메뉴 건너뛰기




Volumn 176, Issue 2, 1999, Pages 279-284

The effect of some antibiotic-resistance-conferring plasmids on the removal of the heat-aggregated proteins from Escherichia coli cells

Author keywords

Antibiotic resistance conferring plasmid; Escherichia coli; Heat aggregated proteins; S fraction

Indexed keywords

AMPICILLIN; BACTERIAL PROTEIN; CHLORAMPHENICOL; CHLORAMPHENICOL ACETYLTRANSFERASE; KANAMYCIN; RNA POLYMERASE; TETRACYCLINE;

EID: 0344731385     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(99)00245-1     Document Type: Article
Times cited : (8)

References (22)
  • 1
    • 0026355680 scopus 로고
    • Response of Escherichia coli cell membranes to induction of λ cI857 prophage by heat shock
    • Kucharczyk K., Laskowska E., Taylor A. Response of Escherichia coli cell membranes to induction of λ cI857 prophage by heat shock. Mol. Microbiol. 5:1991;2935-2945.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2935-2945
    • Kucharczyk, K.1    Laskowska, E.2    Taylor, A.3
  • 2
    • 0025997087 scopus 로고
    • Protein aggregation and inclusion body formation in Escherichia coli rpoH mutant defective in heat-shock protein induction
    • Gragerov A., Martin E.S., Krupenko M.A., Kashlev M.V., Nikiforov V.G. Protein aggregation and inclusion body formation in Escherichia coli rpoH mutant defective in heat-shock protein induction. FEBS Lett. 291:1991;222-224.
    • (1991) FEBS Lett. , vol.291 , pp. 222-224
    • Gragerov, A.1    Martin, E.S.2    Krupenko, M.A.3    Kashlev, M.V.4    Nikiforov, V.G.5
  • 3
    • 0029852402 scopus 로고    scopus 로고
    • Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro
    • Laskowska E., Kuczyńska-Wiśnik D., Skórko-Glonek A., Taylor A. Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro. Mol. Microbiol. 22:1996;555-571.
    • (1996) Mol. Microbiol. , vol.22 , pp. 555-571
    • Laskowska, E.1    Kuczyńska-Wiśnik, D.2    Skórko-Glonek, A.3    Taylor, A.4
  • 4
    • 0345450070 scopus 로고
    • PhD thesis, University of Gdańsk
    • Kucharczyk, K. (1991) PhD thesis, University of Gdańsk.
    • (1991)
    • Kucharczyk, K.1
  • 5
    • 0033063634 scopus 로고    scopus 로고
    • The role of DnaK/DnaJ and GroEL/GroES systems in the removal of endogenous proteins aggregated by heat shock from Escherichia coli cells
    • Kȩdzierska S., Staniszewska M., Wȩgrzyn A., Taylor A. The role of DnaK/DnaJ and GroEL/GroES systems in the removal of endogenous proteins aggregated by heat shock from Escherichia coli cells. FEBS Lett. 446:1999;331-337.
    • (1999) FEBS Lett. , vol.446 , pp. 331-337
    • Kȩdzierska, S.1    Staniszewska, M.2    Wȩgrzyn, A.3    Taylor, A.4
  • 8
    • 0344555088 scopus 로고    scopus 로고
    • Molecular mechanism of heat shock-provoked disassembly of the coliphage λ replication complex
    • Wȩgrzyn A., Herman-Antosiewicz A., Taylor K., Wȩgrzyn G. Molecular mechanism of heat shock-provoked disassembly of the coliphage λ replication complex. J. Bacteriol. 180:1998;2475-2483.
    • (1998) J. Bacteriol. , vol.180 , pp. 2475-2483
    • Wȩgrzyn, A.1    Herman-Antosiewicz, A.2    Taylor, K.3    Wȩgrzyn, G.4
  • 9
    • 0017807890 scopus 로고
    • Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the p15A cryptic miniplasmid
    • Chang A.C.Y., Cohen S.N. Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the p15A cryptic miniplasmid. J. Bacteriol. 134:1978;1141-1156.
    • (1978) J. Bacteriol. , vol.134 , pp. 1141-1156
    • Chang, A.C.Y.1    Cohen, S.N.2
  • 11
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strain: Nucleotide sequence of the M13mm18 and pUC19 vectors
    • Yanisch-Perron C., Vieira J., Messing J. Improved M13 phage cloning vectors and host strain: nucleotide sequence of the M13mm18 and pUC19 vectors. Gene. 33:1985;103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 12
    • 0026460711 scopus 로고
    • Involvement of the Escherichia coli RNA polymerase α subunit in transcriptional activation by the bacteriophage lambda CI and CII proteins
    • Wȩgrzyn G., Glass R.E., Thomas M.S. Involvement of the Escherichia coli RNA polymerase α subunit in transcriptional activation by the bacteriophage lambda CI and CII proteins. Gene. 122:1992;1-7.
    • (1992) Gene , vol.122 , pp. 1-7
    • Wȩgrzyn, G.1    Glass, R.E.2    Thomas, M.S.3
  • 13
    • 84886622040 scopus 로고
    • An efficient and reproducible procedure for the formation of spheroplasts from variously grown Escherichia coli
    • Witholt B., Boekhout M., Broek M., Kingma J., Heerikhuisen H., deLeij L. An efficient and reproducible procedure for the formation of spheroplasts from variously grown Escherichia coli. Anal. Biochem. 74:1976;160-170.
    • (1976) Anal. Biochem. , vol.74 , pp. 160-170
    • Witholt, B.1    Boekhout, M.2    Broek, M.3    Kingma, J.4    Heerikhuisen, H.5    Deleij, L.6
  • 14
    • 0022633653 scopus 로고
    • Isolation of differentiated membrane domains from Escherichia coli and Salmonella typhimurium, including a fraction containing attachment sites between the inner and outer membranes and the murein skeleton of the cell envelope
    • Ishidate K., Creeger E.S., Zrike J., Deb S., Glauner B., McAllister B.J., Rothfield L.I. Isolation of differentiated membrane domains from Escherichia coli and Salmonella typhimurium, including a fraction containing attachment sites between the inner and outer membranes and the murein skeleton of the cell envelope. J. Biol. Chem. 261:1986;428-443.
    • (1986) J. Biol. Chem. , vol.261 , pp. 428-443
    • Ishidate, K.1    Creeger, E.S.2    Zrike, J.3    Deb, S.4    Glauner, B.5    McAllister, B.J.6    Rothfield, L.I.7
  • 15
    • 0039870135 scopus 로고    scopus 로고
    • IbpA and IbpB, the new heat-shock proteins, bind to endogenous Escherichia coli proteins aggregated intracellularly by heat shock
    • Laskowska E., Wawrzynów A., Taylor A. IbpA and IbpB, the new heat-shock proteins, bind to endogenous Escherichia coli proteins aggregated intracellularly by heat shock. Biochimie. 78:1996;117-122.
    • (1996) Biochimie , vol.78 , pp. 117-122
    • Laskowska, E.1    Wawrzynów, A.2    Taylor, A.3
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 84988112567 scopus 로고
    • Long term stability of colours after silver staining
    • Hempelmann E., Kaminsky R. Long term stability of colours after silver staining. Electrophoresis. 7:1986;481.
    • (1986) Electrophoresis , vol.7 , pp. 481
    • Hempelmann, E.1    Kaminsky, R.2
  • 19
    • 0023392871 scopus 로고
    • Fluorescent staining of proteins transferred to nitrocellulose allowing for subsequent probing with antisera
    • Szewczyk B., Summers D.F. Fluorescent staining of proteins transferred to nitrocellulose allowing for subsequent probing with antisera. Anal. Biochem. 164:1987;303-306.
    • (1987) Anal. Biochem. , vol.164 , pp. 303-306
    • Szewczyk, B.1    Summers, D.F.2
  • 20
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow, E. and Lane D. (1988) Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 21
    • 0031860811 scopus 로고    scopus 로고
    • Chaperone coexpression plasmids: Differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of japanese cedar pollen, Cryj2, in Escherichia coli
    • Nishihara K., Kanemori M., Kitagawa M., Yanagi H., Yura T. Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of japanese cedar pollen, Cryj2, in Escherichia coli. Appl. Environ. Microbiol. 64:1998;1694-1699.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1694-1699
    • Nishihara, K.1    Kanemori, M.2    Kitagawa, M.3    Yanagi, H.4    Yura, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.