메뉴 건너뛰기




Volumn 69, Issue 4, 2008, Pages 841-857

Messenger RNA interferase RelE controls relBE transcription by conditional cooperativity

Author keywords

[No Author keywords available]

Indexed keywords

TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR RELB; TRANSCRIPTION FACTOR RELBE; TRANSCRIPTION FACTOR RELE;

EID: 47749089764     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2008.06313.x     Document Type: Article
Times cited : (166)

References (46)
  • 1
    • 0034939217 scopus 로고    scopus 로고
    • The ratio between CcdA and CcdB modulates the transcriptional repression of the ccd poison-antidote system
    • Afif, H., Allali, N., Couturier, M. Van Melderen, L. (2001) The ratio between CcdA and CcdB modulates the transcriptional repression of the ccd poison-antidote system. Mol Microbiol 41 : 73 82.
    • (2001) Mol Microbiol , vol.41 , pp. 73-82
    • Afif, H.1    Allali, N.2    Couturier, M.3    Van Melderen, L.4
  • 2
    • 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. Karlstrom, O.H. (1985) Sequence of the relB transcription unit from Escherichia coli and identification of the relB gene. EMBO J 4 : 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
  • 3
    • 0026728290 scopus 로고
    • Cell killing by the F plasmid CcdB protein involves poisoning of DNA-topoisomerase II complexes
    • Bernard, P. Couturier, M. (1992) Cell killing by the F plasmid CcdB protein involves poisoning of DNA-topoisomerase II complexes. J Mol Biol 226 : 735 745.
    • (1992) J Mol Biol , vol.226 , pp. 735-745
    • Bernard, P.1    Couturier, M.2
  • 4
    • 27944437497 scopus 로고    scopus 로고
    • Toxin-antitoxin modules as bacterial metabolic stress managers
    • Buts, L., Lah, J., Dao-Thi, M.H., Wyns, L. Loris, R. (2005) Toxin-antitoxin modules as bacterial metabolic stress managers. Trends Biochem Sci 30 : 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
  • 5
    • 24044497249 scopus 로고    scopus 로고
    • 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
    • Cherny, I., Rockah, L. 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 : 30063 30072.
    • (2005) J Biol Chem , vol.280 , pp. 30063-30072
    • Cherny, I.1    Rockah, L.2    Gazit, E.3
  • 6
    • 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. 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 : 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
  • 7
    • 0038797797 scopus 로고    scopus 로고
    • RelE toxins from bacteria and Archaea cleave mRNAs on translating ribosomes, which are rescued by tmRNA
    • Christensen, S.K. Gerdes, K. (2003) RelE toxins from bacteria and Archaea cleave mRNAs on translating ribosomes, which are rescued by tmRNA. Mol Microbiol 48 : 1389 1400.
    • (2003) Mol Microbiol , vol.48 , pp. 1389-1400
    • Christensen, S.K.1    Gerdes, K.2
  • 8
    • 0035807805 scopus 로고    scopus 로고
    • RelE, a global inhibitor of translation, is activated during nutritional stress
    • Christensen, S.K., Mikkelsen, M., Pedersen, K. Gerdes, K. (2001) RelE, a global inhibitor of translation, is activated during nutritional stress. Proc Natl Acad Sci USA 98 : 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
  • 9
    • 0041825422 scopus 로고    scopus 로고
    • Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA
    • Christensen, S.K., Pedersen, K., Hansen, F.G. 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 : 809 819.
    • (2003) J Mol Biol , vol.332 , pp. 809-819
    • Christensen, S.K.1    Pedersen, K.2    Hansen, F.G.3    Gerdes, K.4
  • 10
    • 33749178742 scopus 로고    scopus 로고
    • Two higBA loci in the Vibrio cholerae superintegron encode mRNA cleaving enzymes and can stabilize plasmids
    • Christensen-Dalsgaard, M. Gerdes, K. (2006) Two higBA loci in the Vibrio cholerae superintegron encode mRNA cleaving enzymes and can stabilize plasmids. Mol Microbiol 62 : 397 411.
    • (2006) Mol Microbiol , vol.62 , pp. 397-411
    • Christensen-Dalsgaard, M.1    Gerdes, K.2
  • 13
    • 0031816179 scopus 로고    scopus 로고
    • The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family
    • Gotfredsen, M. Gerdes, K. (1998) The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family. Mol Microbiol 29 : 1065 1076.
    • (1998) Mol Microbiol , vol.29 , pp. 1065-1076
    • Gotfredsen, M.1    Gerdes, K.2
  • 14
    • 0019741898 scopus 로고
    • Identification of a sex-factor-affinity site in E. coli as gamma delta
    • Guyer, M.S., Reed, R.R., Steitz, J.A. 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 1 135 140.
    • (1981) Cold Spring Harb Symp Quant Biol , vol.45 , Issue.1 , pp. 135-140
    • Guyer, M.S.1    Reed, R.R.2    Steitz, J.A.3    Low, K.B.4
  • 15
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L.M., Belin, D., Carson, M.J. Beckwith, J. (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter. J Bacteriol 177 : 4121 4130.
    • (1995) J Bacteriol , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 17
    • 0036098378 scopus 로고    scopus 로고
    • ParE toxin encoded by the broad-host-range plasmid RK2 is an inhibitor of Escherichia coli gyrase
    • Jiang, Y., Pogliano, J., Helinski, D.R. Konieczny, I. (2002) ParE toxin encoded by the broad-host-range plasmid RK2 is an inhibitor of Escherichia coli gyrase. Mol Microbiol 44 : 971 979.
    • (2002) Mol Microbiol , vol.44 , pp. 971-979
    • Jiang, Y.1    Pogliano, J.2    Helinski, D.R.3    Konieczny, I.4
  • 18
    • 0029862847 scopus 로고    scopus 로고
    • Plasmid RK2 toxin protein ParE: Purification and interaction with the ParD antitoxin protein
    • Johnson, E.P., Strom, A.R. Helinski, D.R. (1996) Plasmid RK2 toxin protein ParE: purification and interaction with the ParD antitoxin protein. J Bacteriol 178 : 1420 1429.
    • (1996) J Bacteriol , vol.178 , pp. 1420-1429
    • Johnson, E.P.1    Strom, A.R.2    Helinski, D.R.3
  • 19
    • 23744463273 scopus 로고    scopus 로고
    • Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin
    • Kamada, K. Hanaoka, F. (2005) Conformational change in the catalytic site of the ribonuclease YoeB toxin by YefM antitoxin. Mol Cell 19 : 497 509.
    • (2005) Mol Cell , vol.19 , pp. 497-509
    • Kamada, K.1    Hanaoka, F.2
  • 20
    • 33846680128 scopus 로고    scopus 로고
    • Toxin-antitoxin regulation: Bimodal interaction of YefM-YoeB with paired DNA palindromes exerts transcriptional autorepression
    • Kedzierska, B., Lian, L.Y. Hayes, F. (2007) Toxin-antitoxin regulation: bimodal interaction of YefM-YoeB with paired DNA palindromes exerts transcriptional autorepression. Nucleic Acids Res 35 : 325 339.
    • (2007) Nucleic Acids Res , vol.35 , pp. 325-339
    • Kedzierska, B.1    Lian, L.Y.2    Hayes, F.3
  • 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. (2006) Structural basis for nucleic acid and toxin recognition of the bacterial antitoxin CcdA. J Mol Biol 364 : 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
    • 0029743487 scopus 로고    scopus 로고
    • Autoregulation of the plasmid addiction operon of bacteriophage P1
    • Magnuson, P., Lehnherr, H., Mukhopadhyay, G. Yarmolinsky, M.B. (1996) Autoregulation of the plasmid addiction operon of bacteriophage P1. J Biol Chem 271 : 18705 18710.
    • (1996) J Biol Chem , vol.271 , pp. 18705-18710
    • Magnuson, P.1    Lehnherr, H.2    Mukhopadhyay, G.3    Yarmolinsky, M.B.4
  • 23
    • 0031785682 scopus 로고    scopus 로고
    • Corepression of the P1 addiction operon by Phd and Doc
    • Magnuson, R. Yarmolinsky, M.B. (1998) Corepression of the P1 addiction operon by Phd and Doc. J Bacteriol 180 : 6342 6351.
    • (1998) J Bacteriol , vol.180 , pp. 6342-6351
    • Magnuson, R.1    Yarmolinsky, M.B.2
  • 24
    • 33750420023 scopus 로고    scopus 로고
    • The HicAB cassette, a putative novel, RNA-targeting toxin-antitoxin system in archaea and bacteria
    • Makarova, K.S., Grishin, N.V. Koonin, E.V. (2006) The HicAB cassette, a putative novel, RNA-targeting toxin-antitoxin system in archaea and bacteria. Bioinformatics 22 : 2581 2584.
    • (2006) Bioinformatics , vol.22 , pp. 2581-2584
    • Makarova, K.S.1    Grishin, N.V.2    Koonin, E.V.3
  • 25
    • 0035937194 scopus 로고    scopus 로고
    • The regulation of the Escherichia coli mazEF promoter involves an unusual alternating palindrome
    • Marianovsky, I., Aizenman, E., Engelberg-Kulka, H. Glaser, G. (2001) The regulation of the Escherichia coli mazEF promoter involves an unusual alternating palindrome. J Biol Chem 276 : 5975 5984.
    • (2001) J Biol Chem , vol.276 , pp. 5975-5984
    • Marianovsky, I.1    Aizenman, E.2    Engelberg-Kulka, H.3    Glaser, G.4
  • 26
    • 0026504334 scopus 로고
    • 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
    • Miki, T., Park, J.A., Nagao, K., Murayama, N. 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 : 39 52.
    • (1992) J Mol Biol , vol.225 , pp. 39-52
    • Miki, T.1    Park, J.A.2    Nagao, K.3    Murayama, N.4    Horiuchi, T.5
  • 27
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • Miller, J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor, NY : Cold Spring Harbor Laboratory Press.
    • (1972) Experiments in Molecular Genetics.
    • Miller, J.H.1
  • 28
    • 34247133389 scopus 로고    scopus 로고
    • 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
    • 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 : 1737 1749.
    • (2007) Nucleic Acids Res , vol.35 , pp. 1737-1749
    • Monti, M.C.1    Hernandez-Arriaga, A.M.2    Kamphuis, M.B.3    Lopez-Villarejo, J.4    Heck, A.J.R.5    Boelens, R.6
  • 30
    • 14244266086 scopus 로고    scopus 로고
    • Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes
    • Pandey, D.P. Gerdes, K. (2005) Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes. Nucleic Acids Res 33 : 966 976.
    • (2005) Nucleic Acids Res , vol.33 , pp. 966-976
    • Pandey, D.P.1    Gerdes, K.2
  • 31
    • 0036067108 scopus 로고    scopus 로고
    • Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins
    • Pedersen, K., Christensen, S.K. Gerdes, K. (2002) Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins. Mol Microbiol 45 : 501 510.
    • (2002) Mol Microbiol , vol.45 , pp. 501-510
    • Pedersen, K.1    Christensen, S.K.2    Gerdes, K.3
  • 32
    • 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. Ehrenberg, M. (2003) The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site. Cell 112 : 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
  • 33
    • 0027732050 scopus 로고
    • Characteristics and significance of Dna-binding activity of plasmid stabilization protein pard from the broad-host-range plasmid Rk2
    • Roberts, R.C., Spangler, C. 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 : 27109 27117.
    • (1993) J Biol Chem , vol.268 , pp. 27109-27117
    • Roberts, R.C.1    Spangler, C.2    Helinski, D.R.3
  • 36
    • 39149110856 scopus 로고    scopus 로고
    • RASTA-Bacteria: A web-based tool for identifying toxin-antitoxin loci in prokaryotes
    • Sevin, E.W. Barloy-Hubler, F. (2007) RASTA-Bacteria: a web-based tool for identifying toxin-antitoxin loci in prokaryotes. Genome Biol 8 : R155.
    • (2007) Genome Biol , vol.8
    • Sevin, E.W.1    Barloy-Hubler, F.2
  • 37
    • 33745008644 scopus 로고    scopus 로고
    • Dynamic metabolic adjustments and genome plasticity are implicated in the heat shock response of the extremely thermoacidophilic archaeon Sulfolobus solfataricus
    • Tachdjian, S. 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 : 4553 4559.
    • (2006) J Bacteriol , vol.188 , pp. 4553-4559
    • Tachdjian, S.1    Kelly, R.M.2
  • 38
    • 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. 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 : 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
  • 39
    • 0024670831 scopus 로고
    • Control of the Ccd operon in plasmid-F
    • Tam, J.E. Kline, B.C. (1989a) Control of the Ccd operon in plasmid-F. J Bacteriol 171 : 2353 2360.
    • (1989) J Bacteriol , vol.171 , pp. 2353-2360
    • Tam, J.E.1    Kline, B.C.2
  • 40
    • 0024747885 scopus 로고
    • The F plasmid ccd autorepressor is a complex of CcdA and CcdB proteins
    • Tam, J.E. Kline, B.C. (1989b) The F plasmid ccd autorepressor is a complex of CcdA and CcdB proteins. Mol Gen Genet 219 : 26 32.
    • (1989) Mol Gen Genet , vol.219 , pp. 26-32
    • Tam, J.E.1    Kline, B.C.2
  • 41
    • 33846885899 scopus 로고    scopus 로고
    • Investigation of the detoxification mechanism of formaldehyde-treated tetanus toxin
    • Thaysen-Andersen, M., Jorgensen, S.B., Wilhelmsen, E.S., Petersen, J.W. Hojrup, P. (2007) Investigation of the detoxification mechanism of formaldehyde-treated tetanus toxin. Vaccine 25 : 2213 2227.
    • (2007) Vaccine , vol.25 , pp. 2213-2227
    • Thaysen-Andersen, M.1    Jorgensen, S.B.2    Wilhelmsen, E.S.3    Petersen, J.W.4    Hojrup, P.5
  • 42
    • 0015081154 scopus 로고
    • Effect of serine hydroxamate on the growth of Escherichia coli
    • Tosa, T. Pizer, L.I. (1971) Effect of serine hydroxamate on the growth of Escherichia coli. J Bacteriol 106 : 966 971.
    • (1971) J Bacteriol , vol.106 , pp. 966-971
    • Tosa, T.1    Pizer, L.I.2
  • 43
    • 0027461096 scopus 로고
    • Autoregulation by cooperative binding of the Pemi and Pemk proteins to the promoter region of the Pem operon
    • Tsuchimoto, S. 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 : 81 88.
    • (1993) Mol Gen Genet , vol.237 , pp. 81-88
    • Tsuchimoto, S.1    Ohtsubo, E.2
  • 44
    • 0029861722 scopus 로고    scopus 로고
    • ATP-dependent degradation of CcdA by Lon protease - Effects of secondary structure and heterologous subunit interactions
    • Van Melderen, L., Thi, M.H.D., Lecchi, P., Gottesman, S., Couturier, M. Maurizi, M.R. (1996) ATP-dependent degradation of CcdA by Lon protease - effects of secondary structure and heterologous subunit interactions. J Biol Chem 271 : 27730 27738.
    • (1996) J Biol Chem , vol.271 , pp. 27730-27738
    • Van Melderen, L.1    Thi, M.H.D.2    Lecchi, P.3    Gottesman, S.4    Couturier, M.5    Maurizi, M.R.6
  • 45
    • 24944525711 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae FitA interacts with FitB to bind DNA through its ribbon-helix-helix motif
    • Wilbur, J.S., Chivers, P.T., Mattison, K., Potter, L., Brennan, R.G. So, M. (2005) Neisseria gonorrhoeae FitA interacts with FitB to bind DNA through its ribbon-helix-helix motif. Biochemistry 44 : 12515 12524.
    • (2005) Biochemistry , vol.44 , pp. 12515-12524
    • Wilbur, J.S.1    Chivers, P.T.2    Mattison, K.3    Potter, L.4    Brennan, R.G.5    So, M.6
  • 46
    • 0242361323 scopus 로고    scopus 로고
    • MazF cleaves cellular mRNAs specifically at ACA to block protein synthesis in Escherichia coli
    • Zhang, Y., Zhang, J., Hoeflich, K.P., Ikura, M., Qing, G. Inouye, M. (2003) MazF cleaves cellular mRNAs specifically at ACA to block protein synthesis in Escherichia coli. Mol Cell 12 : 913 923.
    • (2003) Mol Cell , vol.12 , pp. 913-923
    • Zhang, Y.1    Zhang, J.2    Hoeflich, K.P.3    Ikura, M.4    Qing, G.5    Inouye, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.