SEARCH

SEARCH BY CITATION

References

  • Afif, H., Allali, N., Couturier, M., and Van Melderen, L. (2001) The ratio between CcdA and CcdB modulates the transcriptional repression of the ccd poison-antidote system. Mol Microbiol 41: 7382.
  • Bech, F.W., Jorgensen, S.T., Diderichsen, B., and Karlstrom, O.H. (1985) Sequence of the relB transcription unit from Escherichia coli and identification of the relB gene. EMBO J 4: 10591066.
  • Bernard, P., and Couturier, M. (1992) Cell killing by the F plasmid CcdB protein involves poisoning of DNA–topoisomerase II complexes. J Mol Biol 226: 735745.
  • Buts, L., Lah, J., Dao-Thi, M.H., Wyns, L., and Loris, R. (2005) Toxin–antitoxin modules as bacterial metabolic stress managers. Trends Biochem Sci 30: 672679.
  • Cherny, I., Rockah, L., and Gazit, E. (2005) The YoeB toxin is a folded protein that forms a physical complex with the unfolded YefM antitoxin. Implications for a structural-based differential stability of toxin–antitoxin systems. J Biol Chem 280: 3006330072.
  • Cherny, I., Overgaard, M., Borch, J., Bram, Y., Gerdes, K., and Gazit, E. (2007) Structural and thermodynamic characterization of the Escherichia coli RelBE toxin–antitoxin system: indication for a functional role of differential stability. Biochemistry 46: 1215212163.
  • Christensen, S.K., and Gerdes, K. (2003) RelE toxins from bacteria and Archaea cleave mRNAs on translating ribosomes, which are rescued by tmRNA. Mol Microbiol 48: 13891400.
  • Christensen, S.K., Mikkelsen, M., Pedersen, K., and Gerdes, K. (2001) RelE, a global inhibitor of translation, is activated during nutritional stress. Proc Natl Acad Sci USA 98: 1432814333.
  • Christensen, S.K., Pedersen, K., Hansen, F.G., and Gerdes, K. (2003) Toxin–antitoxin loci as stress–response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA. J Mol Biol 332: 809819.
  • Christensen-Dalsgaard, M., and Gerdes, K. (2006) Two higBA loci in the Vibrio cholerae superintegron encode mRNA cleaving enzymes and can stabilize plasmids. Mol Microbiol 62: 397411.
  • Dao-Thi, M.H., Charlier, D., Loris, R., Maes, D., Messens, J., Wyns, L., and Backmann, J. (2002) Intricate interactions within the ccd plasmid addiction system. J Biolog Chem 277: 37333742.
  • Gerdes, K., Christensen, S.K., and Lobner-Olesen, A. (2005) Prokaryotic toxin–antitoxin stress response loci. Nat Rev Microbiol 3: 371382.
  • Gotfredsen, M., and Gerdes, K. (1998) The Escherichia coli relBE genes belong to a new toxin–antitoxin gene family. Mol Microbiol 29: 10651076.
  • Guyer, M.S., Reed, R.R., Steitz, J.A., and Low, K.B. (1981) Identification of a sex-factor-affinity site in E. coli as gamma delta. Cold Spring Harb Symp Quant Biol 45 (Part 1): 135140.
  • Guzman, L.M., Belin, D., Carson, M.J., and Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J Bacteriol 177: 41214130.
  • Gvakharia, B.O., Permina, E.A., Gelfand, M.S., Bottomley, P.J., Sayavedra-Soto, L.A., and Arp, D.J. (2007) Global transcriptional response of Nitrosomonas europaea to chloroform and chloromethane. Appl Environ Microbiol 73: 34403445.
  • Jiang, Y., Pogliano, J., Helinski, D.R., and Konieczny, I. (2002) ParE toxin encoded by the broad-host-range plasmid RK2 is an inhibitor of Escherichia coli gyrase. Mol Microbiol 44: 971979.
  • Johnson, E.P., Strom, A.R., and Helinski, D.R. (1996) Plasmid RK2 toxin protein ParE: purification and interaction with the ParD antitoxin protein. J Bacteriol 178: 14201429.
  • Kamada, K., and Hanaoka, F. (2005) Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin. Mol Cell 19: 497509.
  • Kedzierska, B., Lian, L.Y., and Hayes, F. (2007) Toxin–antitoxin regulation: bimodal interaction of YefM–YoeB with paired DNA palindromes exerts transcriptional autorepression. Nucleic Acids Res 35: 325339.
  • Madl, T., Van Melderen, L., Mine, N., Respondek, M., Oberer, M., Keller, W., et al. (2006) Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA. J Mol Biol 364: 170185.
  • Magnuson, P., Lehnherr, H., Mukhopadhyay, G., and Yarmolinsky, M.B. (1996) Autoregulation of the plasmid addiction operon of bacteriophage P1. J Biol Chem 271: 1870518710.
  • Magnuson, R., and Yarmolinsky, M.B. (1998) Corepression of the P1 addiction operon by Phd and Doc. J Bacteriol 180: 63426351.
  • Makarova, K.S., Grishin, N.V., and Koonin, E.V. (2006) The HicAB cassette, a putative novel, RNA-targeting toxin–antitoxin system in archaea and bacteria. Bioinformatics 22: 25812584.
  • Marianovsky, I., Aizenman, E., Engelberg-Kulka, H., and Glaser, G. (2001) The regulation of the Escherichia coli mazEF promoter involves an unusual alternating palindrome. J Biol Chem 276: 59755984.
  • Miki, T., Park, J.A., Nagao, K., Murayama, N., and Horiuchi, T. (1992) Control of segregation of chromosomal DNA by sex factor F in Escherichia coli. Mutants of DNA gyrase subunit A suppress letD (ccdB) product growth inhibition. J Mol Biol 225: 3952.
  • Miller, J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
  • Monti, M.C., Hernandez-Arriaga, A.M., Kamphuis, M.B., Lopez-Villarejo, J., Heck, A.J.R., Boelens, R., et al. (2007) Interactions of kid-kis toxin–antitoxin complexes with the parD operator–promoter region of plasmid R1 are piloted by the Kis antitoxin and tuned by the stoichiometry of kid-kis oligomers. Nucleic Acids Res 35: 17371749.
  • Munoz-Gomez, A.J., Santos-Sierra, S., Berzal-Herranz, A., Lemonnier, M., and Az-Orejas, R. (2004) Insights into the specificity of RNA cleavage by the Escherichia coli MazF toxin. FEBS Lett 567: 316320.
  • Pandey, D.P., and Gerdes, K. (2005) Toxin–antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes. Nucleic Acids Res 33: 966976.
  • Pedersen, K., Christensen, S.K., and Gerdes, K. (2002) Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins. Mol Microbiol 45: 501510.
  • Pedersen, K., Zavialov, A.V., Pavlov, M.Y., Elf, J., Gerdes, K., and Ehrenberg, M. (2003) The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site. Cell 112: 131140.
  • Roberts, R.C., Spangler, C., and Helinski, D.R. (1993) Characteristics and significance of Dna-binding activity of plasmid stabilization protein pard from the broad-host-range plasmid Rk2. J Biol Chem 268: 2710927117.
  • Sambrook, J., Fritsch, E.F., and Maniatis, T. (1989) Molecular Cloning. A Laboratory Manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
  • Schmidt, O., Schuenemann, V.J., Hand, N.J., Silhavy, T.J., Martin, J., Lupas, A.N., and Djuranovic, S. (2007) prlF and yhaV encode a new toxin–antitoxin system in Escherichia coli. J Mol Biol 372: 894905.
  • Sevin, E.W., and Barloy-Hubler, F. (2007) RASTA-Bacteria: a web-based tool for identifying toxin–antitoxin loci in prokaryotes. Genome Biol 8: R155.
  • Tachdjian, S., and Kelly, R.M. (2006) Dynamic metabolic adjustments and genome plasticity are implicated in the heat shock response of the extremely thermoacidophilic archaeon Sulfolobus solfataricus. J Bacteriol 188: 45534559.
  • Takagi, H., Kakuta, Y., Okada, T., Yao, M., Tanaka, I., and Kimura, M. (2005) Crystal structure of archaeal toxin–antitoxin RelE–RelB complex with implications for toxin activity and antitoxin effects. Nat Struct Mol Biol 12: 327331.
  • Tam, J.E., and Kline, B.C. (1989a) Control of the Ccd operon in plasmid-F. J Bacteriol 171: 23532360.
  • Tam, J.E., and Kline, B.C. (1989b) The F plasmid ccd autorepressor is a complex of CcdA and CcdB proteins. Mol Gen Genet 219: 2632.
  • Thaysen-Andersen, M., Jorgensen, S.B., Wilhelmsen, E.S., Petersen, J.W., and Hojrup, P. (2007) Investigation of the detoxification mechanism of formaldehyde-treated tetanus toxin. Vaccine 25: 22132227.
  • Tosa, T., and Pizer, L.I. (1971) Effect of serine hydroxamate on the growth of Escherichia coli. J Bacteriol 106: 966971.
  • Tsuchimoto, S., and Ohtsubo, E. (1993) Autoregulation by cooperative binding of the Pemi and Pemk proteins to the promoter region of the Pem operon. Mol Gen Genet 237: 8188.
  • Van Melderen, L., Thi, M.H.D., Lecchi, P., Gottesman, S., Couturier, M., and Maurizi, M.R. (1996) ATP-dependent degradation of CcdA by Lon protease – effects of secondary structure and heterologous subunit interactions. J Biol Chem 271: 2773027738.
  • Wilbur, J.S., Chivers, P.T., Mattison, K., Potter, L., Brennan, R.G., and So, M. (2005) Neisseria gonorrhoeae FitA interacts with FitB to bind DNA through its ribbon–helix–helix motif. Biochemistry 44: 1251512524.
  • Zhang, Y., Zhang, J., Hoeflich, K.P., Ikura, M., Qing, G., and Inouye, M. (2003) MazF cleaves cellular mRNAs specifically at ACA to block protein synthesis in Escherichia coli. Mol Cell 12: 913923.