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Volumn 258, Issue 3, 1998, Pages 923-928

Importance of heptameric ring integrity for activity of Escherichia coli ClpP

Author keywords

ATP dependent protease; ClpP; Radiation target analysis

Indexed keywords

BACTERIAL ENZYME; PROTEINASE;

EID: 0032534899     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2580923.x     Document Type: Article
Times cited : (9)

References (31)
  • 1
    • 0026454716 scopus 로고
    • Regulation by proteolysis: Energy-dependent proteases and their targets
    • Gottesman, S. & Maurizi, M. R. (1992) Regulation by proteolysis: energy-dependent proteases and their targets, Microbiol. Rev. 56, 592-621.
    • (1992) Microbiol. Rev. , vol.56 , pp. 592-621
    • Gottesman, S.1    Maurizi, M.R.2
  • 3
    • 0029000134 scopus 로고
    • The ClpX heat-shock protein of E. coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone
    • Wawrzynow, A., Wojtkowiak, D., Marszalek, J., Banecki, B., Jonsen, M., Graves, B., Georgopoulos, C. & Zylicz, M. (1995) The ClpX heat-shock protein of E. coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone, EMBO J. 14, 1867-1877.
    • (1995) EMBO J. , vol.14 , pp. 1867-1877
    • Wawrzynow, A.1    Wojtkowiak, D.2    Marszalek, J.3    Banecki, B.4    Jonsen, M.5    Graves, B.6    Georgopoulos, C.7    Zylicz, M.8
  • 5
    • 0029126356 scopus 로고
    • Homology in structural orgnization between E. coli ClpAP protease and the eukaryotic 26 S proteosome
    • Kessel, M., Maurizi, M. R., Kim, B., Kocsis, E., Trus, B. L., Singh, S. K. & Steven, A. C. (1995) Homology in structural orgnization between E. coli ClpAP protease and the eukaryotic 26 S proteosome, J. Mol. Biol. 250, 587-594.
    • (1995) J. Mol. Biol. , vol.250 , pp. 587-594
    • Kessel, M.1    Maurizi, M.R.2    Kim, B.3    Kocsis, E.4    Trus, B.L.5    Singh, S.K.6    Steven, A.C.7
  • 6
    • 0029147711 scopus 로고
    • Scanning transmission electron microscopy and small-angle scattering provide evidence that native Escherichia coli ClpP is a tetradecamer with an axial pore
    • Flanagan, J. M., Wall, J. S., Capel, M. S., Schneider, D. K. & Shanklin, J. (1995) Scanning transmission electron microscopy and small-angle scattering provide evidence that native Escherichia coli ClpP is a tetradecamer with an axial pore, Biochemistry 34, 10910-10917.
    • (1995) Biochemistry , vol.34 , pp. 10910-10917
    • Flanagan, J.M.1    Wall, J.S.2    Capel, M.S.3    Schneider, D.K.4    Shanklin, J.5
  • 7
    • 0025323156 scopus 로고
    • ClpP represents a unique family of serine proteases
    • Maurizi, M. R., Clark, W. P., Kim, S. H. & Gottesman, S. (1990) ClpP represents a unique family of serine proteases, J. Biol. Chem. 265, 12546-12552.
    • (1990) J. Biol. Chem. , vol.265 , pp. 12546-12552
    • Maurizi, M.R.1    Clark, W.P.2    Kim, S.H.3    Gottesman, S.4
  • 8
    • 0030691115 scopus 로고    scopus 로고
    • The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis
    • Wang, J., Hartling, J. A. & Flanagan, J. M. (1997) The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis, Cell 91, 447-456.
    • (1997) Cell , vol.91 , pp. 447-456
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 9
    • 0025870685 scopus 로고
    • ATP-promoted interaction between ClpA and ClpP in activation of ClpP protease from Eschericia coli
    • Maurizi, M. R. (1991) ATP-promoted interaction between ClpA and ClpP in activation of ClpP protease from Eschericia coli, Biochem. Soc. Trans. 19, 719-723.
    • (1991) Biochem. Soc. Trans. , vol.19 , pp. 719-723
    • Maurizi, M.R.1
  • 10
    • 0032524297 scopus 로고    scopus 로고
    • Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP
    • Grimaud, R., Kessel, M., Beuron, F., Sleven, A. C. & Maurizi, M. R. (1998) Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP, J. Biol. Chem. 273, 12476-12481.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12476-12481
    • Grimaud, R.1    Kessel, M.2    Beuron, F.3    Sleven, A.C.4    Maurizi, M.R.5
  • 11
    • 0024552829 scopus 로고
    • Protease Ti from Escherichia coli requires ATP hydro-lysis for protein breakdown but not for hydrolysis of small peptides
    • Woo, K. M., Chung, W. J., Ha, D. B., Goldberg, A. L. & Chung, C. H. (1989) Protease Ti from Escherichia coli requires ATP hydro-lysis for protein breakdown but not for hydrolysis of small peptides, J. Biol. Chem. 264, 2088-2091.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2088-2091
    • Woo, K.M.1    Chung, W.J.2    Ha, D.B.3    Goldberg, A.L.4    Chung, C.H.5
  • 12
    • 0028305742 scopus 로고
    • Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates
    • Thompson, M. W. & Maurizi, M. R. (1994) Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates, J. Biol. Chem. 269, 18201-18208.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18201-18208
    • Thompson, M.W.1    Maurizi, M.R.2
  • 13
    • 0030726160 scopus 로고    scopus 로고
    • Regulatory subunits of energy-dependent proteases
    • Gottesman, S., Maurizi, M. R. & Wickner, S. (1997) Regulatory subunits of energy-dependent proteases, Cell 91, 435-438.
    • (1997) Cell , vol.91 , pp. 435-438
    • Gottesman, S.1    Maurizi, M.R.2    Wickner, S.3
  • 14
    • 0026601663 scopus 로고
    • Proteases and protein degradation in Escherichia coli
    • Maurizi, M. R. (1992) Proteases and protein degradation in Escherichia coli, Experientia 48, 178-201.
    • (1992) Experientia , vol.48 , pp. 178-201
    • Maurizi, M.R.1
  • 15
    • 0028365133 scopus 로고
    • Processive degradation of proteins by the ATP-dependent ClpP protease from Escherichia coli. Requirement for the multiple array of active sites in ClpP but not ATP hydrolysis
    • Thompson, M. W., Singh, S. K. & Maurizi, M. R. (1994) Processive degradation of proteins by the ATP-dependent ClpP protease from Escherichia coli. Requirement for the multiple array of active sites in ClpP but not ATP hydrolysis, J. Biol. Chem. 269, 18209-18215.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18209-18215
    • Thompson, M.W.1    Singh, S.K.2    Maurizi, M.R.3
  • 16
    • 0023773798 scopus 로고
    • Molecular size determination of enzymes by radiation inactivation
    • Kempner, E. S. (1988) Molecular size determination of enzymes by radiation inactivation, Adv. Enzymol. Relat. Areas Mol. Biol. 61, 107-147.
    • (1988) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.61 , pp. 107-147
    • Kempner, E.S.1
  • 17
    • 0028674499 scopus 로고
    • Endopeptidase Clp: ATP-dependent Clp protease from Escherichia coli
    • Maurizi, M. R., Thompson, M. W., Singh, S. K. & Kim, S. H. (1994) Endopeptidase Clp: ATP-dependent Clp protease from Escherichia coli, Methods Enzymol. 244, 314-331.
    • (1994) Methods Enzymol. , vol.244 , pp. 314-331
    • Maurizi, M.R.1    Thompson, M.W.2    Singh, S.K.3    Kim, S.H.4
  • 18
    • 0018786839 scopus 로고
    • Labeling of proteins by reductive methylation using sodium cyanoborohydride
    • Jentoft, N. & Dearborn, D. G. (1979) Labeling of proteins by reductive methylation using sodium cyanoborohydride, J. Biol. Chem. 254, 4359-4365.
    • (1979) J. Biol. Chem. , vol.254 , pp. 4359-4365
    • Jentoft, N.1    Dearborn, D.G.2
  • 19
    • 0025103048 scopus 로고
    • A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis
    • King, D. S., Fields, C. G. & Fields, G. B. (1990) A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis, Int. J. Pept. Protein Res. 36, 255-266.
    • (1990) Int. J. Pept. Protein Res. , vol.36 , pp. 255-266
    • King, D.S.1    Fields, C.G.2    Fields, G.B.3
  • 20
    • 0028209596 scopus 로고
    • Effect of environmental conditions on radiation target size analyses
    • Kempner, E. S. & Miller J. H. (1994) Effect of environmental conditions on radiation target size analyses, Anal. Biochem. 216, 451-455.
    • (1994) Anal. Biochem. , vol.216 , pp. 451-455
    • Kempner, E.S.1    Miller, J.H.2
  • 21
    • 0022294077 scopus 로고
    • Molecular weight determinations from radiation inactivation
    • Harmon, J. T., Nielsen, T. B. & Kempner, E. S. (1985) Molecular weight determinations from radiation inactivation, Methods Enzymol. 117, 65-94.
    • (1985) Methods Enzymol. , vol.117 , pp. 65-94
    • Harmon, J.T.1    Nielsen, T.B.2    Kempner, E.S.3
  • 22
    • 0023184358 scopus 로고
    • A multiple-component, ATP-dependent protease from Escherichia coli
    • Katayama-Fujimura, Y., Gottesman, S. & Maurizi, M. R. (1987) A multiple-component, ATP-dependent protease from Escherichia coli, J. Biol. Chem. 262, 4477-4485.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4477-4485
    • Katayama-Fujimura, Y.1    Gottesman, S.2    Maurizi, M.R.3
  • 23
    • 0032568504 scopus 로고    scopus 로고
    • Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and ClpP
    • Maurizi, M. R., Singh, S. K., Thompson, M. W., Kessel, M. & Ginsburg, A. (1998) Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and ClpP, Biochemistry 37, 7778-7786.
    • (1998) Biochemistry , vol.37 , pp. 7778-7786
    • Maurizi, M.R.1    Singh, S.K.2    Thompson, M.W.3    Kessel, M.4    Ginsburg, A.5
  • 24
    • 0026503828 scopus 로고
    • The mechanism and functions of ATP-dependent proteases in bacterial and animal cells
    • Goldberg, A. L. (1992) The mechanism and functions of ATP-dependent proteases in bacterial and animal cells, Eur. J. Biochem. 203, 9-23.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 9-23
    • Goldberg, A.L.1
  • 25
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko, A. & Ciechanover, A. (1992) The ubiquitin system for protein degradation, Annu. Rev. Biochem. 61, 761-807.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 26
    • 0031030057 scopus 로고    scopus 로고
    • Processive degradation of proteins and other catalytic properties of the proteosorne from Thermoplasma acidophilum
    • Akopian, T. N., Kisselev, A. F. & Goldberg, A. L. (1997) Processive degradation of proteins and other catalytic properties of the proteosorne from Thermoplasma acidophilum, J. Biol. Chem. 272, 1791-1798.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1791-1798
    • Akopian, T.N.1    Kisselev, A.F.2    Goldberg, A.L.3
  • 27
    • 0031105036 scopus 로고    scopus 로고
    • Protein degradation by the proteosome and detection of its in vivo importance in intracellular protein degradation
    • Goldberg, A. L., Akopian, T. N., Kisselev, A. F. & Lee, D. H. (1997) Protein degradation by the proteosome and detection of its in vivo importance in intracellular protein degradation, Mol. Biol. Rep. 24, 69-75.
    • (1997) Mol. Biol. Rep. , vol.24 , pp. 69-75
    • Goldberg, A.L.1    Akopian, T.N.2    Kisselev, A.F.3    Lee, D.H.4
  • 28
    • 0026040834 scopus 로고
    • Inactivation mechanism of tetrameric beta-galactosidase by gamma rays involves both fragmentation and temperature-dependent denaturation of protomers
    • Potier, M., Thauvette, L., Michaud, L., Giroux, S. & Beauregard, G. (1991) Inactivation mechanism of tetrameric beta-galactosidase by gamma rays involves both fragmentation and temperature-dependent denaturation of protomers, Biochemistry 30, 8151-8157.
    • (1991) Biochemistry , vol.30 , pp. 8151-8157
    • Potier, M.1    Thauvette, L.2    Michaud, L.3    Giroux, S.4    Beauregard, G.5
  • 29
    • 0030057695 scopus 로고    scopus 로고
    • Structure-function relationships of phenylalanine hydroxylase revealed by radiation target analysis
    • Davis, M. D., Parniak, M. A., Kaufman, S. & Kempner, E. (1996) Structure-function relationships of phenylalanine hydroxylase revealed by radiation target analysis, Arch. Biochem. Biophys. 325, 235-241.
    • (1996) Arch. Biochem. Biophys. , vol.325 , pp. 235-241
    • Davis, M.D.1    Parniak, M.A.2    Kaufman, S.3    Kempner, E.4
  • 30
    • 0032522167 scopus 로고    scopus 로고
    • Radiation effects on the native structure of proteins: Fragmentation without dissociation
    • Miller, J. H., Fedoronko, D. A., Mass, B. D., Myint, M. & Kempner, E. S. (1998) Radiation effects on the native structure of proteins: fragmentation without dissociation, Arch. Biochem. Biophys. 352, 281-287.
    • (1998) Arch. Biochem. Biophys. , vol.352 , pp. 281-287
    • Miller, J.H.1    Fedoronko, D.A.2    Mass, B.D.3    Myint, M.4    Kempner, E.S.5
  • 31
    • 0031037146 scopus 로고    scopus 로고
    • The role of phenylalanine in structure-function relationships of phenylalanine hydroxylase revealed by radiation target analysis
    • Davis, M. D., Parniak, M. A., Kaufman, S. & Kempner, E. (1997) The role of phenylalanine in structure-function relationships of phenylalanine hydroxylase revealed by radiation target analysis, Proc. Natl Acad. Sci. USA 94, 491-495.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 491-495
    • Davis, M.D.1    Parniak, M.A.2    Kaufman, S.3    Kempner, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.