메뉴 건너뛰기




Volumn 11, Issue 5, 2004, Pages 404-411

Communication between ClpX and ClpP during substrate processing and degradation

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; CLPX PROTEIN, E COLI; ENDOPEPTIDASE CLP; ESCHERICHIA COLI PROTEIN; SERINE PROTEINASE;

EID: 2542443628     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb752     Document Type: Article
Times cited : (116)

References (46)
  • 1
    • 0034885052 scopus 로고    scopus 로고
    • AAA+ superfamily ATPases: Common structure—diverse function. Genes
    • Ogura, T. & Wilkinson, A.J. AAA+ superfamily ATPases: common structure—diverse function. Genes Cells 6, 575-597 (2001).
    • (2001) Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 2
    • 0032483546 scopus 로고    scopus 로고
    • A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3
    • Glickman, M.H. et al. A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Cell 94, 615-623 (1998).
    • (1998) Cell , vol.94 , pp. 615-623
    • Glickman, M.H.1
  • 3
    • 0030936847 scopus 로고    scopus 로고
    • Protein quality control: Triage by chaper- ones and proteases
    • Gottesman, S., Wickner, S. & Maurizi, M.R. Protein quality control: triage by chaper- ones and proteases. Genes Dev. 11, 815-823 (1997).
    • (1997) Genes Dev , vol.11 , pp. 815-823
    • Gottesman, S.1    Wickner, S.2    Maurizi, M.R.3
  • 4
    • 0030726160 scopus 로고    scopus 로고
    • Regulatory subunits of energy-dependent proteases
    • Gottesman, S., Maurizi, M.R. & Wickner, S. Regulatory subunits of energy-dependent proteases. Cell 91, 435-438 (1997).
    • (1997) Cell , vol.91 , pp. 435-438
    • Gottesman, S.1    Maurizi, M.R.2    Wickner, S.3
  • 5
    • 0030925223 scopus 로고    scopus 로고
    • Crystal structure of heat shock locus V (HslV) from Escherichia coli
    • Bochtler, M., Ditzel, L., Groll, M. & Huber, R. Crystal structure of heat shock locus V (HslV) from Escherichia coli. Proc. Natl. Acad. Sci. USA 94, 6070-6074 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6070-6074
    • Bochtler, M.1    Ditzel, L.2    Groll, M.3    Huber, R.4
  • 6
    • 0030897031 scopus 로고    scopus 로고
    • Structure of 20S proteasome from yeast at 2.4 A resolution
    • Groll, M. et al. Structure of 20S proteasome from yeast at 2.4 A resolution. Nature 386, 463-471 (1997).
    • (1997) Nature , vol.386 , pp. 463-471
    • Groll, M.1
  • 7
    • 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. The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis. Cell 91, 447-456 (1997).
    • (1997) Cell , vol.91 , pp. 447-456
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 8
    • 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, 151-163 (1998).
    • (1998) J. Struct. Biol. , vol.124 , pp. 151-163
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 9
    • 0034677361 scopus 로고    scopus 로고
    • The structures of HsIU and the ATP-dependent protease HsIU- HsIV
    • Bochtler, M. et al. The structures of HsIU and the ATP-dependent protease HsIU- HsIV. Nature 403, 800-805 (2000).
    • (2000) Nature , vol.403 , pp. 800-805
    • Bochtler, M.1
  • 10
    • 0033766480 scopus 로고    scopus 로고
    • A gated channel into the proteasome core particle
    • Groll, M. et al. A gated channel into the proteasome core particle. Nat. Struct. Biol. 7, 1062-1067 (2000).
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1062-1067
    • Groll, M.1
  • 11
    • 0033681249 scopus 로고    scopus 로고
    • Crystal and solution structures of an HslUV protease-chaperone complex
    • Sousa, M.C. et al. Crystal and solution structures of an HslUV protease-chaperone complex. Cell 103, 633-643 (2000).
    • (2000) Cell , vol.103 , pp. 633-643
    • Sousa, M.C.1
  • 12
    • 0034597824 scopus 로고    scopus 로고
    • Structural basis for the activation of 20S proteasomes by 11S reg-ulators
    • Whitby, F.G. et al. Structural basis for the activation of 20S proteasomes by 11S reg-ulators. Nature 408, 115-120 (2000).
    • (2000) Nature , vol.408 , pp. 115-120
    • Whitby, F.G.1
  • 13
    • 0035096082 scopus 로고    scopus 로고
    • Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism
    • Wang, J. et al. Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism. Structure 9, 177-184 (2001).
    • (2001) Structure , vol.9 , pp. 177-184
    • Wang, J.1
  • 14
    • 0035211408 scopus 로고    scopus 로고
    • Structure of Haemophilus influenzae HslV protein at 1.9 A resolution, revealing a cation-binding site near the catalytic site
    • Sousa, M.C. & McKay, D.B. Structure of Haemophilus influenzae HslV protein at 1.9 A resolution, revealing a cation-binding site near the catalytic site. Acta Crystallogr. D 57, 1950-1954 (2001).
    • (2001) Acta Crystallogr. D , vol.57 , pp. 1950-1954
    • Sousa, M.C.1    McKay, D.B.2
  • 15
    • 0030666224 scopus 로고    scopus 로고
    • Crystal structure of the 8' subunit of the clamp-loader complex of E. Coli DNA polymerase III
    • Guenther, B., Onrust, R., Sali, A., O'Donnell, M. & Kuriyan, J. Crystal structure of the 8' subunit of the clamp-loader complex of E. coli DNA polymerase III. Cell 91, 335-345 (1997).
    • (1997) Cell , vol.91 , pp. 335-345
    • Guenther, B.1    Onrust, R.2    Sali, A.3    O'donnell, M.4    Kuriyan, J.5
  • 16
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone- like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald, A.F., Aravind, L., Spouge, J.L. & Koonin, E.V. AAA+: a class of chaperone- like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27-43 (1999).
    • (1999) Genome Res , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 17
    • 0035184442 scopus 로고    scopus 로고
    • Nucleotide-dependent conformational changes in a protease-associ- ated ATPase HsIU
    • Wang, J. et al. Nucleotide-dependent conformational changes in a protease-associ- ated ATPase HsIU. Structure 9, 1107-1116 (2001).
    • (2001) Structure , vol.9 , pp. 1107-1116
    • Wang, J.1
  • 18
    • 0036308646 scopus 로고    scopus 로고
    • Crystal structure of HslUV complexed with a vinyl sulfone inhibitor: Corroboration of a proposed mechanism of allosteric activation of HslV by HslU
    • Sousa, M.C., Kessler, B.M., Overkleeft, H.S. & McKay, D.B. Crystal structure of HslUV complexed with a vinyl sulfone inhibitor: corroboration of a proposed mechanism of allosteric activation of HslV by HslU. J. Mol. Biol. 318, 779-785 (2002).
    • (2002) J. Mol. Biol. , vol.318 , pp. 779-785
    • Sousa, M.C.1    Kessler, B.M.2    Overkleeft, H.S.3    McKay, D.B.4
  • 19
    • 0001588962 scopus 로고    scopus 로고
    • Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli
    • Yoo, S.J. et al. Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli. J. Biol. Chem. 271, 14035-14040 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 14035-14040
    • Yoo, S.J.1
  • 20
    • 0030804951 scopus 로고    scopus 로고
    • The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase
    • Seol, J.H. et al. The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase. Eur. J. Biochem. 247, 1143-1150 (1997).
    • (1997) Eur. J. Biochem. , vol.247 , pp. 1143-1150
    • Seol, J.H.1
  • 22
    • 0037135539 scopus 로고    scopus 로고
    • The C-terminal tails of HslU ATPase act as a molecular switch for activation of HslV peptidase
    • Seong, I.S. et al. The C-terminal tails of HslU ATPase act as a molecular switch for activation of HslV peptidase. J. Biol. Chem. 277, 25976-25982 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 25976-25982
    • Seong, I.S.1
  • 23
    • 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, 12476-12481 (1998).
    • (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
  • 24
    • 0032215219 scopus 로고    scopus 로고
    • At sixes and sevens: Characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease
    • Beuron, F. et al. At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease. J. Struct. Biol. 123, 248-259 (1998).
    • (1998) J. Struct. Biol. , vol.123 , pp. 248-259
    • Beuron, F.1
  • 25
    • 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, 1515-1521 (2000).
    • (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
  • 26
    • 0035122947 scopus 로고    scopus 로고
    • Molecular determinants of complex formation between Clp/Hsp100 ATPases and the ClpP peptidase
    • Kim, Y.I. et al. Molecular determinants of complex formation between Clp/Hsp100 ATPases and the ClpP peptidase. Nat. Struct. Biol. 8, 230-233 (2001).
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 230-233
    • Kim, Y.I.1
  • 27
    • 0035800729 scopus 로고    scopus 로고
    • Functional domains of the ClpA and ClpX molecular chaperones identified by limited proteolysis and deletion analysis
    • Singh, S.K. et al. Functional domains of the ClpA and ClpX molecular chaperones identified by limited proteolysis and deletion analysis. J. Biol. Chem. 276, 29420-29429 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 29420-29429
    • Singh, S.K.1
  • 28
    • 0037195418 scopus 로고    scopus 로고
    • Crystal structure of ClpA, an Hsp100 chap- erone and regulator of ClpAP protease
    • Guo, F., Maurizi, M.R., Esser, L. & Xia, D. Crystal structure of ClpA, an Hsp100 chap- erone and regulator of ClpAP protease. J. Biol. Chem. 277, 46743-46752 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 46743-46752
    • Guo, F.1    Maurizi, M.R.2    Esser, L.3    Xia, D.4
  • 29
    • 0348010311 scopus 로고    scopus 로고
    • Crystal structure of ClpX molecular chaperone from Helicobacter pylori
    • Kim, D.Y. & Kim, K.K. Crystal structure of ClpX molecular chaperone from Helicobacter pylori. J. Biol. Chem. 278, 50664-50670 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 50664-50670
    • Kim, D.Y.1    Kim, K.K.2
  • 30
    • 0028365133 scopus 로고
    • Processive degradation of proteins by the ATP-dependent Clp 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. Processive degradation of proteins by the ATP-dependent Clp 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).
    • (1994) J. Biol. Chem. , vol.269 , pp. 18209-18215
    • Thompson, M.W.1    Singh, S.K.2    Maurizi, M.R.3
  • 31
    • 0033638255 scopus 로고    scopus 로고
    • Dynamics of substrate denaturation and translocation by the ClpXP degradation machine
    • Kim, Y.I., Burton, R.E., Burton, B.M., Sauer, R.T. & Baker, T.A. Dynamics of substrate denaturation and translocation by the ClpXP degradation machine. Mol. Cell 5, 639-648 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 639-648
    • Kim, Y.I.1    Burton, R.E.2    Burton, B.M.3    Sauer, R.T.4    Baker, T.A.5
  • 32
    • 0023906054 scopus 로고
    • Protease Ti, a new ATP-depen- dent protease in Escherichia coli, contains protein-activated ATPase and proteolytic functions in distinct subunits
    • Hwang, B.J., Woo, K.M., Goldberg, A.L. & Chung, C.H. Protease Ti, a new ATP-depen- dent protease in Escherichia coli, contains protein-activated ATPase and proteolytic functions in distinct subunits. J. Biol. Chem. 263, 8727-8734 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 8727-8734
    • Hwang, B.J.1    Woo, K.M.2    Goldberg, A.L.3    Chung, C.H.4
  • 33
    • 0032079329 scopus 로고    scopus 로고
    • The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system
    • Gottesman, S., Roche, E., Zhou, Y. & Sauer, R.T. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev. 12, 1338-1347 (1998).
    • (1998) Genes Dev , vol.12 , pp. 1338-1347
    • Gottesman, S.1    Roche, E.2    Zhou, Y.3    Sauer, R.T.4
  • 34
    • 0034254908 scopus 로고    scopus 로고
    • Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP
    • Singh, S.K., Grimaud, R., Hoskins, J.R., Wickner, S. & Maurizi, M.R. Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP. Proc. Natl. Acad. Sci. USA 97, 8898-8903 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8898-8903
    • Singh, S.K.1    Grimaud, R.2    Hoskins, J.R.3    Wickner, S.4    Maurizi, M.R.5
  • 35
    • 0042329502 scopus 로고    scopus 로고
    • Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine
    • Kenniston, J.A., Baker, T.A., Fernandez, J.M. & Sauer, R.T. Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine. Cell 114, 511-520 (2003).
    • (2003) Cell , vol.114 , pp. 511-520
    • Kenniston, J.A.1    Baker, T.A.2    Fernandez, J.M.3    Sauer, R.T.4
  • 36
    • 0036848756 scopus 로고    scopus 로고
    • Characterization of a specificity factor for an AAA+ ATPase. Assembly of SspB dimers with ssrA-tagged proteins and the ClpX hexamer
    • Wah, D.A., Levchenko, I., Baker, T.A. & Sauer, R.T. Characterization of a specificity factor for an AAA+ ATPase. Assembly of SspB dimers with ssrA-tagged proteins and the ClpX hexamer. Chem. Biol. 9, 1237-1245 (2002).
    • (2002) Chem. Biol. , vol.9 , pp. 1237-1245
    • Wah, D.A.1    Levchenko, I.2    Baker, T.A.3    Sauer, R.T.4
  • 37
    • 1242289869 scopus 로고    scopus 로고
    • The N-terminal zinc binding domain of ClpX is a dimerization domain that modulates the chaperone function
    • Wojtyra, U.A., Thibault, G., Tuite, A. & Houry, W.A. The N-terminal zinc binding domain of ClpX is a dimerization domain that modulates the chaperone function. J. Biol. Chem. 278, 48981-48990 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 48981-48990
    • Wojtyra, U.A.1    Thibault, G.2    Tuite, A.3    Houry, W.A.4
  • 38
    • 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, 671-683 (2003).
    • (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
  • 39
    • 0345269855 scopus 로고    scopus 로고
    • C-terminal domain mutations in ClpX uncouple substrate binding from an engagement step required for unfolding
    • Joshi, S.A., Baker, T.A. & Sauer, R.T. C-terminal domain mutations in ClpX uncouple substrate binding from an engagement step required for unfolding. Mol. Microbiol. 48, 67-76 (2003).
    • (2003) Mol. Microbiol. , vol.48 , pp. 67-76
    • Joshi, S.A.1    Baker, T.A.2    Sauer, R.T.3
  • 40
    • 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, 893-902 (2003).
    • (2003) Protein Sci , vol.12 , pp. 893-902
    • Burton, R.E.1    Baker, T.A.2    Sauer, R.T.3
  • 41
    • 0033539690 scopus 로고    scopus 로고
    • ClpA and ClpP remain associated during multi-ple rounds of ATP-dependent protein degradation by ClpAP protease
    • Singh, S.K., Guo, F. & Maurizi, M.R. ClpA and ClpP remain associated during multi-ple rounds of ATP-dependent protein degradation by ClpAP protease. Biochemistry 38, 14906-14915 (1999).
    • (1999) Biochemistry , vol.38 , pp. 14906-14915
    • Singh, S.K.1    Guo, F.2    Maurizi, M.R.3
  • 42
    • 0037119954 scopus 로고    scopus 로고
    • Alternating translocation of pro-tein substrates from both ends of ClpXP protease
    • Ortega, J., Lee, H.S., Maurizi, M.R. & Steven, A.C. Alternating translocation of pro-tein substrates from both ends of ClpXP protease. EMBO J. 21, 4938-4949 (2002).
    • (2002) EMBO J , vol.21 , pp. 4938-4949
    • Ortega, J.1    Lee, H.S.2    Maurizi, M.R.3    Steven, A.C.4
  • 43
    • 0028863006 scopus 로고
    • Disassembly of the Mu transposase tetramer by the ClpX chaperone
    • Levchenko, I., Luo, L. & Baker, T.A. Disassembly of the Mu transposase tetramer by the ClpX chaperone. Genes Dev. 9, 2399-2408 (1995).
    • (1995) Genes Dev , vol.9 , pp. 2399-2408
    • Levchenko, I.1    Luo, L.2    Baker, T.A.3
  • 44
    • 0030908043 scopus 로고    scopus 로고
    • ClpX and MuB interact with overlapping regions of Mu transposase: Implications for control of the transposition pathway
    • Levchenko, I., Yamauchi, M. & Baker, T.A. ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway. Genes Dev. 11, 1561-1572 (1997).
    • (1997) Genes Dev , vol.11 , pp. 1561-1572
    • Levchenko, I.1    Yamauchi, M.2    Baker, T.A.3
  • 45
    • 0003760238 scopus 로고
    • Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems
    • Wiley Classics Library edn, Wiley, New York
    • Segel, I. H. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Wiley Classics Library edn) 72-74 (Wiley, New York, 1993).
    • (1993) , pp. 72-74
    • Segel, I.H.1
  • 46
    • 0028114256 scopus 로고
    • Halothane and cyclopiazonic acid modu-late Ca-ATPase oligomeric state and function in sarcoplasmic reticulum
    • Karon, B.S., Mahaney, J.E. & Thomas, D.D. Halothane and cyclopiazonic acid modu-late Ca-ATPase oligomeric state and function in sarcoplasmic reticulum. Biochemistry 33, 13928-13937 (1994).
    • (1994) Biochemistry , vol.33 , pp. 13928-13937
    • Karon, B.S.1    Mahaney, J.E.2    Thomas, D.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.