Shutdown in protein synthesis due to the expression of mini-genes in bacteria

Journal of Molecular Biology

Volumn 291, Issue 4, 1999, Pages 745-759

  Dinçbas, Vildan ^a   Heurgué Hamard, Valérie ^a   Buckingham, Richard H ^b   Karimi, Reza ^a   Ehrenberg, Måns ^a  

^a UPPSALA UNIVERSITY   (Sweden)

^b INST DE BIOLOGIE PHYSICO CHIMIQUE   (France)

Author keywords

Mini gene; Peptidyl tRNA hydrolase; Ribosome recycling; Shine Dalgarno interaction; Translation termination

Indexed keywords

BACTERIAL ENZYME; BACTERIAL PROTEIN; HYDROLASE; PEPTIDYLTRANSFERASE; TRANSFER RNA;

ARTICLE; BACTERIAL GENE; BACTERIAL GROWTH; BACTERIOPHAGE LAMBDA; CELL KILLING; CELL MUTANT; CODON; CONTROLLED STUDY; DRUG HYDROLYSIS; ESCHERICHIA COLI; GENE EXPRESSION; GENETIC TRANSCRIPTION; NONHUMAN; OPEN READING FRAME; PRIORITY JOURNAL; PROTEIN SYNTHESIS INHIBITION; RIBOSOME; STOP CODON; TRANSLATION REGULATION;

BACTERIA (MICROORGANISMS); BACTERIOPHAGE LAMBDA; ESCHERICHIA COLI; NEGIBACTERIA; PROKARYOTA;

EID: 0038689640     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3028     Document Type: Article

References (38)

1. Amann E., Ochs B., Abel K. J. Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins inEscherichia coli. Gene. 69:1988;301-315.
2. Atherly A. G., Menninger J. R. Mutant Escherichia coli strain with temperature sensitive peptidyl-transfer RNA hydrolase. Nature. 240:1972;245-246.
3. Atkins J. F., Gesteland R. F. Regulatory recoding. Hershey J. W. B., Mathews M. B., Sonenberg N. Translational Control. 1996;653-684 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
4. Brunel C., Romby P., Moine H., Caillet J., Grunberg-Manago M., Springer M., Ehresmann B., Ehresmann C. Translational regulation of the Escherichia coli threonyl-tRNA synthetase gene: structural and functional importance of the thrS operator domains. Biochimie. 75:1993;1167-1179.
5. Calogero R. A., Pon C. L., Canonaco M. A., Gualerzi C. O. Selection of the mRNA translation initiation region by Escherichia coli ribosomes. Proc. Natl Acad. Sci. USA. 85:1988;6427-6431.
6. Coulondre C., Miller J. H. Genetic studies of the lac repressor III: additional correlation of mutational sites with specific aminoacid residues. J. Mol. Biol. 117:1977;525-575.
7. Crawford D. J., Ito K., Nakamura Y., Tate W. P. Indirect regulation of translational termination efficiency at highly expressed genes and recoding sites by the factor recycling function of Escherichia coli release factor RF3. EMBO J. 18:1999;727-732.
8. Dong H., Nilsson L., Kurland C. G. Gratuitous overexpression of genes in Escherichia coli leads to growth inhibition and ribosome destruction. J. Bacteriol. 177:1995;1497-1504.
9. 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. 1990;101-129 IRL PressOxford University PressOxford and New York.
10. Freistroffer D. V., Pavlov M. Y., MacDougall J., Buckingham R. H., Ehrenberg M. Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP dependent manner. EMBO J. 16:1997;4126-4133.
11. García Villegas M. R., De La Vega F. M., Galindo J. M., Segura M., Buckingham R. H., Guarneros G. Peptidyl-tRNA hydrolase is involved in lambda inhibition of host protein synthesis. EMBO J. 10:1991;3549-3555.
12. Grentzmann G., Brechemier-Baey D., Heurgué V., Mora L., Buckingham R. H. Localisation and characterisation of the gene encoding release factor RF3 in Escherichia coli. Proc. Natl Acad. Sci. USA. 91:1994;5848-5852.
13. Guzmán P., Guarneros G. Phage genetic sites involved in lambda growth inhibition by the Escherichia colirap mutant. Genetics. 121:1989;401-410.
14. Guzmán P., Rivera B. E., Court D., Gottesman M. E., Guarneros G. Transcription of a bacteriophage lambda site blocks growth of Escherichia coli. J. Bacteriol. 172:1990;1030-1034.
15. Hernández J., Ontiveros C., Valadez J. G., Buckingham R. H., Guarneros G. Regulation of protein synthesis by minigene expression. Biochimie. 79:1997;527-531.
16. Hernández-Sánchez J., Valadez J. G., Herrera J. V., Ontiveros C., Guarneros G. lambda bar minigene-mediated inhibition of protein synthesis involves accumulation of peptidyl-tRNA and starvation for tRNA. EMBO J. 17:1998;3758-3765.
17. Heurgué-Hamard V., Karimi R., Mora L., MacDougall J., Leboeuf C., Grentzmann G., Ehrenberg M., Buckingham R. H. Ribosome release factor RF4 and termination factor RF3 are involved in dissociation of peptidyl-tRNA from the ribosome. EMBO J. 17:1998;808-816.
18. Iost I., Dreyfus M. The stability of Escherichia coli lacZ mRNA depends upon the simultaneity of its synthesis and translation. EMBO J. 14:1995;3252-3261.
19. Jelenc P. C., Kurland C. G. Nucleoside triphosphate regeneration decreases the frequency of translation errors. Proc. Natl Acad. Sci. USA. 76:1979;3174-3178.
20. Karimi R., Pavlov M. Y., Heurgué-Hamard V., Buckingham R. H., Ehrenberg M. Initiation factors IF1 and IF2 synergistically remove small peptidyl-tRNAs from the P-site of E. coli ribosomes. J. Mol. Biol. 281:1998;241-252.
21. Karimi R., Pavlov M. Y., Buckingham R. H., Ehrenberg M. Novel roles for classical factors at the interface between translation termination and initiation. Mol. Cell. 3:1999;601-609.
22. McCormick J. R., Zengel J. M., Lindahl L. Correlation of the translation efficiency with the decay of lac Z mRNA in Escherichia coli. J. Mol. Biol. 239:1994;608-622.
23. Menninger J. R. Peptidyl-transfer RNA dissociates during protein synthesis from ribosomes of E. coli. J. Biol. Chem. 251:1976;3392-3398.
24. Menninger J. R. The accumulation as peptidyl-transfer RNA of isoaccepting transfer RNA families in E. coli with temperature-sensitive peptidyl-transfer RNA hydrolase. J. Biol. Chem. 253:1978;6808-6813.
25. Miller J. H. A Short Course in Bacterial Genetics. 1992;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
26. Ontiveros C., Valadez G., Hernández J., Guarneros G. Inhibition of Escherichia coli protein synthesis by abortive translation of phage λ minigenes. J. Mol. Biol. 269:1997;167-175.
27. Pavlov M., Ehrenberg M. Rate of translation of natural mRNAs in an optimised in vitro translation system. Arch. Biochem. Biophys. 328:1996;9-16.
28. Pavlov M. Y., Freistroffer D., MacDougall J., Buckingham R. H., Ehrenberg M. Fast recycling of E. coli ribosomes requires both ribosome recycling factor (RRF) and release factor RF3. EMBO J. 16:1997;4134-4141.
29. Pavlov M. Y., Freistroffer D. V., Dincbas V., MacDougall J., Buckingham R. H., Ehrenberg M. A direct estimation of the context effect on the efficiency of termination. J. Mol. Biol. 284:1998;579-590.
30. Ryden S. M., Isaksson L. A. A temperature-sensitive mutant of Escherichia coli that shows enhanced misreading of UAG/A and increased efficiency for some tRNA suppressors. Mol. Gen. Genet. 193:1984;38-45.
31. Sambrook J., Fritsch E. F., Maniatis T. Molecular Cloning: A Laboratory Manual. 1989;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
32. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc. Natl Acad. Sci. USA. 74:1977;5463-5467.
33. Shiloach J., Bauer S., de Groot N., Lapidot Y. The influence of the peptide chain length on the activity of peptidyl-tRNA hydrolase from E. coli. Nucl. Acids Res. 2:1975;1941-1950.
34. Soffientini A., Lorenzetti R., Gastado L., Spurio R., La Teana A., Khalid I. Purification procedure for bacterial initiation factors IF1 and IF2. Expr. Purif. 5:1994;118-124.
35. Studier F. W., Moffatt B. A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:1986;113-130.
36. Tate W. P., Caskey C. T. Spedding G. Ribosomes and Protein Synthesis-A Practical Approach. 1990;81-100 IRL Press, Oxford.
37. Tenson T., Herrera J. V., Kloss P., Guarneros G., Mankin A. S. Inhibition of translation and cell growth by minigene expression. J. Bacteriol. 181:1999;1617-1622.
38. Uno M., Ito K., Nakamura Y. Functional specificity of amino acid at position 246 in the tRNA mimicry domain of bacterial release factor 2. Biochimie. 78:1996;935-944.