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Volumn 51, Issue 6, 2004, Pages 1705-1717

Overproduction of the Lon protease triggers inhibition of translation in Escherichia coli: Involvement of the yefM-yoeB toxin-antitoxin system

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ANTITOXIN; BACTERIAL TOXIN; ENDOPEPTIDASE LA; MESSENGER RNA; PROTEINASE; UNCLASSIFIED DRUG; YEFM ANTITOXIN; YOEB TOXIN;

EID: 1642483754     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2003.03941.x     Document Type: Article
Times cited : (205)

References (42)
  • 1
    • 0030008368 scopus 로고    scopus 로고
    • An Escherichia coli chromosomal 'addiction module' regulated by guanosine 3′,5′-bispyrophosphate: A model for programmed bacterial cell death
    • Aizenman, E., Engelberg-Kulka, H., and Glaser, G. (1996) An Escherichia coli chromosomal 'addiction module' regulated by guanosine 3′,5′- bispyrophosphate: a model for programmed bacterial cell death. Proc Natl Acad Sci USA 93: 6059-6063.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6059-6063
    • Aizenman, E.1    Engelberg-Kulka, H.2    Glaser, G.3
  • 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., and 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
    • 0033770817 scopus 로고    scopus 로고
    • Control of methionine biosynthesis in Escherichia coli by proteolysis
    • Biran, D., Gur, E., Gollan, L., and Ron, E.Z. (2000) Control of methionine biosynthesis in Escherichia coli by proteolysis. Mol Microbiol 37: 1436-1443.
    • (2000) Mol Microbiol , vol.37 , pp. 1436-1443
    • Biran, D.1    Gur, E.2    Gollan, L.3    Ron, E.Z.4
  • 4
    • 0015810658 scopus 로고
    • Mutants of Escherichia coli with a defect in the degradation of nonsense fragments
    • Bukhari, A.I., and Zipser, D. (1973) Mutants of Escherichia coli with a defect in the degradation of nonsense fragments. Nat New Biol 243: 238-241.
    • (1973) Nat New Biol , vol.243 , pp. 238-241
    • Bukhari, A.I.1    Zipser, D.2
  • 5
    • 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. (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
  • 6
    • 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. (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
  • 7
    • 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, G.H., 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: 809-819.
    • (2003) J Mol Biol , vol.332 , pp. 809-819
    • Christensen, S.K.1    Pedersen, K.2    Hansen, G.H.3    Gerdes, K.4
  • 8
    • 0033985117 scopus 로고    scopus 로고
    • Rapid turnover of FlhD and FlhC, the flagellar regulon transcriptional activator proteins, during Proteus swarming
    • Claret, L., and Hughes, C. (2000) Rapid turnover of FlhD and FlhC, the flagellar regulon transcriptional activator proteins, during Proteus swarming. J Bacteriol 182: 833-836.
    • (2000) J Bacteriol , vol.182 , pp. 833-836
    • Claret, L.1    Hughes, C.2
  • 9
    • 0002657642 scopus 로고
    • DNA replication and the division cycle in Escherichia coli
    • Clark, D., and Maaloe, O. (1967) DNA replication and the division cycle in Escherichia coli. J Mol Biol 23: 99-112.
    • (1967) J Mol Biol , vol.23 , pp. 99-112
    • Clark, D.1    Maaloe, O.2
  • 11
    • 0006101303 scopus 로고    scopus 로고
    • Sok antisense RNA from plasmid R1 is functionally inactivated by RNase e and polyadenylated by poly (A) polymerase I
    • Dam Mikkelsen, N., and Gerdes, K. (1997) Sok antisense RNA from plasmid R1 is functionally inactivated by RNase E and polyadenylated by poly (A) polymerase I. Mol Microbiol 26: 311-320.
    • (1997) Mol Microbiol , vol.26 , pp. 311-320
    • Dam Mikkelsen, N.1    Gerdes, K.2
  • 12
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K.A., and Wanner, B.L. (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 13
    • 0032696759 scopus 로고    scopus 로고
    • Addiction modules and programmed cell death and antideath in bacterial cultures
    • Engelberg-Kulka, H., and Glaser, G. (1999) Addiction modules and programmed cell death and antideath in bacterial cultures. Annu Rev Microbiol 53: 43-70.
    • (1999) Annu Rev Microbiol , vol.53 , pp. 43-70
    • Engelberg-Kulka, H.1    Glaser, G.2
  • 14
    • 0033976914 scopus 로고    scopus 로고
    • Toxin-antitoxin modules may regulate synthesis of macromolecules during nutritional stress
    • Gerdes, K. (2000) Toxin-antitoxin modules may regulate synthesis of macromolecules during nutritional stress. J Bacteriol 182: 561-572.
    • (2000) J Bacteriol , vol.182 , pp. 561-572
    • Gerdes, K.1
  • 15
    • 0035171382 scopus 로고    scopus 로고
    • Emerging views on tmRNA-mediated protein tagging and ribosome rescue
    • Gillet, R., and Felden, B. (2001) Emerging views on tmRNA-mediated protein tagging and ribosome rescue. Mol Microbiol 42: 879-885.
    • (2001) Mol Microbiol , vol.42 , pp. 879-885
    • Gillet, R.1    Felden, B.2
  • 16
    • 0001572474 scopus 로고
    • Topography of cotransducible arginine mutations in E. coli K-12
    • Glansdorff, N. (1965) Topography of cotransducible arginine mutations in E. coli K-12. Genetics 51: 167-179.
    • (1965) Genetics , vol.51 , pp. 167-179
    • Glansdorff, N.1
  • 17
    • 0023216021 scopus 로고
    • An increased content of protease La, the lon gene product, increases protein degradation and blocks growth in Escherichia coli
    • Goff, S.A., and Goldberg, A.L. (1987) An increased content of protease La, the lon gene product, increases protein degradation and blocks growth in Escherichia coli. J Biol Chem 262: 4508-4515.
    • (1987) J Biol Chem , vol.262 , pp. 4508-4515
    • Goff, S.A.1    Goldberg, A.L.2
  • 18
    • 0031816179 scopus 로고    scopus 로고
    • The Escherichia coli relBE genes belong to a new toxin-antitoxin gene family
    • Gotfredsen, M., and 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
  • 19
    • 0033118230 scopus 로고    scopus 로고
    • Regulation by proteolysis: Developmental switches
    • Gottesman, S. (1999) Regulation by proteolysis: developmental switches. Curr Opin Microbiol 2: 142-147.
    • (1999) Curr Opin Microbiol , vol.2 , pp. 142-147
    • Gottesman, S.1
  • 20
    • 0017863123 scopus 로고
    • Deg phenotype of Escherichia coli lon mutants
    • Gottesman, S., and Zipser, D. (1978) Deg phenotype of Escherichia coli lon mutants. J Bacteriol 133: 844-851.
    • (1978) J Bacteriol , vol.133 , pp. 844-851
    • Gottesman, S.1    Zipser, D.2
  • 21
    • 0037338682 scopus 로고    scopus 로고
    • Axe-Txe, a broad-spectrum proteic toxin-antitoxin system specified by a multidrug-resistant, clinical isolate of Enterococcus faecium
    • Grady, R., and Hayes, F. (2003) Axe-Txe, a broad-spectrum proteic toxin-antitoxin system specified by a multidrug-resistant, clinical isolate of Enterococcus faecium. Mol Microbiol 47: 1419-1432.
    • (2003) Mol Microbiol , vol.47 , pp. 1419-1432
    • Grady, R.1    Hayes, F.2
  • 22
    • 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., and 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
  • 23
    • 0038690474 scopus 로고    scopus 로고
    • Regulation by proteolysis in bacterial cells
    • Jenal, U., and Hengge-Aronis, R. (2003) Regulation by proteolysis in bacterial cells. Curr Opin Microbiol 6: 163-172.
    • (2003) Curr Opin Microbiol , vol.6 , pp. 163-172
    • Jenal, U.1    Hengge-Aronis, R.2
  • 24
    • 0028124122 scopus 로고
    • A tRNA-like structure is present in 10Sa RNA, a small stable RNA from Escherichia coli
    • Komine, Y., Kitabatake, M., Yokogawa, T., Nishikawa, K., and Inokuchi, H. (1994) A tRNA-like structure is present in 10Sa RNA, a small stable RNA from Escherichia coli. Proc Natl Acad Sci USA 91: 9223-9227.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 9223-9227
    • Komine, Y.1    Kitabatake, M.2    Yokogawa, T.3    Nishikawa, K.4    Inokuchi, H.5
  • 25
    • 0035958678 scopus 로고    scopus 로고
    • Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli
    • Kuroda, A., Nomura, K., Ohtomo, R., Kato, J., Ikeda, T., Takiguchi, N., Ohtake, H., and Kornberg, A. (2001) Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli. Science 293: 705-708.
    • (2001) Science , vol.293 , pp. 705-708
    • Kuroda, A.1    Nomura, K.2    Ohtomo, R.3    Kato, J.4    Ikeda, T.5    Takiguchi, N.6    Ohtake, H.7    Kornberg, A.8
  • 26
    • 0028985596 scopus 로고
    • Addiction protein Phd of plasmid prophage P1 is a substrate of the ClpXP serine protease of Escherichia coli
    • Lehnherr, H., and Yarmolinsky, M.B. (1995) Addiction protein Phd of plasmid prophage P1 is a substrate of the ClpXP serine protease of Escherichia coli. Proc Natl Acad Sci USA 92: 3274-3277.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3274-3277
    • Lehnherr, H.1    Yarmolinsky, M.B.2
  • 27
    • 0033042119 scopus 로고    scopus 로고
    • Role of lon and ClpX in the post-translational regulation of a sigma subunit of RNA polymerase required for cellular differentiation in Bacillus subtilis
    • Liu, J., Cosby, W.M., and Zuber, P. (1999) Role of lon and ClpX in the post-translational regulation of a sigma subunit of RNA polymerase required for cellular differentiation in Bacillus subtilis. Mol Microbiol 33: 415-428.
    • (1999) Mol Microbiol , vol.33 , pp. 415-428
    • Liu, J.1    Cosby, W.M.2    Zuber, P.3
  • 29
    • 0027522090 scopus 로고
    • chpA and chpB, Escherichia coli chromosomal homologs of the pem locus responsible for stable maintenance of plasmid R100
    • Masuda, Y., Miyakawa, K., Nishimura, Y., and Ohtsubo, E. (1993) chpA and chpB, Escherichia coli chromosomal homologs of the pem locus responsible for stable maintenance of plasmid R100. J Bacteriol 175: 6850-6856.
    • (1993) J Bacteriol , vol.175 , pp. 6850-6856
    • Masuda, Y.1    Miyakawa, K.2    Nishimura, Y.3    Ohtsubo, E.4
  • 30
    • 0022405836 scopus 로고
    • Insertional mutagenesis of the lon gene in Escherichia coli: Ion is dispensabl
    • Maurizi, M.R., Trisler, P., and Gottesman, S. (1985) Insertional mutagenesis of the lon gene in Escherichia coli: Ion is dispensabl. J Bacteriol 164: 1124-1135.
    • (1985) J Bacteriol , vol.164 , pp. 1124-1135
    • Maurizi, M.R.1    Trisler, P.2    Gottesman, S.3
  • 32
    • 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., and 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
  • 33
    • 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. (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
  • 34
    • 0035108209 scopus 로고    scopus 로고
    • Programmed cell death in Escherichia coli: Some antibiotics can trigger mazEF lethality
    • Sat, B., Hazan, R., Fisher, T., Khaner, H., Glaser, G., and Engelberg-Kulka, H. (2001) Programmed cell death in Escherichia coli: some antibiotics can trigger mazEF lethality. J Bacteriol 183: 2041-2045.
    • (2001) J Bacteriol , vol.183 , pp. 2041-2045
    • Sat, B.1    Hazan, R.2    Fisher, T.3    Khaner, H.4    Glaser, G.5    Engelberg-Kulka, H.6
  • 35
    • 0037337680 scopus 로고    scopus 로고
    • The Escherichia coli mazEF suicide module mediates thymineless death
    • Sat, B., Reches, M., and Engelberg-Kulka, H. (2003) The Escherichia coli mazEF suicide module mediates thymineless death. J Bacteriol 185: 1803-1807.
    • (2003) J Bacteriol , vol.185 , pp. 1803-1807
    • Sat, B.1    Reches, M.2    Engelberg-Kulka, H.3
  • 36
    • 0026683731 scopus 로고
    • The stable maintenance system pem of plasmid R100: Degradation of PemI protein may allow PemK protein to inhibit cell growth
    • Tsuchimoto, S., Nishimura, Y., and Ohtsubo, E. (1992) The stable maintenance system pem of plasmid R100: degradation of PemI protein may allow PemK protein to inhibit cell growth. J Bacteriol 174: 4205-4211.
    • (1992) J Bacteriol , vol.174 , pp. 4205-4211
    • Tsuchimoto, S.1    Nishimura, Y.2    Ohtsubo, E.3
  • 37
    • 0028222452 scopus 로고
    • Lon-dependent proteolysis of CcdA is the key control for activation of CcdB in plasmid-free segregant bacteria
    • Van Melderen, L., Bernard, P., and Couturier, M. (1994) Lon-dependent proteolysis of CcdA is the key control for activation of CcdB in plasmid-free segregant bacteria. Mol Microbiol 11: 1151-1157.
    • (1994) Mol Microbiol , vol.11 , pp. 1151-1157
    • Van Melderen, L.1    Bernard, P.2    Couturier, M.3
  • 38
    • 0033032942 scopus 로고    scopus 로고
    • Substrate sequestration by a proteolytically inactive Lon mutant
    • Van Melderen, L., and Gottesman, S. (1999) Substrate sequestration by a proteolytically inactive Lon mutant. Proc Natl Acad Sci USA 96: 6064-6071.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6064-6071
    • Van Melderen, L.1    Gottesman, S.2
  • 39
    • 0032986721 scopus 로고    scopus 로고
    • Conditional stability of the HemA protein (glutamyl-tRNA reductase) regulates heme biosynthesis in Salmonella typhimurium
    • Wang, L., Elliott, M., and Elliott, T. (1999a) Conditional stability of the HemA protein (glutamyl-tRNA reductase) regulates heme biosynthesis in Salmonella typhimurium. J Bacteriol 181: 1211-1219.
    • (1999) J Bacteriol , vol.181 , pp. 1211-1219
    • Wang, L.1    Elliott, M.2    Elliott, T.3
  • 40
    • 0032841896 scopus 로고    scopus 로고
    • A mutant HemA protein with positive charge close to the N terminus is stabilized against heme-regulated proteolysis in Salmonella typhimurium
    • Wang, L., Wilson, S., and Elliott, T. (1999b) A mutant HemA protein with positive charge close to the N terminus is stabilized against heme-regulated proteolysis in Salmonella typhimurium. J Bacteriol 181: 6033-6041.
    • (1999) J Bacteriol , vol.181 , pp. 6033-6041
    • Wang, L.1    Wilson, S.2    Elliott, T.3
  • 41
    • 0029743593 scopus 로고    scopus 로고
    • Caulobacter Lon protease has a critical role in cell-cycle control of DNA methylation
    • Wright, R., Stephens, C., Zweiger, G., Shapiro, L., and Alley, M.R. (1996) Caulobacter Lon protease has a critical role in cell-cycle control of DNA methylation. Genes Dev 10: 1532-1542.
    • (1996) Genes Dev , vol.10 , pp. 1532-1542
    • Wright, R.1    Stephens, C.2    Zweiger, G.3    Shapiro, L.4    Alley, M.R.5
  • 42
    • 0025992789 scopus 로고
    • Residual guanosine 3′,5′-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations
    • Xiao, H., Kalman, M., Ikehara, K., Zemel, S., Glaser, G., and Cashel, M. (1991) Residual guanosine 3′,5′-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations. J Biol Chem 266: 5980-5990.
    • (1991) J Biol Chem , vol.266 , pp. 5980-5990
    • Xiao, H.1    Kalman, M.2    Ikehara, K.3    Zemel, S.4    Glaser, G.5    Cashel, M.6


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