic analysis of yeast arginyl-tRNA synthetase-yeast tRNAArg complexes. Acta Crystallogr D Biol Crystallogr. 2000;56:492-4 pubmed
    ..The estimated V(m) of 2.6 A(3) Da(-1) indicates one molecule of complex in the asymmetric unit. The three crystal forms were solved by the molecular-replacement method using the coordinates of the free yArgRS. ..
  3. Igloi G, Schiefermayr E. Amino acid discrimination by arginyl-tRNA synthetases as revealed by an examination of natural specificity variants. FEBS J. 2009;276:1307-18 pubmed publisher
  4. Sekine S, Shimada A, Nureki O, Cavarelli J, Moras D, Vassylyev D, et al. Crucial role of the high-loop lysine for the catalytic activity of arginyl-tRNA synthetase. J Biol Chem. 2001;276:3723-6 pubmed
    ..The results suggest a plausible partition of the ArgRSs into two major groups, on the basis of the conservation of the HIGH lysine. ..
  5. Geslain R, Martin F, Delagoutte B, Cavarelli J, Gangloff J, Eriani G. In vivo selection of lethal mutations reveals two functional domains in arginyl-tRNA synthetase. RNA. 2000;6:434-48 pubmed
    ..Furthermore, by using different tRNA(Arg) isoacceptors and heterologous tRNA(Asp), we highlighted the crucial role of several residues of the carboxy-terminal domain in tRNA recognition and discrimination. ..
  6. Jovanovic M, Lilic M, Janjusevic R, Jovanovic G, Savic D, Milija J. tRNA synthetase mutants of Escherichia coli K-12 are resistant to the gyrase inhibitor novobiocin. J Bacteriol. 1999;181:2979-83 pubmed
    ..Under conditions of stringent response induction, either by the presence of tRNA synthetase mutations or by constitutive production of RelA protein, inactivation of the cls gene diminishes resistance to novobiocin but not to mecillinam. ..
  7. Sivaram P, Deutscher M. Existence of two forms of rat liver arginyl-tRNA synthetase suggests channeling of aminoacyl-tRNA for protein synthesis. Proc Natl Acad Sci U S A. 1990;87:3665-9 pubmed
    ..Other evidence supporting channeling in protein synthesis is discussed. ..
  8. Zhang Q, Wang E, Wang Y. The role of tryptophan residues in Escherichia coli arginyl-tRNA synthetase. Biochim Biophys Acta. 1998;1387:136-42 pubmed
    ..The thermodynamic calculation indicates that this mutation causes a decrease of the binding energy by 2.7 kJ/mol. Our data suggest that Trp162 is involved in the binding of arginine and in the transition state stabilization. ..
  9. Kiga D, Sakamoto K, Sato S, Hirao I, Yokoyama S. Shifted positioning of the anticodon nucleotide residues of amber suppressor tRNA species by Escherichia coli arginyl-tRNA synthetase. Eur J Biochem. 2001;268:6207-13 pubmed
    ..The isolated mutant has mutations at two nonsurface amino-acid residues that interact with each other near the anticodon-binding site. ..

More Information

Publications62

  1. 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. ..
  2. 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. ..
  3. 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. ..
  4. 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. ..
  5. 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. ..
  6. 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. ..
  7. Konno M, Sumida T, Uchikawa E, Mori Y, Yanagisawa T, Sekine S, et al. Modeling of tRNA-assisted mechanism of Arg activation based on a structure of Arg-tRNA synthetase, tRNA, and an ATP analog (ANP). FEBS J. 2009;276:4763-79 pubmed publisher
  8. 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. ..
  9. 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. ..
  10. 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. ..
  11. 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. ..
  12. 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. ..
  13. 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. ..
  14. 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. ..
  15. 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. ..
  16. 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. ..
  17. 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. ..
  18. 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. ..
  19. 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. ..
  20. 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. ..
  21. 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. ..
  22. 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. ..
  23. Teichmann S, Mitchison G. Is there a phylogenetic signal in prokaryote proteins?. J Mol Evol. 1999;49:98-107 pubmed
  24. 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. ..
  25. 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...
  26. 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. ..
  27. 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. ..
  28. 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. ..
  29. 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. ..
  30. Nafisinia M, Sobreira N, Riley L, Gold W, Uhlenberg B, WeiƟ 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. ..
  31. 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. ..
  32. 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. ..
  33. 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
  34. 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. ..
  35. Sharp P, Mitchell K. Corynebacterium glutamicum arginyl-tRNA synthetase. Mol Microbiol. 1993;8:200 pubmed
  36. 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. ..
  37. 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. ..
  38. 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). ..
  39. 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. ..
  40. 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. ..
  41. 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. ..
  42. 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. ..
  43. 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
  44. 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
  45. 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. ..
  46. 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. ..
  47. 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. ..
  48. 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. ..
  49. 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. ..
  50. 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. ..
  51. 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. ..
  52. 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. ..
  53. 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. ..