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Volumn 146, Issue 1-2, 2004, Pages 217-226

ClpA and ClpX ATPases bind simultaneously to opposite ends of ClpP peptidase to form active hybrid complexes

Author keywords

ATP dependent proteolysis; Chaperone; ClpAP protease; ClpXP protease; Electron microscopy; Hybrid ClpXAP protease

Indexed keywords

ADENOSINE TRIPHOSPHATE; ENDOPEPTIDASE CLP; PROTEIN SUBUNIT;

EID: 1642369829     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsb.2003.11.023     Document Type: Conference Paper
Times cited : (51)

References (41)
  • 1
    • 0032215219 scopus 로고    scopus 로고
    • At sixes and sevens: Characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease
    • Beuron F., Maurizi M.R., Belnap D.M., Kocsis E., Booy F.P., Kessel M., Steven A.C. At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease. J. Struct. Biol. 123:1998;248-259.
    • (1998) J. Struct. Biol. , vol.123 , pp. 248-259
    • Beuron, F.1    Maurizi, M.R.2    Belnap, D.M.3    Kocsis, E.4    Booy, F.P.5    Kessel, M.6    Steven, A.C.7
  • 2
    • 0037407940 scopus 로고    scopus 로고
    • Energy-dependent degradation: Linkage between ClpX-catalyzed nucleotide hydrolysis and protein-substrate processing
    • Burton R.E., Baker T.A., Sauer R.T. Energy-dependent degradation: linkage between ClpX-catalyzed nucleotide hydrolysis and protein-substrate processing. Protein Sci. 12:2003;893-902.
    • (2003) Protein Sci. , vol.12 , pp. 893-902
    • Burton, R.E.1    Baker, T.A.2    Sauer, R.T.3
  • 3
    • 0037013955 scopus 로고    scopus 로고
    • Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes
    • Cascio P., Call M., Petre B.M., Walz T., Goldberg A.L. Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes. EMBO J. 21:2002;2636-2645.
    • (2002) EMBO J. , vol.21 , pp. 2636-2645
    • Cascio, P.1    Call, M.2    Petre, B.M.3    Walz, T.4    Goldberg, A.L.5
  • 5
    • 0036210995 scopus 로고    scopus 로고
    • ClpS, a substrate modulator of the ClpAP machine
    • Dougan D.A., Reid B.G., Horwich A.L., Bukau B. ClpS, a substrate modulator of the ClpAP machine. Mol. Cell. 9:2002;673-683.
    • (2002) Mol. Cell , vol.9 , pp. 673-683
    • Dougan, D.A.1    Reid, B.G.2    Horwich, A.L.3    Bukau, B.4
  • 7
    • 0037351068 scopus 로고    scopus 로고
    • Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals
    • Flynn J.M., Neher S.B., Kim Y.I., Sauer R.T., Baker T.A. Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals. Mol. Cell. 11:2003;671-683.
    • (2003) Mol. Cell , vol.11 , pp. 671-683
    • Flynn, J.M.1    Neher, S.B.2    Kim, Y.I.3    Sauer, R.T.4    Baker, T.A.5
  • 8
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover J.R., Lindquist S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell. 94:1998;73-82.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 10
    • 0026454716 scopus 로고
    • Regulation by proteolysis: Energy-dependent proteases and their targets
    • Gottesman S., Maurizi M.R. Regulation by proteolysis: energy-dependent proteases and their targets. Microbiol. Rev. 56:1992;592-621.
    • (1992) Microbiol. Rev. , vol.56 , pp. 592-621
    • Gottesman, S.1    Maurizi, M.R.2
  • 12
    • 0030936847 scopus 로고    scopus 로고
    • Protein quality control: Triage by chaperones and proteases
    • Gottesman S., Wickner S., Maurizi M.R. Protein quality control: triage by chaperones and proteases. Genes Dev. 11:1997;815-823.
    • (1997) Genes Dev. , vol.11 , pp. 815-823
    • Gottesman, S.1    Wickner, S.2    Maurizi, M.R.3
  • 13
    • 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., Steven A.C., Maurizi M.R. Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP. J. Biol. Chem. 273:1998;12476-12481.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12476-12481
    • Grimaud, R.1    Kessel, M.2    Beuron, F.3    Steven, A.C.4    Maurizi, M.R.5
  • 14
    • 0037195418 scopus 로고    scopus 로고
    • Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease
    • Guo F., Maurizi M.R., Esser L., Xia D. Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease. J. Biol. Chem. 277:2002;46743-46752.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46743-46752
    • Guo, F.1    Maurizi, M.R.2    Esser, L.3    Xia, D.4
  • 15
    • 0034255124 scopus 로고    scopus 로고
    • Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP
    • Hoskins J.R., Singh S.K., Maurizi M.R., Wickner S. Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP. Proc. Natl. Acad. Sci. USA. 97:2000;8892-8897.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8892-8897
    • Hoskins, J.R.1    Singh, S.K.2    Maurizi, M.R.3    Wickner, S.4
  • 17
    • 1242345623 scopus 로고    scopus 로고
    • The N-terminal substrate-binding domain of ClpA unfoldase is highly mobile and extends axially from the distal surface of ClpAP complexes
    • Ishikawa T., Maurizi M.R., Steven A.C. The N-terminal substrate-binding domain of ClpA unfoldase is highly mobile and extends axially from the distal surface of ClpAP complexes. J. Struct. Biol. 146:2004;180-188.
    • (2004) J. Struct. Biol. , vol.146 , pp. 180-188
    • Ishikawa, T.1    Maurizi, M.R.2    Steven, A.C.3
  • 18
    • 0029126356 scopus 로고
    • Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26S proteasome
    • Kessel M., Maurizi M.R., Kim B., Kocsis E., Trus B.L., Singh S.K., Steven A.C. Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26S proteasome. J. Mol. Biol. 250:1995;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
  • 20
    • 0029360470 scopus 로고
    • Improved methods for determination of rotational symmetries in macromolecules
    • Kocsis E., Cerritelli M.E., Trus B.L., Cheng N., Steven A.C. Improved methods for determination of rotational symmetries in macromolecules. Ultramicroscopy. 60:1995;219-228.
    • (1995) Ultramicroscopy , vol.60 , pp. 219-228
    • Kocsis, E.1    Cerritelli, M.E.2    Trus, B.L.3    Cheng, N.4    Steven, A.C.5
  • 21
    • 0025148583 scopus 로고
    • The ClpP component of Clp protease is the sigma 32-dependent heat shock protein F21.5
    • Kroh H.E., Simon L.D. The ClpP component of Clp protease is the sigma 32-dependent heat shock protein F21.5. J. Bacteriol. 172:1990;6026-6034.
    • (1990) J. Bacteriol. , vol.172 , pp. 6026-6034
    • Kroh, H.E.1    Simon, L.D.2
  • 22
    • 0031457264 scopus 로고    scopus 로고
    • PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits
    • Levchenko I., Smith C.K., Walsh N.P., Sauer R.T., Baker T.A. PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits. Cell. 91:1997;939-947.
    • (1997) Cell , vol.91 , pp. 939-947
    • Levchenko, I.1    Smith, C.K.2    Walsh, N.P.3    Sauer, R.T.4    Baker, T.A.5
  • 23
    • 0020490602 scopus 로고
    • Quantitation of aromatic residues in proteins: Model compounds for second-derivative spectroscopy
    • Levine R.L., Federici M.M. Quantitation of aromatic residues in proteins: model compounds for second-derivative spectroscopy. Biochemistry. 21:1982;2600-2606.
    • (1982) Biochemistry , vol.21 , pp. 2600-2606
    • Levine, R.L.1    Federici, M.M.2
  • 24
    • 0028363358 scopus 로고
    • Pattern recognition and classification of images of biological macromolecules using artificial neural networks
    • Marabini R., Carazo J.M. Pattern recognition and classification of images of biological macromolecules using artificial neural networks. Biophys. J. 66:1994;1804-1814.
    • (1994) Biophys. J. , vol.66 , pp. 1804-1814
    • Marabini, R.1    Carazo, J.M.2
  • 26
    • 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. Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and clpP. Biochemistry. 37:1998;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
  • 27
    • 0028674499 scopus 로고
    • Endopeptidase Clp: ATP-dependent Clp protease from Escherichia coli
    • Maurizi M.R., Thompson M.W., Singh S.K., Kim S.H. Endopeptidase Clp: ATP-dependent Clp protease from Escherichia coli. Methods Enzymol. 244:1994;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
  • 28
    • 0037705402 scopus 로고    scopus 로고
    • Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity
    • Mogk A., Schlieker C., Strub C., Rist W., Weibezahn J., Bukau B. Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity. J. Biol. Chem. 278:2003;17615-17624.
    • (2003) J. Biol. Chem. , vol.278 , pp. 17615-17624
    • Mogk, A.1    Schlieker, C.2    Strub, C.3    Rist, W.4    Weibezahn, J.5    Bukau, B.6
  • 29
    • 0037119954 scopus 로고    scopus 로고
    • Alternating translocation of protein substrates from both ends of ClpXP protease
    • Ortega J., Lee H.S., Maurizi M.R., Steven A.C. Alternating translocation of protein substrates from both ends of ClpXP protease. EMBO J. 21:2002;4938-4949.
    • (2002) EMBO J. , vol.21 , pp. 4938-4949
    • Ortega, J.1    Lee, H.S.2    Maurizi, M.R.3    Steven, A.C.4
  • 30
    • 0034502532 scopus 로고    scopus 로고
    • Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP
    • Ortega J., Singh S.K., Ishikawa T., Maurizi M.R., Steven A.C. Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP. Mol. Cell. 6:2000;1515-1521.
    • (2000) Mol. Cell , vol.6 , pp. 1515-1521
    • Ortega, J.1    Singh, S.K.2    Ishikawa, T.3    Maurizi, M.R.4    Steven, A.C.5
  • 31
    • 0033516473 scopus 로고    scopus 로고
    • Concurrent chaperone and protease activities of ClpAP and the requirement for the N-terminal ClpA ATP binding site for chaperone activity
    • Pak M., Hoskins J.R., Singh S.K., Maurizi M.R., Wickner S. Concurrent chaperone and protease activities of ClpAP and the requirement for the N-terminal ClpA ATP binding site for chaperone activity. J. Biol. Chem. 274:1999;19316-19322.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19316-19322
    • Pak, M.1    Hoskins, J.R.2    Singh, S.K.3    Maurizi, M.R.4    Wickner, S.5
  • 32
    • 0030784698 scopus 로고    scopus 로고
    • Use of the green fluorescent protein and its mutants in quantitative fluorescence microscopy
    • Patterson G.H., Knobel S.M., Sharif W.D., Kain S.R., Piston D.W. Use of the green fluorescent protein and its mutants in quantitative fluorescence microscopy. Biophys. J. 73:1997;2782-2790.
    • (1997) Biophys. J. , vol.73 , pp. 2782-2790
    • Patterson, G.H.1    Knobel, S.M.2    Sharif, W.D.3    Kain, S.R.4    Piston, D.W.5
  • 33
    • 0033539690 scopus 로고    scopus 로고
    • ClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease
    • Singh S.K., Guo F., Maurizi M.R. ClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease. Biochemistry. 38:1999;14906-14915.
    • (1999) Biochemistry , vol.38 , pp. 14906-14915
    • Singh, S.K.1    Guo, F.2    Maurizi, M.R.3
  • 34
    • 0035800729 scopus 로고    scopus 로고
    • Functional domains of the ClpA and ClpX molecular chaperones identified by limited proteolysis and deletion analysis
    • Singh S.K., Rozycki J., Ortega J., Ishikawa T., Lo J., Steven A.C., Maurizi M.R. Functional domains of the ClpA and ClpX molecular chaperones identified by limited proteolysis and deletion analysis. J. Biol. Chem. 276:2001;29420-29429.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29420-29429
    • Singh, S.K.1    Rozycki, J.2    Ortega, J.3    Ishikawa, T.4    Lo, J.5    Steven, A.C.6    Maurizi, M.R.7
  • 36
    • 0029975086 scopus 로고    scopus 로고
    • Digital image processing of electron micrographs: The PIC system-III
    • Trus B.L., Kocsis E., Conway J.F., Steven A.C. Digital image processing of electron micrographs: the PIC system-III. J. Struct. Biol. 116:1996;61-67.
    • (1996) J. Struct. Biol. , vol.116 , pp. 61-67
    • Trus, B.L.1    Kocsis, E.2    Conway, J.F.3    Steven, A.C.4
  • 37
    • 0023067967 scopus 로고
    • A new resolution criterion based on spectral signal-to-noise ratios
    • Unser M., Trus B.L., Steven A.C. A new resolution criterion based on spectral signal-to-noise ratios. Ultramicroscopy. 23:1987;39-51.
    • (1987) Ultramicroscopy , vol.23 , pp. 39-51
    • Unser, M.1    Trus, B.L.2    Steven, A.C.3
  • 38
    • 0032469437 scopus 로고    scopus 로고
    • Crystal structure determination of Escherichia coli ClpP starting from an EM-derived mask
    • Wang J., Hartling J.A., Flanagan J.M. Crystal structure determination of Escherichia coli ClpP starting from an EM-derived mask. J. Struct. Biol. 124:1998;151-163.
    • (1998) J. Struct. Biol. , vol.124 , pp. 151-163
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 39
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: Folding, refolding, and degrading proteins
    • Wickner S., Maurizi M.R., Gottesman S. Posttranslational quality control: folding, refolding, and degrading proteins. Science. 286:1999;1888-1893.
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 40
    • 0033214052 scopus 로고    scopus 로고
    • ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli
    • Zolkiewski M. ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli. J. Biol. Chem. 274:1999;28083-28086.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28083-28086
    • Zolkiewski, M.1
  • 41
    • 0034076210 scopus 로고    scopus 로고
    • Dis-assembly lines: The proteasome and related ATPase-assisted proteases
    • Zwickl P., Baumeister W., Steven A. Dis-assembly lines: the proteasome and related ATPase-assisted proteases. Curr. Opin. Struct. Biol. 10:2000;242-250.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 242-250
    • Zwickl, P.1    Baumeister, W.2    Steven, A.3


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