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Volumn 380, Issue 1, 2008, Pages 107-119

Structural Mechanism of Transcriptional Autorepression of the Escherichia coli RelB/RelE Antitoxin/Toxin Module

Author keywords

antitoxin; cooperative binding; RelB; RHH; transcriptional repressor

Indexed keywords

ANTITOXIN; BACTERIAL PROTEIN; BACTERIAL TOXIN; DIMER; PALINDROMIC DNA; PROTEIN RELE; TETRAMER; TRANSCRIPTION FACTOR RELB;

EID: 44649143795     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.04.039     Document Type: Article
Times cited : (80)

References (47)
  • 1
    • 0032696759 scopus 로고    scopus 로고
    • Addiction modules and programmed cell death and antideath in bacterial cultures
    • Engelberg-Kulka H., and Glaser G. Addiction modules and programmed cell death and antideath in bacterial cultures. Annu. Rev. Microbiol. 53 (1999) 43-70
    • (1999) Annu. Rev. Microbiol. , vol.53 , pp. 43-70
    • Engelberg-Kulka, H.1    Glaser, G.2
  • 2
    • 0141707105 scopus 로고    scopus 로고
    • Toxins-antitoxins: plasmid maintenance, programmed cell death, and cell cycle arrest
    • Hayes F. Toxins-antitoxins: plasmid maintenance, programmed cell death, and cell cycle arrest. Science 301 (2003) 1496-1499
    • (2003) Science , vol.301 , pp. 1496-1499
    • Hayes, F.1
  • 4
    • 39149110856 scopus 로고    scopus 로고
    • RASTA-Bacteria: a web-based tool for identifying toxin-antitoxin loci in prokaryotes
    • Sevin E.W., and Barloy-Hubler F. RASTA-Bacteria: a web-based tool for identifying toxin-antitoxin loci in prokaryotes. Genome Biol. 8 (2007) R155
    • (2007) Genome Biol. , vol.8
    • Sevin, E.W.1    Barloy-Hubler, F.2
  • 5
    • 0029083946 scopus 로고
    • Programmed cell death in bacteria: proteic plasmid stabilization systems
    • Jensen R.B., and Gerdes K. Programmed cell death in bacteria: proteic plasmid stabilization systems. Mol. Microbiol. 17 (1995) 205-210
    • (1995) Mol. Microbiol. , vol.17 , pp. 205-210
    • Jensen, R.B.1    Gerdes, K.2
  • 6
    • 14244266086 scopus 로고    scopus 로고
    • Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes
    • Pandey D.P., and Gerdes K. Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes. Nucleic Acids Res. 33 (2005) 966-976
    • (2005) Nucleic Acids Res. , vol.33 , pp. 966-976
    • Pandey, D.P.1    Gerdes, K.2
  • 7
    • 0035807805 scopus 로고    scopus 로고
    • RelE, a global inhibitor of translation, is activated during nutritional stress
    • Christensen S.K., Mikkelsen M., Pedersen K., and Gerdes K. RelE, a global inhibitor of translation, is activated during nutritional stress. Proc. Natl Acad. Sci. USA 98 (2001) 14328-14333
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 14328-14333
    • Christensen, S.K.1    Mikkelsen, M.2    Pedersen, K.3    Gerdes, K.4
  • 8
    • 0038797797 scopus 로고    scopus 로고
    • RelE toxins from bacteria and Archaea cleave mRNAs on translating ribosomes, which are rescued by tmRNA
    • Christensen S.K., and Gerdes K. RelE toxins from bacteria and Archaea cleave mRNAs on translating ribosomes, which are rescued by tmRNA. Mol. Microbiol. 48 (2003) 1389-1400
    • (2003) Mol. Microbiol. , vol.48 , pp. 1389-1400
    • Christensen, S.K.1    Gerdes, K.2
  • 9
    • 0037428226 scopus 로고    scopus 로고
    • The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site
    • Pedersen K., Zavialov A.V., Pavlov M.Y., Elf J., Gerdes K., and Ehrenberg M. The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site. Cell 112 (2003) 131-140
    • (2003) Cell , vol.112 , pp. 131-140
    • Pedersen, K.1    Zavialov, A.V.2    Pavlov, M.Y.3    Elf, J.4    Gerdes, K.5    Ehrenberg, M.6
  • 10
    • 0033614011 scopus 로고    scopus 로고
    • Toxin-antitoxin systems homologous with relBE of Escherichia coli plasmid P307 are ubiquitous in prokaryotes
    • Gronlund H., and Gerdes K. Toxin-antitoxin systems homologous with relBE of Escherichia coli plasmid P307 are ubiquitous in prokaryotes. J. Mol. Biol. 285 (1999) 1401-1415
    • (1999) J. Mol. Biol. , vol.285 , pp. 1401-1415
    • Gronlund, H.1    Gerdes, K.2
  • 11
    • 1542472730 scopus 로고    scopus 로고
    • New connections in the prokaryotic toxin-antitoxin network: relationship with the eukaryotic nonsense-mediated RNA decay system
    • Anantharaman V., and Aravind L. New connections in the prokaryotic toxin-antitoxin network: relationship with the eukaryotic nonsense-mediated RNA decay system. Genome Biol. 4 (2003) R81
    • (2003) Genome Biol. , vol.4
    • Anantharaman, V.1    Aravind, L.2
  • 12
    • 18744409067 scopus 로고    scopus 로고
    • Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects
    • Takagi H., Kakuta Y., Okada T., Yao M., Tanaka I., and Kimura M. Crystal structure of archaeal toxin-antitoxin RelE-RelB complex with implications for toxin activity and antitoxin effects. Nat. Struct. Mol. Biol. 12 (2005) 327-331
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 327-331
    • Takagi, H.1    Kakuta, Y.2    Okada, T.3    Yao, M.4    Tanaka, I.5    Kimura, M.6
  • 13
    • 27944437497 scopus 로고    scopus 로고
    • Toxin-antitoxin modules as bacterial metabolic stress managers
    • Buts L., Lah J., Dao-Thi M.H., Wyns L., and Loris R. Toxin-antitoxin modules as bacterial metabolic stress managers. Trends Biochem. Sci. 30 (2005) 672-679
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 672-679
    • Buts, L.1    Lah, J.2    Dao-Thi, M.H.3    Wyns, L.4    Loris, R.5
  • 14
    • 35649008288 scopus 로고    scopus 로고
    • Structural and thermodynamic characterization of the Escherichia coli RelBE toxin-antitoxin system: indication for a functional role of differential stability
    • Cherny I., Overgaard M., Borch J., Bram Y., Gerdes K., and Gazit E. Structural and thermodynamic characterization of the Escherichia coli RelBE toxin-antitoxin system: indication for a functional role of differential stability. Biochemistry 46 (2007) 12152-12163
    • (2007) Biochemistry , vol.46 , pp. 12152-12163
    • Cherny, I.1    Overgaard, M.2    Borch, J.3    Bram, Y.4    Gerdes, K.5    Gazit, E.6
  • 15
    • 0033562629 scopus 로고    scopus 로고
    • Analyzing protein circular dichroism spectra for accurate secondary structures
    • Johnson W.C. Analyzing protein circular dichroism spectra for accurate secondary structures. Proteins: Struct. Funct. Genet. 35 (1999) 307-312
    • (1999) Proteins: Struct. Funct. Genet. , vol.35 , pp. 307-312
    • Johnson, W.C.1
  • 16
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones D.T. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292 (1999) 195-202
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 17
    • 0028519733 scopus 로고
    • An efficient triple-resonance experiment for proton-directed sequential backbone assignment of medium-sized proteins
    • Wang A.C., Lodi P.J., Qin J., Vuister G.W., Gronenborn A.M., and Clore G.M. An efficient triple-resonance experiment for proton-directed sequential backbone assignment of medium-sized proteins. J. Magn. Reson., Ser. B 105 (1994) 196-198
    • (1994) J. Magn. Reson., Ser. B , vol.105 , pp. 196-198
    • Wang, A.C.1    Lodi, P.J.2    Qin, J.3    Vuister, G.W.4    Gronenborn, A.M.5    Clore, G.M.6
  • 21
    • 33750443632 scopus 로고    scopus 로고
    • Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA
    • Madl T., Van Melderen L., Mine N., Respondek M., Oberer M., Keller W., et al. Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA. J. Mol. Biol. 364 (2006) 170-185
    • (2006) J. Mol. Biol. , vol.364 , pp. 170-185
    • Madl, T.1    Van Melderen, L.2    Mine, N.3    Respondek, M.4    Oberer, M.5    Keller, W.6
  • 22
    • 34547564386 scopus 로고    scopus 로고
    • The solution structure of ParD, the antidote of the ParDE toxin-antitoxin module, provides the structural basis for DNA and toxin binding
    • Oberer M., Zangger K., Gruber K., and Keller W. The solution structure of ParD, the antidote of the ParDE toxin-antitoxin module, provides the structural basis for DNA and toxin binding. Protein Sci. 16 (2007) 1676-1688
    • (2007) Protein Sci. , vol.16 , pp. 1676-1688
    • Oberer, M.1    Zangger, K.2    Gruber, K.3    Keller, W.4
  • 23
    • 0022052166 scopus 로고
    • Sequence of the relB transcription unit from Escherichia coli and identification of the relB gene
    • Bech F.W., Jorgensen S.T., Diderichsen B., and Karlstrom O.H. Sequence of the relB transcription unit from Escherichia coli and identification of the relB gene. EMBO J. 4 (1985) 1059-1066
    • (1985) EMBO J. , vol.4 , pp. 1059-1066
    • Bech, F.W.1    Jorgensen, S.T.2    Diderichsen, B.3    Karlstrom, O.H.4
  • 24
    • 0031816179 scopus 로고    scopus 로고
    • The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family
    • Gotfredsen M., and Gerdes K. The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family. Mol. Microbiol. 29 (1998) 1065-1076
    • (1998) Mol. Microbiol. , vol.29 , pp. 1065-1076
    • Gotfredsen, M.1    Gerdes, K.2
  • 26
    • 33645528243 scopus 로고    scopus 로고
    • Structures of omega repressors bound to direct and inverted DNA repeats explain modulation of transcription
    • Weihofen W.A., Cicek A., Pratto F., Alonso J.C., and Saenger W. Structures of omega repressors bound to direct and inverted DNA repeats explain modulation of transcription. Nucleic Acids Res. 34 (2006) 1450-1458
    • (2006) Nucleic Acids Res. , vol.34 , pp. 1450-1458
    • Weihofen, W.A.1    Cicek, A.2    Pratto, F.3    Alonso, J.C.4    Saenger, W.5
  • 28
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert P., Mumenthaler C., and Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273 (1997) 283-298
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 30
    • 0025336625 scopus 로고
    • Structure of Arc repressor in solution: evidence for a family of beta-sheet DNA-binding proteins
    • Breg J.N., van Opheusden J.H., Burgering M.J., Boelens R., and Kaptein R. Structure of Arc repressor in solution: evidence for a family of beta-sheet DNA-binding proteins. Nature 346 (1990) 586-589
    • (1990) Nature , vol.346 , pp. 586-589
    • Breg, J.N.1    van Opheusden, J.H.2    Burgering, M.J.3    Boelens, R.4    Kaptein, R.5
  • 31
    • 0026641755 scopus 로고
    • Crystal structure of the met repressor-operator complex at 2.8 Å resolution reveals DNA recognition by beta-strands
    • Somers W.S., and Phillips S.E. Crystal structure of the met repressor-operator complex at 2.8 Å resolution reveals DNA recognition by beta-strands. Nature 359 (1992) 387-393
    • (1992) Nature , vol.359 , pp. 387-393
    • Somers, W.S.1    Phillips, S.E.2
  • 32
    • 34548046005 scopus 로고    scopus 로고
    • Ribbon-helix-helix transcription factors: variations on a theme
    • Schreiter E.R., and Drennan C.L. Ribbon-helix-helix transcription factors: variations on a theme. Nat. Rev., Microbiol. 5 (2007) 710-720
    • (2007) Nat. Rev., Microbiol. , vol.5 , pp. 710-720
    • Schreiter, E.R.1    Drennan, C.L.2
  • 35
    • 0003845223 scopus 로고    scopus 로고
    • DeLANO Scientific, Palo Alto, CA, USA website at http://www.pymol.org
    • DeLano W.L. The PyMOL molecular graphics system (2002), DeLANO Scientific, Palo Alto, CA, USA. http://www.pymol.org website at http://www.pymol.org
    • (2002) The PyMOL molecular graphics system
    • DeLano, W.L.1
  • 36
    • 0033514299 scopus 로고    scopus 로고
    • Origins of DNA-binding specificity: role of protein contacts with the DNA backbone
    • Schildbach J.F., Karzai A.W., Raumann B.E., and Sauer R.T. Origins of DNA-binding specificity: role of protein contacts with the DNA backbone. Proc. Natl Acad. Sci. USA 96 (1999) 811-817
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 811-817
    • Schildbach, J.F.1    Karzai, A.W.2    Raumann, B.E.3    Sauer, R.T.4
  • 37
    • 23744463273 scopus 로고    scopus 로고
    • Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin
    • Kamada K., and Hanaoka F. Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin. Mol. Cell 19 (2005) 497-509
    • (2005) Mol. Cell , vol.19 , pp. 497-509
    • Kamada, K.1    Hanaoka, F.2
  • 38
    • 0037738520 scopus 로고    scopus 로고
    • Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition
    • Kamada K., Hanaoka F., and Burley S.K. Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition. Mol. Cell 11 (2003) 875-884
    • (2003) Mol. Cell , vol.11 , pp. 875-884
    • Kamada, K.1    Hanaoka, F.2    Burley, S.K.3
  • 39
    • 0344826584 scopus 로고    scopus 로고
    • ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure
    • Golovanov A.P., Barilla D., Golovanova M., Hayes F., and Lian L.Y. ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure. Mol. Microbiol. 50 (2003) 1141-1153
    • (2003) Mol. Microbiol. , vol.50 , pp. 1141-1153
    • Golovanov, A.P.1    Barilla, D.2    Golovanova, M.3    Hayes, F.4    Lian, L.Y.5
  • 41
    • 0032805887 scopus 로고    scopus 로고
    • The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils
    • Nooren I.M., Kaptein R., Sauer R.T., and Boelens R. The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils. Nat. Struct. Biol. 6 (1999) 755-759
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 755-759
    • Nooren, I.M.1    Kaptein, R.2    Sauer, R.T.3    Boelens, R.4
  • 42
    • 33846011436 scopus 로고    scopus 로고
    • Structure of FitAB from Neisseria gonorrhoeae bound to DNA reveals a tetramer of toxin-antitoxin heterodimers containing pin domains and ribbon-helix-helix motifs
    • Mattison K., Wilbur J.S., So M., and Brennan R.G. Structure of FitAB from Neisseria gonorrhoeae bound to DNA reveals a tetramer of toxin-antitoxin heterodimers containing pin domains and ribbon-helix-helix motifs. J. Biol. Chem. 281 (2006) 37942-37951
    • (2006) J. Biol. Chem. , vol.281 , pp. 37942-37951
    • Mattison, K.1    Wilbur, J.S.2    So, M.3    Brennan, R.G.4
  • 43
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • Johnson B.A. Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol. Biol. 278 (2004) 313-352
    • (2004) Methods Mol. Biol. , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 44
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels C., Xia T., Billeter M., Guntert P., and Wuthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR 6 (1995) 1-10
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.2    Billeter, M.3    Guntert, P.4    Wuthrich, K.5
  • 45
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., and Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13 (1999) 289-302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 46
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., and Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8 (1996) 477-486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5


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