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2002 | 49 | 1 | 1-10
Article title

Aminoacyl-tRNA synthetases and aminoacylation of tRNA in the nucleus.

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Abstracts
EN
This review is focused on findings concerning the presence of translation apparatus components (aminoacyl-tRNA synthetases, aminoacyl-tRNA, elongation factors) as well as translation itself in the nucleus. A nuclear role of these molecules is unknown. New findings suggest that well-accepted model of spatial segregation of transcription and translation in eukaryotic cell may be oversimplifcation. Nuclear coupling of both these processes show us how exciting and surprising may be the world of the living cell.
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Year
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49
Issue
1
Pages
1-10
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Dates
published
2002
received
2001-10-17
revised
2002-02-14
accepted
2002-02-27
Contributors
author
  • University of Gdańsk, Department of Chemistry, Gdańsk, Poland
References
  • 1. Lee, N., Bessho, Y., Wei, K., Szostak, J.W. & Suga, H. (2000) Ribozyme-catalyzed tRNA aminoacylation. Nat. Struct. Biol. 7, 28-33.
  • 2. Kisselev, L.L. & Wolfson, A.D. (1994) Aminoacyl-tRNA synthetases from higher eukaryotes. Prog. Nucleic Acid Res. Mol. Biol. 48, 83-142.
  • 3. Krzyzaniak, A., Salanski, P., Twardowski, T., Jurczak, J. & Barciszewski, J. (1998) tRNA aminoacylated at high pressure is a correct substrate for protein biosynthesis Biochem. Mol. Biol. Int. 45, 489-500.
  • 4. Beuning, P.J. & Musier-Forsyth, K. (1999) Transfer RNA recognition by aminoacyl-tRNA synthetases. Biopolymers 52, 1-28.
  • 5. Martinis, S.A., Plateau, P., Cavarelli, J. & Florentz, C. (1999) Aminoacyl-tRNA synthetases: A new image for a classical family. Biochimie 81, 683-700.
  • 6. Lund, E. & Dahlberg, J.E. (1998) Proofreading and aminoacylation of tRNAs before export from the nucleus. Science 282, 2082-2085.
  • 7. Nathanson, L. & Deutscher, M.P. (2000) Active aminoacyl-tRNA synthetases are present in nuclei as a high molecular weight multienzyme complex. J. Biol. Chem. 275, 31559-31562.
  • 8. Grosshans, H., Hurt, E. & Simos, G. (2000) An aminoacylation-dependent nuclear tRNA export pathway in yeast. Genes Dev. 14, 830-840.
  • 9. Ibba, M. & Soll, D. (2000) Aminoacyl-tRNA synthesis. Annu. Rev. Biochem. 69, 617-650.
  • 10. Bandyopadhyay, A.K. & Deutscher, M.P. (1971) Complex of aminoacyl-transfer RNA synthetases. J. Mol. Biol. 60, 113-122.
  • 11. Yang, D.C. (1996) Mammalian aminoacyl- tRNA synthetases. Curr. Top. Cell. Regul. 34, 101-136.
  • 12. Simos, G. & Hurt, E. (1999) Transfer RNA biogenesis: A visa to leave the nucleus. Curr. Biol. 9, R238-R241.
  • 13. Robinson, J.C., Kerjan, P. & Mirande, M. (2000) Macromolecular assemblage of aminoacyl-tRNA synthetases: Quantitative analysis of protein -protein interactions and mechanism of complex assembly. J. Mol. Biol. 304, 983-994.
  • 14. Norcum, M.T. & Warrington, J.A. (1998) Structural analysis of the multienzyme aminoacyl-tRNA synthetase complex: A three- domain model based on reversible chemical crosslinking. Protein Sci. 7, 79-87.
  • 15. Deinert, K., Fasiolo, F., Hurt, E.C. & Simos, G. (2001) Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes its interaction with the cognate tRNAs. J. Biol. Chem. 276, 6000-6008.
  • 16. Mirande, M. (1991) Aminoacyl-tRNA synthetase family from prokaryotes and eukaryotes: Structural domains and their implications. Progr. Nucleic Acid Res. Mol. Biol. 40, 95-142.
  • 17. Norcum, M.T. (1999) Ultrastructure of the eukaryotic aminoacyl-tRNA synthetase complex derived from two dimensional averaging and classification of negatively stained electron microscopic images. FEBS Lett. 447, 217-222.
  • 18. Norcum, M.T. (1989) Isolation and electron microscopic characterization of the high molecular mass aminoacyl-tRNA synthetase complex from murine erythroleukemia cells. J. Biol. Chem. 264, 15043-15051.
  • 19. Norcum, M.T. & Dignam, J.D. (1999) Immunoelectron microscopic localization of glutamyl-prolyl-tRNA synthetase within the eukaryotic multisynthetase complex. J. Biol. Chem. 274, 12205-12208.
  • 20. Cerini, C., Kerjan, P., Astier, M., Gratecos, D., Mirande, M. & Semeriva, M. (1991) A component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase. EMBO J. 10, 4267-4277.
  • 21. Kaiser, E., Hu, B., Becher, S., Eberhard, D., Schray, B., Baack, M., Hameister, H. & Knippers, R. (1994) The human EPRS locus (formerly the QARS locus): A gene encoding a class I and a class II aminoacyl-tRNA synthetase. Genomics 19, 280-290.
  • 22. Schimmel, P. & Wang, C.C. (1999) Getting tRNA synthetases into the nucleus. Trends Biochem. Sci. 24, 127-128.
  • 23. Ibba, M., Curnow, A.W. & Soll, D. (1997) Aminoacyl-tRNA synthesis: Divergent routes to a common goal. Trends Biochem. Sci. 22, 39-42.
  • 24. Negrutskii, B.S., Stapulionis, R. & Deutscher, M.P. (1994) Supramolecular organization of the mammalian translation system. Proc. Natl. Acad. Sci. U.S.A. 91, 964-968.
  • 25. Sivaram, P. & Deutscher, M.P. (1990) 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. 87, 3665-3669.
  • 26. Amar-Costesec, A. & Turu, C. (1989) Subcellular topology of rat liver methionyl-, leucyl-, and arginyl-tRNA synthetases. Biol. Cell 65, 21-28.
  • 27. Hampel, A. & Enger, M.D. (1973) Subcellular distribution of aminoacyl-transfer RNA synthetases in Chinese hamster ovary cell culture. J. Mol. Biol. 79, 285-293.
  • 28. Mirande, M., Le Corre, D. & Waller, J.P. (1985) A complex from cultured Chinese hamster ovary cells containing nine aminoacyl-tRNA synthetases. Thermolabile leucyl- tRNA synthetase from the tsH1 mutant cell line is an integral component of this complex. Eur. J. Biochem. 147, 281-289.
  • 29. Popenko, V.I., Ivanova, J.L., Cherny, N.E., Filonenko, V.V., Beresten, S.F., Wolfson, A.D. & Kisselev, L.L. (1994) Compartmentalization of certain components of the protein synthesis apparatus in mammalian cells. Eur. J. Cell. Biol. 65, 60-69.
  • 30. Barbarese, E., Koppel, D.E., Deutscher, M.P., Smith, C.L., Ainger, K., Morgan, F. & Carson, J.H. (1995) Protein translation components are colocalized in granules in oligodendrocytes. J. Cell Sci. 108, 2781-2790.
  • 31. Sanders, J., Brandsma, M., Janssen, G.M., Dijk, J. & Moller, W. (1996) Immunofluorescence studies of human fibroblasts demonstrate the presence of the complex of elongation factor-1 beta gamma delta in the endoplasmic reticulum. J. Cell Sci.109, 1113-1117.
  • 32. Gamblin, S.J. & Smerdon, S.J. (1999) Nuclear transport: What a kary-on! Structure Fold. Des. 7, R199-R204.
  • 33. Cullen, B.R. (2000) Nuclear RNA export pathways. Mol. Cell. Biol. 20, 4181-4187.
  • 34. Grosshans, H., Simos, G. & Hurt, E. (2000) Review: Transport of tRNA out of the nucleus - direct channeling to the ribosome? J. Struct. Biol. 129, 288-294.
  • 35. Adam, S.A. (1999) Transport pathways of macromolecules between the nucleus and the cytoplasm. Curr. Opin. Cell Biol. 11, 402-406.
  • 36. Nigg, E.A. (1997) Nucleoplasmatic transport: Signals, mechanisms and regulation. Nature 386, 779-786.
  • 37. Strom, A.C. & Weis, K. (2001) Importin-beta-like nuclear transport receptors. Genome Biol. 2, 1-9.
  • 38. Weis, K. (1998) Importins and exportins: How to get in and out of the nucleus. Trends Biochem. Sci. 23, 185-189.
  • 39. Kutay, U., Hartmann, E., Treichel, N., Calado, A., Carmo-Fonseca, M., Prehn, S., Kraft, R., Gorlich, D. & Bischoff, F.R. (2000) Identification of two novel RanGTP-binding proteins belonging to the importin beta superfamily. J. Biol. Chem. 275, 40163-40168.
  • 40. Corbett, A.H. & Silver, P.A. (1997) Nucleocytoplasmic transport of macromolecules. Microbiol. Mol. Biol. Rev. 61, 193-211.
  • 41. Kalderon, D., Roberts, B.L., Richardson, W.D. & Smith, A.E. (1984) A short amino acid sequence able to specify nuclear location. Cell 39, 499-509.
  • 42. Makkerh, J.P., Dingwall, C. & Laskey, R.A. (1996) Comparative mutagenesis of nuclear localization signals reveals the importance of neutral and acidic amino acids. Curr. Biol. 6, 1025-1027.
  • 43. Krzyzaniak, A., Siatecka, M., Szyk, A., Mucha, P., Rekowski, P., Kupryszewski, G. & Barciszewski, J. (2000) Specific induction of Z-DNA conformation by a nuclear localization signal peptide of lupin glutaminyl tRNA synthetase. Mol. Biol. Rep. 27, 51-54.
  • 44. Schade, M., Behlke, J., Lowenhaupt, K., Herbert, A., Rich, A. & Oschkinat, H. (1999) A 6 bp Z-DNA hairpin binds two Z alpha domains from the human RNA editing enzyme ADAR1. FEBS Lett. 458, 27-31.
  • 45. Herbert, A. & Rich, A. (1996) The biology of left-handed Z-DNA. J. Biol. Chem. 271, 11595-11598.
  • 46. Peck, L.J. & Wang, J.C. (1985) Transcriptional block caused by a negative supercoiling induced structural change in an alternating CG sequence. Cell 40, 129-137.
  • 47. Kim, Y.G., Lowenhaupt, K., Maas, S., Herbert, A., Schwartz, T. & Rich, A. (2000) The zab domain of the human RNA editing enzyme ADAR1 recognizes Z-DNA when surrounded by B-DNA. J. Biol. Chem. 275, 26828-26833.
  • 48. Dou, X., Limmer, S. & Kreutzer, R. (2001) DNA-binding of phenylalanyl-tRNA synthetase is accompanied by loop formation of the double-stranded DNA. J. Mol. Biol. 305, 451-458.
  • 49. Lechler, A. & Kreutzer, R. (1998) The phenylalanyl-tRNA synthetase specifically binds DNA. J. Mol. Biol. 278, 897-901.
  • 50. Deutscher, M.P. & Ni, R.C. (1982) Purification of a low molecular weight form of rat liver arginyl-tRNA synthetase. J. Biol. Chem. 257, 6003-6006.
  • 51. Vellekamp, G., Sihag, R.K. & Deutscher, M.P. (1985) Comparison of the complexed and free forms of rat liver arginyltRNA synthetase and origin of the free form. J. Biol. Chem. 260, 9843-9847.
  • 52. Sarkar, S., Azad, A.K. & Hopper, A.K. (1999) Nuclear tRNA aminoacylation and its role in nuclear export of endogenous tRNAs in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 96, 14366-14371.
  • 53. Wolin, S.L. & Matera, A.G. (1999) The trials and travels of tRNA. Genes Dev. 13, 1-10.
  • 54. Hopper, A.K., Schultz, L.D. & Shapiro, R.A. (1980) Processing of intervening sequences: A new yeast mutant which fails to excise intervening sequences from precursor tRNAs. Cell 19, 741-751.
  • 55. Hellmuth, K., Lau, D.M., Bischoff, F.R., Kunzler, M., Hurt, E. & Simos, G. (1998) Yeast Los1p has properties of an exportin-like nucleocytoplasmic transport factor for tRNA. Mol. Cell. Biol. 18, 6374-6386.
  • 56. Gorlich, D., Dabrowski, M., Bischoff, F.R., Kutay, U., Bork, P., Hartmann, E., Prehn, S. & Izaurralde, E. (1997) A novel class of RanGTP binding proteins. J. Cell Biol. 138, 65-80.
  • 57. Kutay, U., Lipowsky, G., Izaurralde, E., Bischoff, F.R., Schwarzmaier, P., Hartmann, E. & Gorlich, D. (1998) Identification of a tRNA-specific nuclear export receptor. Mol. Cell 1, 359-369.
  • 58. Arts, G.J., Fornerod, M. & Mattaj, I.W. (1998) Identification of a nuclear export receptor for tRNA. Curr. Biol. 8, 305-314.
  • 59. Dahlberg, J.E. & Lund, E. (1998) Functions of the GTPase Ran in RNA export from the nucleus. Curr. Opin. Cell. Biol. 10, 400-408.
  • 60. Izaurralde, E. & Adam, S. (1998) Transport of macromolecules between the nucleus and the cytoplasm. RNA 4, 351-364.
  • 61. Sarkar, S. & Hopper, A.K. (1998) tRNA nuclear export in Saccharomyces cerevisiae: In situ hybridization analysis. Mol. Biol. Cell 9, 3041-3055.
  • 62. Hurt, D.J., Wang, S.S., Lin, Y.H. & Hopper, A.K. (1987) Cloning and characterization of Los1, a Saccharomyces cerevisiae gene that affects tRNA splicing. Mol. Cell. Biol. 7, 1208-1216.
  • 63. Arts, G.J., Kuersten, S., Romby, P., Ehresmann, B. & Mattaj, I.W. (1998) The role of exportin-t in selective nuclear export of mature tRNAs. EMBO J. 17, 7430-7441.
  • 64. Lipowsky, G., Bischoff, F.R., Izaurralde, E., Kutay, U., Schafer, S., Gross, H.J., Beier, H. & Gorlich, D. (1999) Coordination of tRNA nuclear export with processing of tRNA. RNA 5, 539-549.
  • 65. Simos, G., Sauer, A., Fasiolo, F. & Hurt, E.C. (1998) A conserved domain within Arc1p delivers tRNA to aminoacyltRNA synthetases. Mol. Cell. 1, 235-242.
  • 66. Iborra, F.J., Jackson, D.A. & Cook, P.R. (2001) Coupled transcription and translation within nuclei and mammalian cells. Science. 293, 1139-1142.
  • 67. Dreher, T.W., Uhlenbeck, O.C. & Browning, K.S. (1999) Quantitative assessment of EF-1alpha. GTP binding to aminoacyl-tRNAs, aminoacyl-viral RNA, and tRNA shows close correspondence to the RNA binding properties of EF-Tu. J. Biol. Chem.274, 666-672.
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Publication order reference
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YADDA identifier
bwmeta1.element.bwnjournal-article-abpv49i1p1kz
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