An A to U transversion at position 1067 of 23 S rRNA from Escherichia coli impairs EF-Tu and EF-G function

Journal of Molecular Biology

Volumn 272, Issue 3, 1997, Pages 327-335

  Saarma, Urmas ^a   Remme, Jaanus ^a   Ehrenberg, Måns ^b   Bilgin, Neş'e ^b,c  

^a UNIVERSITY OF TARTU   (Estonia)

^b UPPSALA UNIVERSITY   (Sweden)

^c UPPSALA UNIVERSITY   (Sweden)

Author keywords

EF G; EF Tu; Ribosome kinetics; rRNA; Translation

Indexed keywords

AMINOACYL TRANSFER RNA; ELONGATION FACTOR G; ELONGATION FACTOR TU; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; RIBOSOME RNA;

ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; DRUG HYDROLYSIS; ESCHERICHIA COLI; GENE MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN RNA BINDING; RIBOSOME; RNA SEQUENCE;

ESCHERICHIA COLI; FELIS CATUS;

EID: 0031587290     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1254     Document Type: Article

References (39)

1. Aevarsson A., Brazhnikov E., Garber M., Zheltonosova J., Chirgadze Yu, Al-karadaghi S., Svensson L. A., Liljas A. Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus. EMBO J. 13:1994;3669-3677.
2. Bilgin N., Ehrenberg M. Mutations in 23 S ribosomal RNA perturb transfer RNA selection and lead to streptomycin dependence. J. Mol. Biol. 235:1994;813-824.
3. Bilgin N., Richter A. A., Ehrenberg M., Dahlberg A. E., Kurland C. G. Ribosomal RNA and protein mutants resistant to spectinomycin. EMBO J. 9:1990;735-739.
4. Bilgin N., Claesens F., Pahverk H., Ehrenberg M. Kinetic properties of Escherichia coli ribosomes with altered forms of S12. J. Mol. Biol. 224:1992;1011-1027.
5. Cundliffe E. Recognition sites for antibiotics within rRNA. The Ribosome, Structure, Function and Evolution. 1990;American Society of Microbiology Press, Washington.
6. Cundliffe E., Thompson J. Concerning the mode of action of micrococcin upon bacterial protein synthesis. Eur. J. Biochem. 118:1981;47-52.
7. Czworkowski J., Moore P. B. The elongation phase of protein synthesis. Prog. Nucl. Acid Res. Mol. Biol. 54:1996;293-332.
8. Czworkowski J., Wang J., Steitz T. A., Moore P. B. The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution. EMBO J. 13:1994;3661-3668.
9. De Rijk P., van de Peer Y., de Wachter R. Database on the structure of large ribosomal subunit RNA. Nucl. Acids Res. 24:1996;92-97.
10. Draper D. E. Ribosomal protein-RNA interactions. Zimmermann R. A., Dahlberg A. E. Ribosomal RNA: Structure, Evolution, Processing and Function. 1996.
11. Egebjerg J., Douthwaite S., Garrett R. A. Antibiotic interactions at the GTPase-associated centre within Escherichia coli 23 S rRNA. EMBO. J. 8:1989;607-611.
12. Ehrenberg M., Bilgin N., Kurland C. G. Design and use of a fast and accurate in vitro translation system. Spedding G. Ribosomes and Protein Synthesis: A Practical Approach. 1990;IRL Press at Oxford University Press, New York.
13. Gale E. F., Cundliffe E., Reynolds P. E., Richmond M. H., Waring M. J. The Molecular Basis of Antibiotic Action. 1981;John Wiley & Sons, London.
14. Gillam J., Millward S., Blew D., von Tigerstrom M., Wimmer E., Tener G. M. The separation of soluble ribonucleic acids on benzoylated diethylaminoethylcellulose. Biochemistry. 6:1967;3043-3056.
15. Jelenc P. C. Rapid purification of highly active ribosomes from Escherichia coli. Anal. Biochem. 105:1980;369-374.
16. Jelenc P. C., Kurland C. G. Nucleoside triphosphate regeneration decreases the frequency of translation errors. Proc. Natl Acad. Sci, USA. 76:1979;3174-3178.
17. Karimi R., Ehrenberg M. Dissociation rate of cognate peptidyl-transfer-RNA from the A-site of hyper-accurate and error-prone ribosomes. Eur. J. Biochem. 226:1994;355-360.
18. Kaziro Y. The role of guanosine-5′-triphosphate in polypeptide chain elongation. Biochim. Biophys. Acta. 505:1978;95-127.
19. Kelmers A. D., Hancher C. W., Phares E. F., Novelli G. D. Large-scale fermentation of Escherichia coli and recovery of transfer ribonucleic acids. Methods Enzymol. 20:1971;3-9.
20. Kurland C. G., Ehrenberg M. Optimization of translational accuracy. Progr. Nucl. Acid Res. Mol. Biol. 31:1984;191-219.
21. Kurland C. G., Hughes D., Ehrenberg M. Limitations of translational accuracy. Neidhardt F. C. Escherichia coli and Salmonella, Cellular and Molecular Biology. 1996;ASM Press, Washington DC.
22. Kutay U. R., Spahn C. M., Nierhaus K. H. Similarities and differences in the inhibition patterns of thiostrepton and viomycin: evidence for two functionally different populations of P-sites when occupied with AcPhe-tRNA. Biochim. Biophys. Acta. 1050:1990;193-196.
23. Mankin A. S., Leviev I., Garrett R. A. Cross-hypersensitivity effects of mutations in 23 S rRNA yield insight into aminoacyl-tRNA binding. J. Mol. Biol. 244:1994;151-157.
24. Moazed D., Noller H. Interaction of tRNA with 23 S rRNA in the ribosomal A, P and E sites. Cell. 57:1989;585-597.
25. Moazed D., Robertson J. M., Noller H. F. Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23 S rRNA. Nature. 334:1988;362-364.
26. Musters W., GonÁalves P. M., Boon K., RauÈ H. A., van Heerikhuizen H., Planta R. J. The conserved GTPase center and variable region V9 from Saccharomyces cerevisiae 26 S rRNA can be replaced by their equivalents from other prokaryotes or eukaryotes without detectable loss of ribosomal function. Proc. Natl Acad. Sci. USA. 88:1991;1469-1473.
27. Phe, EF-Tu, and a GTP analog. Science. 270:1995;1464-1472.
28. Nyborg J., Nissen P., Kjeldgaard M., Thirup S., Polekhina G., Clark B. F. C. Trends Biochem. Sci. 1996.
29. Pedersen S. Escherichia coli ribosomes translate in vivo with variable rate. EMBO J. 3:1984;2895-2898.
30. Rosendahl G., Douthwaite S. The antibiotics micrococcin and thiostrepton interact directly with 23 S rRNA nucleotides 1067A and 1095A. Nucl. Acids Res. 22:1995;357-363.
31. Sköld S. E. Chemical cross-linking of elongation factor G to the 23 S RNA in 70 S ribosomes from Escherichia coli. Nucl. Acids Res. 11:1983;4923-4932.
32. Spahn C. M. T., Remme J., Schäfer M. A., Nierhaus K. H. Mutational analysis of two highly conserved UGG sequences of 23 S rRNA from Escherichia coli. J. Biol. Chem. 271:1996;32849-32856.
33. Tapio S., Bilgin N., Ehrenberg M. Impaired in vitro kinetics of EF-Tu mutant Aa. Eur. J. Biochem. 188:1990;347-354.
34. Thompson J. Ribosomal RNA, translocation, and elongation factor-associated GTP hydrolysis. Zimmermann R. A., Dahlberg A. Ribosomal RNA: Structure, Evolution, Processing and Function. 1996.
35. Thompson J., Schmidt F., Cundliffe E. Site of action of a ribosomal RNA methylase conferring resistance to thiostrepton. J. Biol. Chem. 257:1982;7915-7917.
36. Thompson J., Cundliffe E., Dahlberg A. E. Site-directed mutagenesis of Escherichia coli 23 S ribosomal RNA at position 1067 within the GTP hydrolysis centre. J. Mol. Biol. 203:1988;457-465.
37. Thompson J., Musters W., Cundliffe E., Dahlberg A. E. Replacement of the L11 binding region within E. coli 23 S ribosomal RNA with its homologue from yeast: in vivo and in vitro analysis of hybrid ribosomes altered in the GTPase center. EMBO J. 12:1993;1499-1504.
38. Vazquez D. Inhibitors of Protein Synthesis. 1979;Springer Verlag, New York.
39. Wagner E. G. H., Jelenc P. C., Ehrenberg M., Kurland C. G. Rate of elongation of polyphenylalanine in vitro. Eur. J. Biochem. 122:1982;193-197.