메뉴 건너뛰기




Volumn 383, Issue 11, 2002, Pages 1701-1713

In vitro and in vivo stability of the ε2ζ2 protein complex of the broad host-range Streptococcus pyogenes pSM19035 addiction system

Author keywords

Plasmid addiction; Postegregational killing; Protein folding; Protein stability; Protein protein interaction

Indexed keywords

ANTITOXIN; BACTERIAL PROTEIN; BACTERIAL TOXIN; TETRAMER;

EID: 12244282678     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2002.191     Document Type: Article
Times cited : (59)

References (35)
  • 1
    • 0031029481 scopus 로고    scopus 로고
    • Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles
    • Behlke, J. and Ristau, O. (1997). Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles. Biophys. J. 72, 428-434.
    • (1997) Biophys. J. , vol.72 , pp. 428-434
    • Behlke, J.1    Ristau, O.2
  • 2
    • 0032536430 scopus 로고    scopus 로고
    • Analysis of the thermodynamic non-ideality of proteins by sedimentation equilibrium experiments
    • Behlke, J. and Ristau, O. (1998). Analysis of the thermodynamic non-ideality of proteins by sedimentation equilibrium experiments. Biophys. Chem. 70, 133-146.
    • (1998) Biophys. Chem. , vol.70 , pp. 133-146
    • Behlke, J.1    Ristau, O.2
  • 3
    • 0030995661 scopus 로고    scopus 로고
    • Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions
    • Behlke, J., Ristau, O. and Schönfeld, H.-J. (1997). Nucleotide-dependent complex formation between the Escherichia coli chaperonins GroEL and GroES studied under equilibrium conditions. Biochemistry 36, 5149-5156.
    • (1997) Biochemistry , vol.36 , pp. 5149-5156
    • Behlke, J.1    Ristau, O.2    Schönfeld, H.-J.3
  • 4
    • 0035066666 scopus 로고    scopus 로고
    • Regulatory circuits for plasmid survival
    • Bingle, L.E.H. and Thomas, C.M. (2001). Regulatory circuits for plasmid survival. Curr. Opin. Microbiol. 4, 194-200.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 194-200
    • Bingle, L.E.H.1    Thomas, C.M.2
  • 5
    • 0027137890 scopus 로고
    • Characterization of the effectors required for stable inheritance of Streptococcus pyogenes pSM19035-derived plasmids in Bacillus subtilis
    • Ceglowski, P., Boitsov, A., Karamyan, N., Chai, S. and Alonso, J.C. (1993a). Characterization of the effectors required for stable inheritance of Streptococcus pyogenes pSM19035-derived plasmids in Bacillus subtilis. Mol. Gen. Genet. 241, 579-585.
    • (1993) Mol. Gen. Genet. , vol.241 , pp. 579-585
    • Ceglowski, P.1    Boitsov, A.2    Karamyan, N.3    Chai, S.4    Alonso, J.C.5
  • 6
    • 0027771641 scopus 로고
    • Analysis of the stabilization system of the pSM19035-derived plasmid pBT233 in Bacillus subtilis
    • Ceglowski, P., Boitsov, A., Chai, S. and Alonso, J.C. (1993b). Analysis of the stabilization system of the pSM19035-derived plasmid pBT233 in Bacillus subtilis. Gene 136, 1-12.
    • (1993) Gene , vol.136 , pp. 1-12
    • Ceglowski, P.1    Boitsov, A.2    Chai, S.3    Alonso, J.C.4
  • 7
    • 0034705331 scopus 로고    scopus 로고
    • The thermodynamic stability of the proteins of the ccd plasmid addiction system
    • Dao-Thi, M.-H., Messens, J., Wyns, L. and Backmann, J. (2000). The thermodynamic stability of the proteins of the ccd plasmid addiction system. J. Mol. Biol. 299, 1373-1386.
    • (2000) J. Mol. Biol. , vol.299 , pp. 1373-1386
    • Dao-Thi, M.-H.1    Messens, J.2    Wyns, L.3    Backmann, J.4
  • 10
    • 0033859844 scopus 로고    scopus 로고
    • Plasmid copy number control: An ever-growing story
    • del Solar, G. and Espinosa, M. (2000). Plasmid copy number control: an ever-growing story. Mol. Microblol. 37, 492-500.
    • (2000) Mol. Microbiol. , vol.37 , pp. 492-500
    • del Solar, G.1    Espinosa, M.2
  • 11
    • 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
  • 12
    • 0033546274 scopus 로고    scopus 로고
    • The Doc toxin and the Phd antidote proteins of the bacteriophage P1 plasmid addiction system form a heterotrimeric complex
    • Gazit, E. and Sauer, R.T. (1999a). The Doc toxin and the Phd antidote proteins of the bacteriophage P1 plasmid addiction system form a heterotrimeric complex. J. Biol. Chem. 274, 16813-16818.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16813-16818
    • Gazit, E.1    Sauer, R.T.2
  • 13
    • 0033613864 scopus 로고    scopus 로고
    • Stability and DNA binding of the Phd protein of the phage P1 plasmid addiction system
    • Gazit, E. and Sauer, R.T. (1999b). Stability and DNA binding of the Phd protein of the phage P1 plasmid addiction system. J. Biol. Chem. 274, 2652-2657.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2652-2657
    • Gazit, E.1    Sauer, R.T.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
  • 17
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S.C. and von Hippel, P.H. (1989). Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 18
    • 0034511875 scopus 로고    scopus 로고
    • Dynamic localization of bacterial and plasmid chromosomes
    • Hiraga, S. (2000). Dynamic localization of bacterial and plasmid chromosomes. Annu. Rev. Genet. 34, 21-59.
    • (2000) Annu. Rev. Genet. , vol.34 , pp. 21-59
    • Hiraga, S.1
  • 19
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Johnson, W.C., Jr. (1990). Protein secondary structure and circular dichroism: a practical guide. Proteins: Struct. Funct. Genet. 7, 205-214.
    • (1990) Proteins: Struct. Funct. Genet. , vol.7 , pp. 205-214
    • Johnson W.C., Jr.1
  • 20
    • 0031823984 scopus 로고    scopus 로고
    • Selfishness and death: Raison d'être of restriction, recombination and mitochondria
    • Kobayashi, I. (1998). Selfishness and death: raison d'être of restriction, recombination and mitochondria. Trends Genet. 14, 368-374.
    • (1998) Trends Genet. , vol.14 , pp. 368-374
    • Kobayashi, I.1
  • 21
    • 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
  • 22
    • 0029743487 scopus 로고    scopus 로고
    • Autoregulation of the plasmid addiction operon of bacteriophage P1
    • Magnuson, R., Lehnherr, H., Mukhopadhyay, G. and 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, R.1    Lehnherr, H.2    Mukhopadhyay, G.3    Yarmolinsky, M.B.4
  • 23
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B. M. (1968). Solvent content of protein crystals. J. Mol. Biol. 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.M.1
  • 24
    • 0035022716 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of the εζ addiction system encoded by Streptococcus pyogenes plasmid pSM19035
    • Meinhart, A., Alings, C., Sträter, N., Camacho, A.G., Alonso, J.C. and Saenger, W. (2001). Crystallization and preliminary X-ray diffraction studies of the εζ addiction system encoded by Streptococcus pyogenes plasmid pSM19035. Acta Cryst. D57, 745-747.
    • (2001) Acta Cryst. , vol.57 D , pp. 745-747
    • Meinhart, A.1    Alings, C.2    Sträter, N.3    Camacho, A.G.4    Alonso, J.C.5    Saenger, W.6
  • 25
    • 0033401440 scopus 로고    scopus 로고
    • Thermodynamic properties and DNA binding of the parD protein from the broad host-range plasmid RK2/RP4 killing system
    • Oberer, M., Lindner, H., Glatter, O., Kratky, C. and Keller, W. (1999). Thermodynamic properties and DNA binding of the parD protein from the broad host-range plasmid RK2/RP4 killing system. Biol. Chem. 380, 1413-1420.
    • (1999) Biol. Chem. , vol.380 , pp. 1413-1420
    • Oberer, M.1    Lindner, H.2    Glatter, O.3    Kratky, C.4    Keller, W.5
  • 26
    • 0002846347 scopus 로고    scopus 로고
    • Measuring the conformational stability of a protein
    • T.E. Creighton, ed. (Oxford, UK: IRL Press)
    • Pace, C.N. and Scholtz, J.M. (1997). Measuring the conformational stability of a protein. In: Protein Structure: A Practical Approach, T.E. Creighton, ed. (Oxford, UK: IRL Press), pp. 299-321.
    • (1997) Protein Structure: A Practical Approach , pp. 299-321
    • Pace, C.N.1    Scholtz, J.M.2
  • 27
    • 0028341724 scopus 로고
    • A novel site-specific recombinase encoded by the Streptococcus pyogenes plasmid pSM19035
    • Rojo, F. and Alonso, J.C. (1994). A novel site-specific recombinase encoded by the Streptococcus pyogenes plasmid pSM19035. J. Mol. Biol. 238, 159-172.
    • (1994) J. Mol. Biol. , vol.238 , pp. 159-172
    • Rojo, F.1    Alonso, J.C.2
  • 28
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional structure by profile-bound neural networks
    • Rost, B. (1996). PHD: predicting one-dimensional structure by profile-bound neural networks. Methods Enzymol. 266, 525-539.
    • (1996) Methods Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 29
    • 0027169638 scopus 로고
    • Improved prediction of protein secondary structure by use of sequence profiles and neural networks
    • Rost, B. and Sander, C. (1993). Improved prediction of protein secondary structure by use of sequence profiles and neural networks. Proc. Natl. Acad. Sci. USA 90, 7558-7562.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7558-7562
    • Rost, B.1    Sander, C.2
  • 31
    • 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
  • 32
    • 0033083161 scopus 로고    scopus 로고
    • Upheaval in the bacterial nucleoid. An active chromosome segregation mechanism
    • Sharpe, M.E. and Errington, J. (1999). Upheaval in the bacterial nucleoid. An active chromosome segregation mechanism. Trends Genet. 15, 70-74.
    • (1999) Trends Genet. , vol.15 , pp. 70-74
    • Sharpe, M.E.1    Errington, J.2
  • 33
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • Studier, F.W. (1991). Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. J. Mol. Biol. 219, 37-44.
    • (1991) J. Mol. Biol. , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 34
    • 0029861722 scopus 로고    scopus 로고
    • ATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions
    • Van Melderen, L., Dao Thi, M.-H., 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, 27730-27738.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27730-27738
    • Van Melderen, L.1    Dao Thi, M.-H.2    Lecchi, P.3    Gottesman, S.4    Couturier, M.5    Maurizi, M.R.6
  • 35
    • 0004244695 scopus 로고
    • Binding and Linkage
    • (Mill Valley, USA: University Science Books)
    • Wyman, J. and Gill, S. J. (1990). Binding and Linkage (Mill Valley, USA: University Science Books).
    • (1990)
    • Wyman, J.1    Gill, S.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.