Genomic organization of the rat aspartyl-tRNA synthetase gene family: A single active gene and several retropseudogenes

Gene

Volumn 180, Issue 1-2, 1996, Pages 197-205

  Lazard, Myriam ^a,c   Agou, Fabrice ^a   Cavarelli, Jean ^a   Latreille, Marie Thérèse ^a   Moras, Dino ^b   Mirande, Marc ^a  

^a LABORATOIRE D ENZYMOLOGIE ET BIOCHIMIE STRUCTURALES   (France)

^b INSTITUT DE GÉNÉTIQUE ET DE BIOLOGIE MOLÉCULAIRE ET CELLULAIRE   (France)

^c LABORATOIRE DE BIOCHIMIE   (France)

Author keywords

Aminoacyl trna synthetase complex; Gene structure; Line; Mammals; Pseudogene; Retrotransposition

Indexed keywords

ASPARTATE TRANSFER RNA LIGASE; COMPLEMENTARY DNA;

ANIMAL TISSUE; ARTICLE; DNA LIBRARY; EVOLUTION; EXON; GENE ISOLATION; GENE STRUCTURE; INTRON; MULTIGENE FAMILY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PSEUDOGENE; RAT; SEQUENCE HOMOLOGY; STOP CODON;

AMINO ACID SEQUENCE; ANIMALS; ASPARTATE-TRNA LIGASE; BASE SEQUENCE; BLOTTING, SOUTHERN; DNA, COMPLEMENTARY; EXONS; INTRONS; MOLECULAR SEQUENCE DATA; MULTIGENE FAMILY; PROTEIN CONFORMATION; PSEUDOGENES; RATS;

ANIMALIA; MAMMALIA;

EID: 0030597355     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(96)00455-6     Document Type: Article

References (40)

1. Ambrosio, E., Waitzkin, S.D., Witney, F.R., Salemme, A. and Furano, A.V. (1986) Structure of the highly repeated, long interspersed DNA family (LINE or L1Rn) of the rat. Mol. Cell. Biol. 6, 411-424.
2. Bec, G., Kerjan, P. and Waller, J.-P. (1994) Reconstitution in vitro of the valyl-tRNA synthetase-elongation factor 1βγδ complex. J. Biol. Chem. 269, 2086-2092.
3. Belrhali, H., Yaremchuk, A., Tukalo, M., Larsen, K., Bertbet-Colominas, C., Leberman, R., Beijer, B., Sproat, B., Als-Nielsen, J., Grübel, G., Legrand, J.-F., Lehmann, M. and Cusack, S. (1994) Crystal structure at 2.5 Å resolution of seryl-tRNA synthetase complexed with two analogs of seryl-adenylate. Science 263, 1432-1436.
4. Benton, W.D. and Davis, R.W. (1977) Screening λgt recombinant clones by hybridization to single plaques in situ. Science 196, 180-182.
5. Burbaum, J.J. and Schimmel, P. (1991) Structural relationships and the classification of aminoacyl-tRNA synthetases. J. Biol. Chem. 266, 16965-16968.
6. Asp recognition by its cognate class II aminoacyl-tRNA synthetase. Nature 362, 181-184.
7. Cavarelli, J., Eriani, G., Rees, B., Ruff, M., Boeglin, M., Mitschler, A., Martin, F., Gangloff, J., Thierry, J.-C. and Moras, D. (1994) The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction. EMBO J. 13, 327-337.
8. Cusack, S., Härtlein, M. and Leberman, R. (1991) Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases. Nucleic Acids Res. 19, 3489-3498.
9. Delarue, M. and Moras, D. (1993) The aminoacyl-tRNA synthetase family: modules at work. Bioessays 15, 675-687.
10. Delarue, M., Poterszman, A., Nikonov, S., Garber, M., Moras, D. and Thierry, J.C. (1994) Crystal structure of a prokaryotic aspartyl-tRNA synthetase. EMBO J. 13, 3219-3229.
11. Dynan, W.S. (1986) Promoters for housekeeping genes. Trends Genet. 2, 196-197.
12. Eriani, G., Delarue, M., Poch, O., Gangloff, J. and Moras, D. (1990) Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature, 347, 203-206.
13. Frolova, L.Y., Grigorieva, A.Y., Sudomoina, M.A. and Kisselev, L.L. (1993) The human gene encoding tryptophanyl-tRNA synthetase: interferon-response elements and exon-intron organization. Gene 128, 237-245.
14. Hsieh, S.L. and Campbell, R.D. (1991) Evidence that gene G7a in the human major histocompatibility complex encodes valyl-tRNA synthetase. Biochem. J. 278, 809-816.
15. Jacobo-Molina, A., Peterson, R. and Yang, D.C.H. (1989) cDNA sequence, predicted primary structure, and evolving amphiphilic helix of human aspartyl-tRNA synthetase. J. Biol. Chem. 264, 16608-16612
16. Kaiser, E., Hu, B., Becher, S., Eberhard, D., Schray, B., Baack, M., Hameister, H. and Knippers, R. (1994) The human EPRS locus (formerly the QARS locus): a gene encoding a class I and class II aminoacyl-tRNA synthetase. Genomics 19, 280-290.
17. Kontis, K.J. and Arfin, S.M. (1989) Isolation of a cDNA clone for human threonyl-tRNA synthetase: amplification of the structural gene in borrelidin-resistant cell lines. Mol. Cell. Biol. 9, 1832-1838.
18. Lazard, M. and Mirande, M. (1993) Cloning and analysis of a cDNA encoding mammalian arginyl-tRNA synthetase, a component of the multisynthetase complex with a hydrophobic N-terminal extension. Gene 132, 237-245.
19. Li, W.-H., Gojobori, T. and Nei, M. (1981) Pseudogenes as a paradigm of neutral evolution. Nature 292, 237-239.
20. Mathias, S.L., Scott, A.F., Kazazian, H.H. Jr., Boeke, J.D. and Gabriel, A. (1991) Reverse transcriptase encoded by a human transposable element. Science 254, 1808-1810.
21. Mirande, M. and Waller, J.-P. (1989) Molecular cloning and primary structure of cDNA encoding the catalytic domain of rat liver aspartyl-tRNA synthetase. J. Biol. Chem. 264, 842-847.
22. Mirande, M. (1991) Aminoacyl-tRNA synthetase family from prokaryotes and eukaryotes: structural domains and their implications. Prog. Nucleic Acid Res. Mol. Biol. 40, 95-142.
23. Mirande, M., LeCorre, D. and Waller, J.-P. (1985) A complex from cultured chinese hamster ovary cells containing nine aminoacyl-tRNA synthetases. Eur. J. Biochem. 147, 281-289.
24. Mirande, M., Lazard, M., Martinez, R. and Latreille, M.-T. (1992) Engineering mammalian aspartyl-tRNA synthetase to probe structural features mediating its association with the multisynthetase complex. Eur. J. Biochem. 203, 459-466.
25. Nagel, G.M. and Doolittle, R.F. (1995) Phylogenetic analysis of the aminoacyl-tRNA synthetases. J. Mol. Evol. 40, 487-498.
26. Pascale, E., Liu, C., Valle, E., Usdin, K. and Furano, A.V. (1993) The evolution of long interspersed DNA (L1, LINE) as revealed by the analysis of an ancient rodent L1 DNA family. J. Mol. Evol. 36, 9-20.
27. Poterszman, A., Delarue, M., Thierry, J.-C. and Moras, D. (1994) Synthesis and recognition of aspartyl-adenylate by Thermus thermophilus aspartyl-tRNA synthetase. J. Mol. Biol. 244, 158-167.
28. Asp. Science 252, 1682-1689.
29. Sambrook, J., Fritsch, E.F. and Maniatis, T. (1989) Molecular Cloning. A Laboratory Manual, 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
30. Sanger, F., Nicklen, S. and Coulson, A.R. (1977) DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74, 5463-5467.
31. Schimmel, P. and Söll, D. (1979) Aminoacyl-tRNA synthetases: general features and recognition of transfer RNAs. Annu. Rev. Biochem. 48, 601-648.
32. Schimmel, P., Giegé, R., Moras, D. and Yokoyama, S. (1993) An operational RNA code for amino acids and possible relationship to genetic code. Proc. Natl. Acad. Sci. USA 90, 8763-8768.
33. Sivaram, P. and Deutscher, M. (1990) Existence of two forms of rat liver arginyl-tRNA synthetase suggests channeling of aminoacyl-tRNA for protein synthesis. Proc. Natl. Acad. Sci. USA 87, 3665-3669.
34. Stoltzfus, A., Spencer, D.F., Zuker, M., Logsdon, J.M. and Doolittle, W.F. (1994) Testing the exon theory of genes: the evidence from protein structure. Science 265, 202-207.
35. Tamkun, J.W., Schwarzbauer, J.E. and Hynes, R.O. (1984) A single rat fibronectin gene generates three different mRNAs by alternative splicing of a complex exon. Proc. Natl. Acad. Sci. USA 81, 5140-5144.
36. Tchenio, T., Segal-Bendirdjian, E. and Heidmann, T. (1993) Generation of processed pseudogenes in murine cells. EMBO J. 12, 1487-1497.
37. Tsui, F.W.L. and Siminovitch, L. (1987) Isolation, structure and expression of mammalian genes for histidyl-tRNA synthetase. Nucleic Acids Res. 15, 3349-3367.
38. Vanin, E.F. (1985) Processed pseudogenes: characteristics and evolution. Annu. Rev. Genet. 19, 253-272.
39. Vellekamp, G.J., Coyle, C.L. and Kull, F.J. (1983) Low molecular weight aspartyl-tRNA synthetase from porcine thyroid. J. Biol. Chem. 258, 8195-8200.
40. Vellekamp, G.J., Sihag, R.K. and Deutscher, M.P. (1985) Comparison of the complexed and free forms of rat liver arginyl-tRNA synthetase and origin of the free form. J. Biol. Chem. 260, 9843-9847.