메뉴 건너뛰기




Volumn 48, Issue 1, 2003, Pages 67-76

C-terminal domain mutations in ClpX uncouple substrate binding from an engagement step required for unfolding

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ENDOPEPTIDASE CLPX; HEAT SHOCK PROTEIN; MUTANT PROTEIN; NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 0345269855     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2003.03424.x     Document Type: Article
Times cited : (11)

References (44)
  • 1
    • 0027203762 scopus 로고
    • Division of labor among monomers within the Mu transposase tetramer
    • Baker, T.A., Mizuuchi, M., Savilahti, H., and Mizuuchi, K. (1993) Division of labor among monomers within the Mu transposase tetramer. Cell 74: 723-733.
    • (1993) Cell , vol.74 , pp. 723-733
    • Baker, T.A.1    Mizuuchi, M.2    Savilahti, H.3    Mizuuchi, K.4
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0035875890 scopus 로고    scopus 로고
    • Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine
    • Burton, R.E., Siddiqui, S.M., Kim, Y.I., Baker, T.A., and Sauer, R.T. (2001a) Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine. EMBO J 20: 3092-3100.
    • (2001) EMBO J , vol.20 , pp. 3092-3100
    • Burton, R.E.1    Siddiqui, S.M.2    Kim, Y.I.3    Baker, T.A.4    Sauer, R.T.5
  • 5
    • 0034840284 scopus 로고    scopus 로고
    • ClpX-mediated remodeling of Mu transpososomes: Selective unfolding of subunits destabilizes the entire complex
    • Burton, B.M., Williams, T.L., and Baker, T.A. (2001b) ClpX-mediated remodeling of Mu transpososomes: selective unfolding of subunits destabilizes the entire complex. Mol Cell 8: 449-454.
    • (2001) Mol Cell , vol.8 , pp. 449-454
    • Burton, B.M.1    Williams, T.L.2    Baker, T.A.3
  • 6
    • 0036238432 scopus 로고    scopus 로고
    • Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein
    • Cashikar, A.G., Schirmer, E.C., Hattendorf, D.A., Glover, J.R., Ramakrishnan, M.S., Ware, D.M., and Lindquist, S.L. (2002) Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein. Mol Cell 9: 751-760.
    • (2002) Mol Cell , vol.9 , pp. 751-760
    • Cashikar, A.G.1    Schirmer, E.C.2    Hattendorf, D.A.3    Glover, J.R.4    Ramakrishnan, M.S.5    Ware, D.M.6    Lindquist, S.L.7
  • 7
    • 0032543669 scopus 로고    scopus 로고
    • Molecular chaperones: Clamps for the Clps?
    • Feng, H.P., and Gierasch, L.M. (1998) Molecular chaperones: clamps for the Clps? Curr Biol 8: R464-R467.
    • (1998) Curr Biol , vol.8
    • Feng, H.P.1    Gierasch, L.M.2
  • 8
    • 0033553474 scopus 로고    scopus 로고
    • Recognition, targeting, and hydrolysis of the lambda O replication protein by the ClpP/ClpX protease
    • Gonciarz-Swiatek, M., Wawrzynow, A., Um, S.J., Learn, B.A., McMacken, R., Kelley, W.L., et al. (1999) Recognition, targeting, and hydrolysis of the lambda O replication protein by the ClpP/ClpX protease. J Biol Chem 274: 13999-14005.
    • (1999) J Biol Chem , vol.274 , pp. 13999-14005
    • Gonciarz-Swiatek, M.1    Wawrzynow, A.2    Um, S.J.3    Learn, B.A.4    McMacken, R.5    Kelley, W.L.6
  • 9
    • 0030936847 scopus 로고    scopus 로고
    • Protein quality control: Triage by chaperones and proteases
    • Gottesman, S., Wickner, S., and Maurizi, M.R. (1997a) Protein quality control: triage by chaperones and proteases. Genes Dev 11: 815-823.
    • (1997) Genes Dev , vol.11 , pp. 815-823
    • Gottesman, S.1    Wickner, S.2    Maurizi, M.R.3
  • 10
    • 0030726160 scopus 로고    scopus 로고
    • Regulatory subunits of energy-dependent proteases
    • Gottesman, S., Maurizi, M.R., and Wickner, S. (1997b) 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
  • 11
    • 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., and Sauer, R.T. (1998) The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev 12: 1338-1347.
    • (1998) Genes Dev , vol.12 , pp. 1338-1347
    • Gottesman, S.1    Roche, E.2    Zhou, Y.3    Sauer, R.T.4
  • 12
    • 0030666224 scopus 로고    scopus 로고
    • Crystal structure of the δ' subunit of the clamp-loader complex of E. Coli DNA Polymerase III
    • Guenther, B., Onrust, R., Sali, A., O'Donnell, M., and Kuriyan, J. (1997) Crystal structure of the δ' subunit of the clamp-loader complex of E. Coli DNA Polymerase III. Cell 91: 335-345.
    • (1997) Cell , vol.91 , pp. 335-345
    • Guenther, B.1    Onrust, R.2    Sali, A.3    O'Donnell, M.4    Kuriyan, J.5
  • 13
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K., and Pease, L.R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77: 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 15
    • 0035943342 scopus 로고    scopus 로고
    • Crystal structure of the processivity clamp loader gamma (γ) complex of E. Coli DNA Polymerase III
    • Jeruzalmi, D., O'Donnell, M., and Kuriyan, J. (2001) Crystal structure of the processivity clamp loader gamma (γ) complex of E. Coli DNA Polymerase III. Cell 106: 429-441.
    • (2001) Cell , vol.106 , pp. 429-441
    • Jeruzalmi, D.1    O'Donnell, M.2    Kuriyan, J.3
  • 16
    • 0035116848 scopus 로고    scopus 로고
    • Probing the mechanism of ATP hydrolysis and substrate translocation in the AAA protease FtsH by modelling and mutagenesis
    • Karata, K., Verma, C.S., Wilkinson, A.J., and Ogura, T. (2001) Probing the mechanism of ATP hydrolysis and substrate translocation in the AAA protease FtsH by modelling and mutagenesis. Mol Microbiol 39: 890-903.
    • (2001) Mol Microbiol , vol.39 , pp. 890-903
    • Karata, K.1    Verma, C.S.2    Wilkinson, A.J.3    Ogura, T.4
  • 17
    • 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., and Baker, T.A. (2000) Dynamics of substrate denaturation and translocation by the ClpXP degradation machine. Mol Cell 5: 639-648.
    • (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
  • 18
    • 0035122947 scopus 로고    scopus 로고
    • Molecular determinants of complex formation between Clp/Hsp100 ATPases and the ClpP peptidase
    • Kim, Y.I., Levchenko, I., Fraczkowska, K., Woodruff, R.V., Sauer, R.T., and Baker, T.A. (2001) Molecular determinants of complex formation between Clp/Hsp100 ATPases and the ClpP peptidase. Nat Struct Biol 8: 230-233.
    • (2001) Nat Struct Biol , vol.8 , pp. 230-233
    • Kim, Y.I.1    Levchenko, I.2    Fraczkowska, K.3    Woodruff, R.V.4    Sauer, R.T.5    Baker, T.A.6
  • 19
    • 0344059840 scopus 로고    scopus 로고
    • Cooperative action of Escherichia coli ClpB protein and DnaK chaperone in the activation of a replication initiation protein
    • Konieczny, I., and Liberek, K. (2002) Cooperative action of Escherichia coli ClpB protein and DnaK chaperone in the activation of a replication initiation protein. J Biol Chem 11: 11.
    • (2002) J Biol Chem , vol.11 , pp. 11
    • Konieczny, I.1    Liberek, K.2
  • 20
    • 0028863006 scopus 로고
    • Disassembly of the Mu transposase tetramer by the ClpX chaperone
    • Levchenko, I., Luo, L., and Baker, T.A. (1995) Disassembly of the Mu transposase tetramer by the ClpX chaperone. Genes Dev 9: 2399-2408.
    • (1995) Genes Dev , vol.9 , pp. 2399-2408
    • Levchenko, I.1    Luo, L.2    Baker, T.A.3
  • 21
    • 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., and Baker, T.A. (1997a) PDZ-like domains mediate binding specificity in the Clp/Hsp100 family of chaperones and protease regulatory subunits. Cell 91: 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
  • 22
    • 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., and Baker, T.A. (1997b) ClpX and MuB interact with overlapping regions of Mu transposase: implications for control of the transposition pathway. Genes Dev 11: 1561-1572.
    • (1997) Genes Dev , vol.11 , pp. 1561-1572
    • Levchenko, I.1    Yamauchi, M.2    Baker, T.A.3
  • 23
    • 0034730496 scopus 로고    scopus 로고
    • A specificity-enhancing factor for the ClpXP degradation machine
    • Levchenko, I., Seidel, M., Sauer, R.T., and Baker, T.A. (2000) A specificity-enhancing factor for the ClpXP degradation machine. Science 289: 2354-2356.
    • (2000) Science , vol.289 , pp. 2354-2356
    • Levchenko, I.1    Seidel, M.2    Sauer, R.T.3    Baker, T.A.4
  • 24
    • 0035199034 scopus 로고    scopus 로고
    • AAA proteins: In search of a common molecular basis. International meeting on cellular functions of AAA proteins
    • Maurizi, M.R., and Li, C.C. (2001) AAA proteins: in search of a common molecular basis. International Meeting on Cellular Functions of AAA Proteins. EMBO Rep 2: 980-985.
    • (2001) EMBO Rep , vol.2 , pp. 980-985
    • Maurizi, M.R.1    Li, C.C.2
  • 25
    • 0028359550 scopus 로고
    • A new component of bacteriophage Mu replicative transposition machinery: The Escherichia coli ClpX protein
    • Mhammedi-Alaoui, A., Pato, M., Gama, M.J., and Toussaint, A. (1994) A new component of bacteriophage Mu replicative transposition machinery: the Escherichia coli ClpX protein. Mol Microbiol 11: 1109-1116.
    • (1994) Mol Microbiol , vol.11 , pp. 1109-1116
    • Mhammedi-Alaoui, A.1    Pato, M.2    Gama, M.J.3    Toussaint, A.4
  • 26
    • 0029097732 scopus 로고
    • Disassembly of the bacteriophage Mu transposase for the initiation of Mu DNA replication
    • Nakai, H., and Kruklitis, R. (1995) Disassembly of the bacteriophage Mu transposase for the initiation of Mu DNA replication. J Biol Chem 270: 19591-19598.
    • (1995) J Biol Chem , vol.270 , pp. 19591-19598
    • Nakai, H.1    Kruklitis, R.2
  • 27
    • 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., and Koonin, E.V. (1999) AAA+: a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res 9: 27-43.
    • (1999) Genome Res , vol.9 , pp. 27-43
    • Neuwald, A.F.1    Aravind, L.2    Spouge, J.L.3    Koonin, E.V.4
  • 28
    • 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., and Steven, A.C. (2000) Visualization of substrate binding and translocation by the ATP- dependent protease, ClpXP. Mol Cell 6: 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
  • 29
    • 0030219939 scopus 로고    scopus 로고
    • HSP100/Clp proteins: A common mechanism explains diverse functions
    • Schirmer, E.C., Glover, J.R., Singer, M.A., and Lindquist, S. (1996) HSP100/Clp proteins: a common mechanism explains diverse functions. Trends Biochem Sci 21: 289-296.
    • (1996) Trends Biochem Sci , vol.21 , pp. 289-296
    • Schirmer, E.C.1    Glover, J.R.2    Singer, M.A.3    Lindquist, S.4
  • 30
    • 0034698280 scopus 로고    scopus 로고
    • The HsIU ATPase acts as a molecular chaperone in prevention of aggregation of SuIA, an inhibitor of cell division in Escherichia coli
    • Seonga, I.S., Oha, J.Y., Leeab, J.W., Tanakab, K., and Chunga, C.H. (2000) The HsIU ATPase acts as a molecular chaperone in prevention of aggregation of SuIA, an inhibitor of cell division in Escherichia coli. FEBS Lett 477: 224-229.
    • (2000) FEBS Lett , vol.477 , pp. 224-229
    • Seonga, I.S.1    Oha, J.Y.2    Leeab, J.W.3    Tanakab, K.4    Chunga, C.H.5
  • 31
    • 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., and Maurizi, M.R. (2001) Functional domains of the ClpA and ClpX molecular chaperones identified by limited proteolysis and deletion analysis. J Biol Chem 276: 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
  • 32
    • 0033535955 scopus 로고    scopus 로고
    • Lon and Clp family proteases and chaperones share homologous substrate-recognition domains
    • Smith, C.K., Baker, T.A., and Sauer, R.T. (1999) Lon and Clp family proteases and chaperones share homologous substrate-recognition domains. Proc Natl Acad Sci USA 96: 6678-6682.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6678-6682
    • Smith, C.K.1    Baker, T.A.2    Sauer, R.T.3
  • 34
    • 0033681249 scopus 로고    scopus 로고
    • Crystal and solution structures of an HsIUV protease-chaperone complex
    • Sousa, M.C., Trame, C.B., Tsuruta, H., Wilbanks, S.M., Reddy, V.S., and McKay, D.B. (2000) Crystal and solution structures of an HsIUV protease-chaperone complex. Cell 103: 633-643.
    • (2000) Cell , vol.103 , pp. 633-643
    • Sousa, M.C.1    Trame, C.B.2    Tsuruta, H.3    Wilbanks, S.M.4    Reddy, V.S.5    McKay, D.B.6
  • 36
    • 0035783135 scopus 로고    scopus 로고
    • A corrected quaternary arrangement of the peptidase HsIV and ATPase HsIU in a cocrystal structure
    • Wang, J. (2001) A corrected quaternary arrangement of the peptidase HsIV and ATPase HsIU in a cocrystal structure. J Struct Biol 134: 15-24.
    • (2001) J Struct Biol , vol.134 , pp. 15-24
    • Wang, J.1
  • 37
    • 0035096082 scopus 로고    scopus 로고
    • Crystal structures of the HsIVU peptidase-ATPase complex reveal an ATP- dependent proteolysis mechanism
    • Wang, J., Song, J.J., Franklin, M.C., Kamtekar, S., Im, Y.J., Rho, S.H., et al. (2001) Crystal structures of the HsIVU peptidase-ATPase complex reveal an ATP- dependent proteolysis mechanism. Structure (Camb) 9: 177-184.
    • (2001) Structure (Camb) , vol.9 , pp. 177-184
    • Wang, J.1    Song, J.J.2    Franklin, M.C.3    Kamtekar, S.4    Im, Y.J.5    Rho, S.H.6
  • 38
    • 0029000134 scopus 로고
    • The ClpX heat-shock protein of Escherichia 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., et al. (1995) The ClpX heat-shock protein of Escherichia 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
  • 39
    • 0033517351 scopus 로고    scopus 로고
    • Global unfolding of a substrate protein by the Hsp100 chaperone ClpA
    • Weber-Ban, E.U., Reid, B.G., Miranker, A.D., and Horwich, A.L. (1999) Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature 401: 90-93.
    • (1999) Nature , vol.401 , pp. 90-93
    • Weber-Ban, E.U.1    Reid, B.G.2    Miranker, A.D.3    Horwich, A.L.4
  • 41
    • 0033587680 scopus 로고    scopus 로고
    • Here's the hook: Similar substrate binding sites in the chaperone domains of Clp and Lon
    • Wickner, S., and Maurizi, M.R. (1999) Here's the hook: similar substrate binding sites in the chaperone domains of Clp and Lon. Proc Natl Acad Sci USA 96: 8318-8320.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8318-8320
    • Wickner, S.1    Maurizi, M.R.2
  • 42
    • 0033569428 scopus 로고    scopus 로고
    • Organization and dynamics of the Mu transpososome: Recombination by communication between two active sites
    • Williams, T.L., Jackson, E.L., Carritte, A., and Baker, T.A. (1999) Organization and dynamics of the Mu transpososome: recombination by communication between two active sites. Genes Dev 13: 2725-2737.
    • (1999) Genes Dev , vol.13 , pp. 2725-2737
    • Williams, T.L.1    Jackson, E.L.2    Carritte, A.3    Baker, T.A.4
  • 44
    • 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. (1999) ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli. J Biol Chem 274: 28083-28086.
    • (1999) J Biol Chem , vol.274 , pp. 28083-28086
    • Zolkiewski, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.