Structural requirements for the formation of 1-methylguanosine in vivo in tRNA(GGG)(Pro) of Salmonella typhimurium

Journal of Molecular Biology

Volumn 266, Issue 2, 1997, Pages 283-296

  Qian, Qiang ^a   Björk, Glenn R ^a  

^a UMEÅ UNIVERSITY   (Sweden)

Author keywords

1 methylguanosine; Proline tRNA synthetase; RNA protein interactions; tRNA modifying enzyme; tRNA(m1G37)methyltransferase

Indexed keywords

GUANOSINE DERIVATIVE; METHYL GROUP; PROLINE TRANSFER RNA; RIBOSOME RNA; RNA BINDING PROTEIN; TRANSFER RNA METHYLTRANSFERASE;

AMINOACYLATION; ANTICODON; ARTICLE; NONHUMAN; PRIORITY JOURNAL; RIBOSOME; RNA STRUCTURE; SALMONELLA TYPHIMURIUM;

SALMONELLA TYPHIMURIUM; TYPHIMURIUM;

EID: 0031581873     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0789     Document Type: Article

References (58)

1. Björk G. R. Transfer RNA modification in different organisms. Chem. Scr. 26B:1986;91-95.
2. Björk G. R. Genetic dissection of synthesis and function of modified nucleosides in bacterial transfer RNA. Prog. Nucl. Acid Res. Mol. Biol. 50:1995a;263-338.
3. Björk G. R. Biosynthesis and function of modified nucleosides in tRNA. In tRNA: Structure, Biosynthesis, and Function. 1995b;ASM Press, Washington, DC.
4. Björk G. R., Wikström P.M, Byström A. S. Prevention of translational frameshifting by the modified nucleoside 1-methylguanosine. Science. 244:1989;986-989.
5. Chan R. K., Botstein D., Watanabe T., Ogata Y. Specialised transduction of tetracycline resistance by phage P22 in Salmonella typhimurium. II. Properties of a high-frequency-transducing lysate. Virology. 50:1972;883-898.
6. Chattapadhyay R., Pelka H., Schulman L.H. Initiation of in vivo protein synthesis with non-methionine amino acids. Biochemistry. 29:1990;4263-4268.
7. Curnow A. W., Kung F. L., Koch K. A., Garcia G. A. tRNA-guanine transglycosylase from Escherichia coli: gross tRNA structural requirements for recognition. Biochemistry. 32:1993;5239-5246.
8. Davis R. W., Botstein D., Roth J. R. A Manual for Genetic Engineering. Advanced Bacterial Genetics. 1980;Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
9. Draper D. E. Protein-RNA recognition. Annu. Rev. Biochem. 64:1995;593-620.
10. Edqvist J., Grosjean H., Stråby K. B. Identity elements for N2-dimethylation of guanosine-26 in yeast tRNAs. Nucl. Acids Res. 20:1992;6575-6581.
11. Edqvist J., Stråby K. B., Grosjean H. Pleiotrophic effects of point mutations in yeast tRNA(Asp) on the base modification pattern. Nucl. Acids Res. 21:1993;413-417.
12. Edqvist J., Blomqvist K., Stråby K. Structural elements in yeast tRNAs required for homologous modification of guanosine-26 into dimethylguanosine-26 by the yeast Trm1 tRNA-modifying enzyme. Biochemistry. 33:1994;9546-9551.
13. Freese E., Bautz E., Freese E. B. The chemical and mutagenic specificity of hydroxylamine. Proc. Natl Acad. Sci. USA. 47:1961;845-855.
14. Gabriel K., Schneider J., McClain W. H. Functional evidence for indirect recognition of G.U in tRNA(Ala) by alanyl-tRNA synthetase. Science. 271:1996;195-197.
15. Gehrke C. W., Kuo K. C., McCune R. A., Gerhardt K. O., Agris P. F. Quantitative enzymatic hydrolysis of tRNAs: reversed-phase high-performance liquid chromatography of tRNA nucleosides. J. Chromatog. 230:1982;297-308.
16. Giegé R., Puglisi J. D., Florentz C. tRNA structure and aminoacylation efficiency. Prog. Nucl. Acid Res. Mol. Biol. 45:1993;129-206.
17. Grosjean H., Nicoghosian K., Haumont E., Söll D., Cedergren R. Nucleotide sequences of two serine tRNAs with a GGA anticodon: the structure-function relationships in the serine family of E. coli tRNAs. Nucl. Acids Res. 13:1985;5697-5706.
18. Grosjean H., Haumont E., Droogmans L., Carbon P., Fournier M., de Henau S., Doi T., Keith G., Ganglof J., Kretz K., Trewyn R. A novel approach to the biosynthesis of modified nucleosides in the anticodon loops of eukaryotic transfer RNAs. Bruzik K. S., Stec W. J. Biophosphates and Their Analogues - Synthesis, Structure, Metabolism and Activity. 1987;Elsevier, Amsterdam.
19. Grosjean H., Droogmans L., Giégé R., Uhlenbeck O. C. Guanosine modifications in runoff transcripts of synthetic transfer RNA-Phe genes microinjected into Xenopus oocytes. Biochim. Biophys. Acta. 1050:1990;267-273.
20. Grosjean H., Edqvist J., Stråby K. B., Giegé R. Enzymatic formation of modified nucleosides in tRNA: Dependence on tRNA architecture. J. Mol. Biol. 255:1996;67-85.
21. 5U54)-methyltransferase. Biochemistry. 30:1991;2999-3002.
22. Hagervall T. G., Tuohy T. M., Atkins J. F., Björk G. R. Deficiency of 1-methylguanosine in tRNA from Salmonella typhimurium induces frameshifting by quadruplet translocation. J. Mol. Biol. 232:1993;756-765.
23. Hjalmarsson K. J., Byström A. S., Björk G. R. Purification and characterization of transfer RNA (guanine-1)methyltransferase from Escherichia coli. J. Biol. Chem. 258:1983;1343-1351.
24. Leustructural variants. J. Biol. Chem. 267:1992;13440-13445.
25. 1G methyltransferase interactions: touching bases with structure. Biochimie. 77:1995;62-65.
26. Hooper M. L., Russell R. L., Smith J. D. Miccharging in mutant tyrosine tRNAs. FEBS Letters. 22:1972;149-155.
27. Hüttenhofer A., Weiss-Brummer B., Dirheimer G., Martin R. P. A novel type of+1 frameshift suppressor: a base substitution in the anticodon stem of a yeast mitochondrial serine-tRNA causes frameshift suppression. EMBO J. 9:1990;551-558.
28. Keith G. Mobilities of modified ribonucleotides on two-dimensional cellulose thin-layer chromatography. Biochimie. 77:1995;142-144.
29. Pheand general structural feature of other tRNAs. Schimmel P. R., Söll D., Abelson J. N. Transfer RNA: Structure, Properties and Recognition. 1980;Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
30. Kuchino Y., Yabusaki Y., Mori F., Nishimura S. Nucleotide sequences of three proline tRNAs from Salmonella typhimurium. Nucl. Acids Res. 12:1984;1559-1562.
31. Li J.-N., Björk G. R. 1-methylguanosine deficiency of tRNA influences cognate codon interaction and metabolism in Salmonella typhimurium. J. Bacteriol. 177:1995;6593-6600.
32. Limbach P. A., Crain P. F., McCloskey J. A. Summary: the modified nucleosides of RNA. Nucl. Acids Res. 22:1994;2183-2196.
33. Limmer S., Hofmann H. P., Ott G., Sprinzl M. The 3′-terminal end (NCCA) of tRNA determines the structure and stability of the aminoacyl acceptor stem. Proc. Natl Acad. Sci. USA. 90:1993;6199-6202.
34. Proby Escherichia coli proline tRNA synthetase in vitro. Nucleic Acids Res. 11:1995;165-169.
35. McClain W. H. Rules that govern transfer rna identity in protein synthesis. J. Mol. Biol. 234:1993;257-280.
36. Proidentity. Nucl. Acids Res. 22:1994;522-529.
37. Nakanishi S., Ueda T., Hori H., Yamazaki N., Okada N., Watanabe K. A UGU sequence in the anticodon loop is a minimum requirement for recognition by Escherichia coli tRNA-guanine transglycosylase. J. Biol. Chem. 269:1994;32221-32225.
38. Neidhardt F. C., Bloch P. L., Smith D. F. Culture medium for enterobacteria. J. Bacteriol. 119:1974;736-747.
39. Nishimura S. Chromatographic mobilities of modified nucleotides. Schimmel P. R., Söll D., Abelson J. N. In Transfer RNA: Structure, Properties and Recognition. 1979;Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
40. Nurse K., Wrezesinski J., Bakin A., Lane B. G., Ofengand J. Purification, cloning, and properties of the tRNA Y55 synthetase from Escherichia coli. RNA. 1:1995;102-112.
41. Persson B. C., Bylund G. O., Berg D. E., Wikström P. M. Functional analysis of the ffh-trmD region of the Escherichia coli chromosome by using reverse genetics. J. Bacteriol. 177:1995;5554-5560.
42. Riddle D. L., Roth J. R. Frameshift suppressors. II. Genetic mapping and dominance studies. J. Mol. Biol. 66:1972;483-493.
43. His-containing antigen is recogniszed by the polymyositis-specific antiboy anti-Jo-1. Nucl. Acids Res. 11:1983;853-870.
44. Rould M. A., Perona J. J., Söll D., Steitz T. A. Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution. Science. 246:1989;1135-1142.
45. Sampson J. R., Uhlenbeck O. C. Biochemical and physical characterization of an unmodified yeast phenylalanine transfer RNA transcribed in vitro. Proc. Natl Acad. Sci. USA. 85:1988;1033-1037.
46. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc. Natl Acad. Sci. USA. 74:1977;5463-5467.
47. Schmieger H. Phage P22-mutant with increased transduction abilities. Mol. Gen. Genet. 119:1972;75-88.
48. Schulman L. H. Recognition of tRNAs by aminoacyl-tRNA synthetases. Prog. Nucl. Acid Res. Mol. Biol. 41:1991;23-87.
49. Scott J. F., Roth J. R., Artz S. W. Regulation of histidine operon does not required hisG enzyme. Proc. Nat. Acad. Sci. USA. 72:1975;5021-5025.
50. Shimura Y., Aono H., Ozeki H. Mutant tyrosine tRNA of altered amino acid specificity. FEBS Letters. 22:1972;144-148.
51. IIfrom Salmonella typhimurium induces suppression of frameshift mutations. Nucl. Acids Res. 20:1992;3463-3469.
52. Steinberg S., Misch A., Sprinzl M. Compilation of tRNA sequences and sequences of tRNA genes. Nucl. Acids Res. 21:1993;3011-3015.
53. Sugimoto N., Kierzek R., Turner D. H. Sequence dependence for the energetics of dangling ends and terminal base pairs in ribonucleic acid. Biochemistry. 14:1987;4554-4558.
54. Leuanticodon IAG in Xenopus oocytes. Nucl. Acids Res. 10:1982;7919-7934.
55. Tsang T. H., Buck M., Ames B. N. Sequence specificity of tRNA-modifying enzymes. An analysis of 258 tRNA sequences. Biochim. Biophys. Acta. 741:1983;180-196.
56. Varshney U., Lee C. P., Seong B. L., RajBhandary U. L. Mutants of initiator tRNA that function both as initiators and elongators. J. Biol. Chem. 266:1991;18018-18024.
57. Vogel H. J., Bonner D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J. Biol. Chem. 218:1956;97-106.
58. Yarus M., Cline S., Raftery L., Wier P., Bradley D. The translational efficiency of tRNA is a property of the anticodon arm. J. Biol. Chem. 261:1986;10496-10505.