The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site

Cell

Volumn 112, Issue 1, 2003, Pages 131-140

  Pedersen, Kim ^a   Zavialov, Andrey V ^b   Pavlov, Michael Yu ^b   Elf, Johan ^b   Gerdes, Kenn ^a   Ehrenberg, Måns ^b  

^a UNIVERSITY OF SOUTHERN DENMARK   (Denmark)

^b UPPSALA UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; BACTERIAL TOXIN; MESSENGER RNA; PROTEIN SYNTHESIS INHIBITOR;

ADAPTATION; BACTERIAL GENE; BIOCHEMISTRY; CATALYSIS; ESCHERICHIA COLI; GENE INACTIVATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN SECRETION; PROTEIN SYNTHESIS INHIBITION; REVIEW; RIBOSOME SUBUNIT; RNA CLEAVAGE; RNA DEGRADATION; RNA SEQUENCE; STOP CODON;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PROKARYOTA;

EID: 0037428226     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(02)01248-5     Document Type: Article

References (43)

1. Bech F.W., Jorgensen S.T., Diderichsen B., Karlstrom O.H. Sequence of the relB transcription unit from Escherichia coli and identification of the relB gene. EMBO J. 4:1985;1059-1066.
2. Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.et al. The complete genome sequence of Escherichia coli K-12. Science. 277:1997;1453-1474.
3. Block R., Haseltine A.W. Purification and properties of stringent factor. J. Biol. Chem. 250:1975;1212-1217.
4. Brunschede H., Bremer H. Synthesis and breakdown of proteins in Escherichia coli during amino-acid starvation. J. Mol. Biol. 37:1971;35-57.
5. Cashel M., Gentry D., Hernandez V.J., Vinella D. The stringent response. Neidthardt F.C. Escherichia coli and Salmonella. 1996;ASM Press, Washington, DC. 1458-1496.pp.
6. Christensen S.K., Mikkelsen M., Pedersen K., Gerdes K. RelE, a global inhibitor of translation, is activated during nutritional stress. Proc. Natl. Acad. Sci. USA. 98:2001;14328-14333.
7. Diderichsen B., Desmarez L. Variations in phenotype of relB mutants of Escherichia coli and the effect of pus and sup mutations. Mol. Gen. Genet. 180:1980;429-437.
8. Diderichsen B., Fiil N.P., Lavalle R. Genetics of the relB locus in Escherichia coli. J. Bacteriol. 131:1977;30-33.
9. Fersht A. Structure and Mechanism in Protein Science. A Guide to Enzyme Catalysis and Protein Folding:1999;W.H. Freeman & Co, New York.
10. Fiil N.P., Willumsen B.M., von Meyenburg K. Interaction of alleles of the relA, relC and spoT genes in Escherichia coli. analysis of the interconversion of GTP, ppGpp and pppGpp Mol. Gen. Genet. 150:1977;87-101.
11. 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.
12. Freistroffer D.V., Kwiatkowski M., Buckingham R.H., Ehrenberg M. The accuracy of codon recognition by polypeptide release factors. Proc. Natl. Acad. Sci. USA. 97:2000;2046-2051.
13. Galvani C., Terry J., Ishiguro E.E. Purification of the RelB and RelE proteins of Escherichia coli. RelE binds to RelB and to ribosomes J. Bacteriol. 183:2001;2700-2703.
14. Gerdes K. Toxin-antitoxin modules may regulate synthesis of macromolecules during nutritional stress. J. Bacteriol. 182:2000;561-572.
15. Gillet R., Felden B. Emerging views on tmRNA-mediated protein tagging and ribosome rescue. Mol. Microbiol. 42:2001;879-885.
16. Gotfredsen M., Gerdes K. The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family. Mol. Microbiol. 29:1998;1065-1076.
17. Gottesman S., Maurizi M.R. Surviving starvation. Science. 293:2001;614-615.
18. Guzman P., Guarneros G. Phage genetic sites involved in lambda growth inhibition by the Escherichia coli rap mutant. Genetics. 121:1989;401-409.
19. Hastie T., Tibshirani R., Friedman J. The elements of statistical learning. 2001;Springer, New York, USA.
20. Hazan R., Sat B., Reches M., Engelberg-Kulka H. Postsegregational killing mediated by the P1 phage "addiction module" phd-doc requires the Escherichia coli programmed cell death system mazEF. J. Bacteriol. 183:2001;2046-2050.
21. Jelenc P.C., Kurland C.G. Nucleoside triphosphate regeneration decreases the frequency of translation errors. Proc. Natl. Acad. Sci. USA. 76:1979;3174-3178.
22. Jensen R.B., Gerdes K. Programmed cell death in bacteria. proteic plasmid stabilization systems Mol. Microbiol. 17:1995;205-210.
23. 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.
24. Karzai A.W., Roche E.D., Sauer R.T. The SsrA-SmpB system for protein tagging, directed degradation and ribosome rescue. Nat. Struct. Biol. 7:2000;449-455.
25. Keiler K.C., Waller P.R., Sauer R.T. Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA. Science. 271:1996;990-993.
26. Kisselev L.L., Buckingham R.H. Translational termination comes of age. Trends Biochem. Sci. 25:2000;561-566.
27. Kuroda A., Nomura K., Ohtomo R., Kato J., Ikeda T., Takiguchi N., Ohtake H., Kornberg A. Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli. Science. 293:2001;705-708.
28. Lavallé R. Nouveaux mutants de regulation de la synthese de l'ARN. Bull. Soc. Chim. Biol. 47:1965;1567-1570.
29. Lavallé R., Desmarez L., deHauwer G. Natural messenger translation impairment in an E. coli mutant. Kjeldgaard N.O., Maaloe O. In Control of Ribosome Synthesis, Alfred Benzon symposium IX. 1976;Munksgaard, Copenhagen., pp. 408-416.
30. Mosteller R.D. Evidence that glucose starvation-sensitive mutants are altered in the relB locus. J. Bacteriol. 133:1978;1034-1037.
31. Monro R.E., Staehelin T., Celma M.L., Vazquez D. The peptidyl transferase activity of ribosomes. Cold Spring Harb. Symp. Quant. Biol. 34:1969;357-368.
32. Nielsen K., Boston R.S. Ribosome-inactivating proteins. a plant perspective Annu. Rev. Plant Physiol. Plant Mol. Biol. 52:2001;785-816.
33. O'Farrell P.H. The suppression of defective translation by ppGpp and its role in the stringent response. Cell. 14:1978;545-557.
34. Ogawa T., Tomita K., Ueda T., Watanabe K., Uozumi T., Masaki H. A cytotoxic ribonuclease targeting specific transfer RNA anticodons. Science. 283:1999;2097-2100.
35. Pavlov M.Y., Freistroffer D.V., MacDougall J., Buckingham R.H., Ehrenberg M. Fast recycling of Escherichia coli ribosomes requires both ribosomal recycling factor (RRF) and release factor RF3. EMBO J. 16:1997;4134-4141.
36. Pedersen K., Christensen S.K., Gerdes K. Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins. Mol. Microbiol. 45:2002;501-510.
37. Peumans W.J., Hao Q., Van Damme E.J. Ribosome-inactivating proteins from plants. more than RNA N-glycosidases? FASEB J. 15:2001;1493-1506.
38. Riley M.A., Gordon D.M. The ecological role of bacteriocins in bacterial competition. Trends Microbiol. 7:1999;129-133.
39. Soelaiman S., Jakes K., Wu N., Li C., Shoham M. Crystal structure of colicin E3. implications for cell entry and ribosome inactivation Mol. Cell. 8:2001;1053-1062.
40. Somerville C.R., Ahmed A. Mutants of Escherichia coli defective in the degradation of guanosine 5′-triphosphate, 3′-diphosphate (ppGpp). Mol. Gen. Genet. 169:1979;315-323.
41. Wool I.G., Gluck A., Endo Y. Ribotoxin recognition of ribosomal RNA and a proposal for the mechanism of translocation. Trends Biochem. Sci. 17:1992;266-269.
42. Zavialov A.V., Buckingham R.H., Ehrenberg M. A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3. Cell. 107:2001;115-124.
43. Zavialov A.V., Mora L., Buckingham R.H., Ehrenberg M. Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3. Mol. Cell. 10:2002;789-798.