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Volumn 35, Issue 2, 2009, Pages 154-163

Rejuvenation of CcdB-Poisoned Gyrase by an Intrinsically Disordered Protein Domain

Author keywords

DNA; MICROBIO; PROTEINS

Indexed keywords

ANTITOXIN; CCDB ANTITOXIN; UNCLASSIFIED DRUG;

EID: 67651091627     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2009.05.025     Document Type: Article
Times cited : (136)

References (46)
  • 1
    • 0001314221 scopus 로고
    • The hemoglobin system. VI. The oxygen dissociation curve of hemoglobin
    • Adair G.S. The hemoglobin system. VI. The oxygen dissociation curve of hemoglobin. J. Biol. Chem. 63 (1925) 529-545
    • (1925) J. Biol. Chem. , vol.63 , pp. 529-545
    • Adair, G.S.1
  • 2
    • 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., and Van Melderen L. The ratio between CcdA and CcdB modulates the transcriptional repression of the ccd poison-antidote system. Mol. Microbiol. 41 (2001) 73-82
    • (2001) Mol. Microbiol. , vol.41 , pp. 73-82
    • Afif, H.1    Allali, N.2    Couturier, M.3    Van Melderen, L.4
  • 4
    • 0025761119 scopus 로고
    • The 41 carboxy-terminal residues of the miniF plasmid CcdA protein are sufficient to antagonize the killer activity of the CcdB protein
    • Bernard P., and Couturier M. The 41 carboxy-terminal residues of the miniF plasmid CcdA protein are sufficient to antagonize the killer activity of the CcdB protein. Mol. Gen. Genet. 226 (1991) 297-304
    • (1991) Mol. Gen. Genet. , vol.226 , pp. 297-304
    • Bernard, P.1    Couturier, M.2
  • 5
    • 0026728290 scopus 로고
    • Cell killing by the F plasmid CcdB protein involves poisoning of DNA-topoisomerase II complexes
    • Bernard P., and Couturier M. Cell killing by the F plasmid CcdB protein involves poisoning of DNA-topoisomerase II complexes. J. Mol. Biol. 226 (1992) 735-745
    • (1992) J. Mol. Biol. , vol.226 , pp. 735-745
    • Bernard, P.1    Couturier, M.2
  • 8
    • 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
  • 9
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, N.4
    • Collaborative Computational Project, N.4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 10
    • 0031558807 scopus 로고    scopus 로고
    • The interaction of the F plasmid killer protein, CcdB, with DNA gyrase: induction of DNA cleavage and blocking of transcription
    • Critchlow S.E., O'Dea M.H., Howells A.J., Couturier M., Gellert M., and Maxwell A. The interaction of the F plasmid killer protein, CcdB, with DNA gyrase: induction of DNA cleavage and blocking of transcription. J. Mol. Biol. 273 (1997) 826-839
    • (1997) J. Mol. Biol. , vol.273 , pp. 826-839
    • Critchlow, S.E.1    O'Dea, M.H.2    Howells, A.J.3    Couturier, M.4    Gellert, M.5    Maxwell, A.6
  • 14
    • 37549023863 scopus 로고    scopus 로고
    • Structural basis for gate-DNA recognition and bending by type IIA topoisomerases
    • Dong K.C., and Berger J.M. Structural basis for gate-DNA recognition and bending by type IIA topoisomerases. Nature 450 (2007) 1201-1205
    • (2007) Nature , vol.450 , pp. 1201-1205
    • Dong, K.C.1    Berger, J.M.2
  • 15
    • 40949105259 scopus 로고    scopus 로고
    • Signal transduction via unstructured protein conduits
    • Dunker A.K., and Uversky V.N. Signal transduction via unstructured protein conduits. Nat. Chem. Biol. 4 (2008) 229-230
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 229-230
    • Dunker, A.K.1    Uversky, V.N.2
  • 16
    • 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
  • 18
    • 0032947158 scopus 로고    scopus 로고
    • Quaternary changes in topoisomerase II may direct orthogonal movement of two DNA strands
    • Fass D., Bogden C.E., and Berger J.M. Quaternary changes in topoisomerase II may direct orthogonal movement of two DNA strands. Nat. Struct. Biol. 6 (1999) 322-326
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 322-326
    • Fass, D.1    Bogden, C.E.2    Berger, J.M.3
  • 19
    • 0033976914 scopus 로고    scopus 로고
    • Toxin-antitoxin modules may regulate synthesis of macromolecules during nutritional stress
    • Gerdes K. Toxin-antitoxin modules may regulate synthesis of macromolecules during nutritional stress. J. Bacteriol. 182 (2000) 561-572
    • (2000) J. Bacteriol. , vol.182 , pp. 561-572
    • Gerdes, K.1
  • 21
    • 0029862847 scopus 로고    scopus 로고
    • Plasmid RK2 toxin protein ParE: purification and interaction with the ParD antitoxin protein
    • Johnson E.P., Strom A.R., and Helinski D.R. Plasmid RK2 toxin protein ParE: purification and interaction with the ParD antitoxin protein. J. Bacteriol. 178 (1996) 1420-1429
    • (1996) J. Bacteriol. , vol.178 , pp. 1420-1429
    • Johnson, E.P.1    Strom, A.R.2    Helinski, D.R.3
  • 22
    • 0032756532 scopus 로고    scopus 로고
    • The interaction of DNA gyrase with the bacterial toxin CcdB: evidence for the existence of two gyrase-CcdB complexes
    • Kampranis S.C., Howells A.J., and Maxwell A. The interaction of DNA gyrase with the bacterial toxin CcdB: evidence for the existence of two gyrase-CcdB complexes. J. Mol. Biol. 293 (1999) 733-744
    • (1999) J. Mol. Biol. , vol.293 , pp. 733-744
    • Kampranis, S.C.1    Howells, A.J.2    Maxwell, A.3
  • 23
    • 35548944074 scopus 로고    scopus 로고
    • A linear pentapeptide is a quorum-sensing factor required for mazEF-mediated cell death in Escherichia coli
    • Kolodkin-Gal I., Hazan R., Gaathon A., Carmeli S., and Engelberg-Kulka H. A linear pentapeptide is a quorum-sensing factor required for mazEF-mediated cell death in Escherichia coli. Science 318 (2007) 652-655
    • (2007) Science , vol.318 , pp. 652-655
    • Kolodkin-Gal, I.1    Hazan, R.2    Gaathon, A.3    Carmeli, S.4    Engelberg-Kulka, H.5
  • 24
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland Jr. D.E., Nemethy G., and Filmer D. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5 (1966) 365-385
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland Jr., D.E.1    Nemethy, G.2    Filmer, D.3
  • 25
    • 0004238344 scopus 로고    scopus 로고
    • Oxford Univ. Press and Cell Press, New York
    • Lewin B. Genes VII (2000), Oxford Univ. Press and Cell Press, New York
    • (2000) Genes VII
    • Lewin, B.1
  • 28
    • 0031785682 scopus 로고    scopus 로고
    • Corepression of the P1 addiction operon by Phd and Doc
    • Magnuson R., and Yarmolinsky M.B. Corepression of the P1 addiction operon by Phd and Doc. J. Bacteriol. 180 (1998) 6342-6351
    • (1998) J. Bacteriol. , vol.180 , pp. 6342-6351
    • Magnuson, R.1    Yarmolinsky, M.B.2
  • 29
    • 34548488930 scopus 로고    scopus 로고
    • Hypothetical functions of toxin-antitoxin systems
    • Magnuson R.D. Hypothetical functions of toxin-antitoxin systems. J. Bacteriol. 189 (2007) 6089-6092
    • (2007) J. Bacteriol. , vol.189 , pp. 6089-6092
    • Magnuson, R.D.1
  • 30
    • 0029871378 scopus 로고    scopus 로고
    • Partner switching mechanisms in inactivation and rejuvenation of Escherichia coli DNA gyrase by F plasmid proteins LetD (CcdB) and LetA (CcdA)
    • Maki S., Takiguchi S., Horiuchi T., Sekimizu K., and Miki T. Partner switching mechanisms in inactivation and rejuvenation of Escherichia coli DNA gyrase by F plasmid proteins LetD (CcdB) and LetA (CcdA). J. Mol. Biol. 256 (1996) 473-482
    • (1996) J. Mol. Biol. , vol.256 , pp. 473-482
    • Maki, S.1    Takiguchi, S.2    Horiuchi, T.3    Sekimizu, K.4    Miki, T.5
  • 31
    • 0021685636 scopus 로고
    • Control of cell division by sex factor F in Escherichia coli. I. The 42.84-43.6 F segment couples cell division of the host bacteria with replication of plasmid DNA
    • Miki T., Yoshioka K., and Horiuchi T. Control of cell division by sex factor F in Escherichia coli. I. The 42.84-43.6 F segment couples cell division of the host bacteria with replication of plasmid DNA. J. Mol. Biol. 174 (1984) 605-625
    • (1984) J. Mol. Biol. , vol.174 , pp. 605-625
    • Miki, T.1    Yoshioka, K.2    Horiuchi, T.3
  • 32
    • 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., Boelens R., Diaz-Orejas R., and van den Heuvel R.H. 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 (2007) 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.5    Boelens, R.6    Diaz-Orejas, R.7    van den Heuvel, R.H.8
  • 35
    • 37649005671 scopus 로고    scopus 로고
    • MazF, an mRNA interferase, mediates programmed cell death during multicellular Myxococcus development
    • Nariya H., and Inouye M. MazF, an mRNA interferase, mediates programmed cell death during multicellular Myxococcus development. Cell 132 (2008) 55-66
    • (2008) Cell , vol.132 , pp. 55-66
    • Nariya, H.1    Inouye, M.2
  • 36
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z.M.W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 257 (1997) 307-326
    • (1997) Methods Enzymol. , vol.257 , pp. 307-326
    • Otwinowski, Z.M.W.1
  • 37
    • 47749089764 scopus 로고    scopus 로고
    • Messenger RNA interferase RelE controls relBE transcription by conditional cooperativity
    • Overgaard M., Borch J., Jorgensen M.G., and Gerdes K. Messenger RNA interferase RelE controls relBE transcription by conditional cooperativity. Mol. Microbiol. 69 (2008) 841-857
    • (2008) Mol. Microbiol. , vol.69 , pp. 841-857
    • Overgaard, M.1    Borch, J.2    Jorgensen, M.G.3    Gerdes, K.4
  • 38
    • 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
  • 41
    • 0025726701 scopus 로고
    • Probing the limits of the DNA breakage-reunion domain of the Escherichia coli DNA gyrase A protein
    • Reece R.J., and Maxwell A. Probing the limits of the DNA breakage-reunion domain of the Escherichia coli DNA gyrase A protein. J. Biol. Chem. 266 (1991) 3540-3546
    • (1991) J. Biol. Chem. , vol.266 , pp. 3540-3546
    • Reece, R.J.1    Maxwell, A.2
  • 42
    • 0024670831 scopus 로고
    • Control of the ccd operon in plasmid F
    • Tam J.E., and Kline B.C. Control of the ccd operon in plasmid F. J. Bacteriol. 171 (1989) 2353-2360
    • (1989) J. Bacteriol. , vol.171 , pp. 2353-2360
    • Tam, J.E.1    Kline, B.C.2
  • 43
    • 0024747885 scopus 로고
    • The F plasmid ccd autorepressor is a complex of CcdA and CcdB proteins
    • Tam J.E., and Kline B.C. The F plasmid ccd autorepressor is a complex of CcdA and CcdB proteins. Mol. Gen. Genet. 219 (1989) 26-32
    • (1989) Mol. Gen. Genet. , vol.219 , pp. 26-32
    • Tam, J.E.1    Kline, B.C.2
  • 44
    • 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. Lon-dependent proteolysis of CcdA is the key control for activation of CcdB in plasmid-free segregant bacteria. Mol. Microbiol. 11 (1994) 1151-1157
    • (1994) Mol. Microbiol. , vol.11 , pp. 1151-1157
    • Van Melderen, L.1    Bernard, P.2    Couturier, M.3
  • 45
    • 50449110851 scopus 로고    scopus 로고
    • Exposing plasmids as the Achilles' heel of drug-resistant bacteria
    • Williams J.J., and Hergenrother P.J. Exposing plasmids as the Achilles' heel of drug-resistant bacteria. Curr. Opin. Chem. Biol. 12 (2008) 389-399
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 389-399
    • Williams, J.J.1    Hergenrother, P.J.2
  • 46
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
    • Wright P.E., and Dyson H.J. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293 (1999) 321-331
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.