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Volumn 15, Issue 6, 2008, Pages 641-650

Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments

Author keywords

[No Author keywords available]

Indexed keywords

ATPASE ASSOCIATED WITH VARIOUS CELLULAR ACTIVITY CHAPERONE; CHAPERONE; HYBRID PROTEIN; PEPTIDE FRAGMENT; POLYPEPTIDE; PROTEIN; PROTEIN CLPB; PROTEIN DNAK;

EID: 44849138934     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1425     Document Type: Article
Times cited : (129)

References (50)
  • 1
    • 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, 1888-1893 (1999).
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 3
    • 33751228400 scopus 로고    scopus 로고
    • ATP-dependent proteases of bacteria: Recognition logic and operating principles
    • Baker, T.A. & Sauer, R.T. ATP-dependent proteases of bacteria: recognition logic and operating principles. Trends Biochem. Sci. 31, 647-653 (2006).
    • (2006) Trends Biochem. Sci , vol.31 , pp. 647-653
    • Baker, T.A.1    Sauer, R.T.2
  • 4
    • 1242283848 scopus 로고    scopus 로고
    • Protein binding and disruption by Clp/Hsp100 chaperones
    • Maurizi, M.R. & Xia, D. Protein binding and disruption by Clp/Hsp100 chaperones. Structure 12, 175-183 (2004).
    • (2004) Structure , vol.12 , pp. 175-183
    • Maurizi, M.R.1    Xia, D.2
  • 5
    • 0025799542 scopus 로고
    • ClpB is the Escherichia coli heat shock protein F84.1
    • Squires, C.L., Pedersen, S., Ross, B.M. & Squires, C. ClpB is the Escherichia coli heat shock protein F84.1. J. Bacteriol. 173, 4254-4262 (1991).
    • (1991) J. Bacteriol , vol.173 , pp. 4254-4262
    • Squires, C.L.1    Pedersen, S.2    Ross, B.M.3    Squires, C.4
  • 6
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • Goloubinoff, P., Mogk, A., Peres Ben Zvi, A., Tomoyasu, T. & Bukau, B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc. Natl. Acad. Sci. USA 96, 13732-13737 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Peres Ben Zvi, A.3    Tomoyasu, T.4    Bukau, B.5
  • 7
    • 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, 28083-28086 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 28083-28086
    • Zolkiewski, M.1
  • 8
    • 0033594880 scopus 로고    scopus 로고
    • Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones
    • Motohashi, K., Watanabe, Y., Yohda, M. & Yoshida, M. Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones. Proc. Natl. Acad. Sci. USA 96, 7184-7189 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7184-7189
    • Motohashi, K.1    Watanabe, Y.2    Yohda, M.3    Yoshida, M.4
  • 9
    • 0025193343 scopus 로고
    • HSP104 required for induced thermotolerance
    • Sanchez, Y. & Lindquist, S.L. HSP104 required for induced thermotolerance. Science 248, 1112-1115 (1990).
    • (1990) Science , vol.248 , pp. 1112-1115
    • Sanchez, Y.1    Lindquist, S.L.2
  • 10
    • 0034119621 scopus 로고    scopus 로고
    • Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis
    • Queitsch, C., Hong, S.W., Vierling, E. & Lindquist, S. Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis. Plant Cell 12, 479-492 (2000).
    • (2000) Plant Cell , vol.12 , pp. 479-492
    • Queitsch, C.1    Hong, S.W.2    Vierling, E.3    Lindquist, S.4
  • 11
    • 0034636040 scopus 로고    scopus 로고
    • Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress
    • Hong, S.W. & Vierling, E. Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress. Proc. Natl. Acad. Sci. USA 97, 4392-4397 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4392-4397
    • Hong, S.W.1    Vierling, E.2
  • 12
    • 1542283751 scopus 로고    scopus 로고
    • Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates
    • Siddiqui, S.M., Sauer, R.T. & Baker, T.A. Role of the processing pore of the ClpX AAA+ ATPase in the recognition and engagement of specific protein substrates. Genes Dev. 18, 369-374 (2004).
    • (2004) Genes Dev , vol.18 , pp. 369-374
    • Siddiqui, S.M.1    Sauer, R.T.2    Baker, T.A.3
  • 13
    • 8844251486 scopus 로고    scopus 로고
    • Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB
    • Weibezahn, J. et al. Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell 119, 653-665 (2004).
    • (2004) Cell , vol.119 , pp. 653-665
    • Weibezahn, J.1
  • 14
    • 3142657524 scopus 로고    scopus 로고
    • Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104
    • Lum, R., Tkach, J.M., Vierling, E. & Glover, J.R. Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. J. Biol. Chem. 279, 29139-29146 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 29139-29146
    • Lum, R.1    Tkach, J.M.2    Vierling, E.3    Glover, J.R.4
  • 15
    • 0348010363 scopus 로고    scopus 로고
    • Conserved pore residues in the AAA protease FtsH are important for proteolysis and its coupling to ATP hydrolysis
    • Yamada-Inagawa, T., Okuno, T., Karata, K., Yamanaka, K. & Ogura, T. Conserved pore residues in the AAA protease FtsH are important for proteolysis and its coupling to ATP hydrolysis. J. Biol. Chem. 278, 50182-50187 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 50182-50187
    • Yamada-Inagawa, T.1    Okuno, T.2    Karata, K.3    Yamanaka, K.4    Ogura, T.5
  • 16
    • 21244480104 scopus 로고    scopus 로고
    • Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation
    • Hinnerwisch, J., Fenton, W.A., Furtak, K.J., Farr, G.W. & Horwich, A.L. Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation. Cell 121, 1029-1041 (2005).
    • (2005) Cell , vol.121 , pp. 1029-1041
    • Hinnerwisch, J.1    Fenton, W.A.2    Furtak, K.J.3    Farr, G.W.4    Horwich, A.L.5
  • 17
    • 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, 673-683 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 673-683
    • Dougan, D.A.1    Reid, B.G.2    Horwich, A.L.3    Bukau, B.4
  • 18
    • 33645745841 scopus 로고    scopus 로고
    • Cyanobacterial ClpC/HSP100 protein displays intrinsic chaperone activity
    • Andersson, F.I. et al. Cyanobacterial ClpC/HSP100 protein displays intrinsic chaperone activity. J. Biol. Chem. 281, 5468-5475 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 5468-5475
    • Andersson, F.I.1
  • 19
    • 0029785532 scopus 로고    scopus 로고
    • The heat shock protein ClpB mediates the development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942
    • Eriksson, M.J. & Clarke, A.K. The heat shock protein ClpB mediates the development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942. J. Bacteriol. 178, 4839-4846 (1996).
    • (1996) J. Bacteriol , vol.178 , pp. 4839-4846
    • Eriksson, M.J.1    Clarke, A.K.2
  • 20
    • 0033573135 scopus 로고    scopus 로고
    • Identification of thermolabile E. coli proteins: Prevention and reversion of aggregation by DnaK and ClpB
    • Mogk, A. et al. Identification of thermolabile E. coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 18, 6934-6949 (1999).
    • (1999) EMBO J , vol.18 , pp. 6934-6949
    • Mogk, A.1
  • 21
    • 0035029482 scopus 로고    scopus 로고
    • Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol
    • Tomoyasu, T., Mogk, A., Langen, H., Goloubinoff, P. & Bukau, B. Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol. Mol. Microbiol. 40, 397-413 (2001).
    • (2001) Mol. Microbiol , vol.40 , pp. 397-413
    • Tomoyasu, T.1    Mogk, A.2    Langen, H.3    Goloubinoff, P.4    Bukau, B.5
  • 22
    • 0037427448 scopus 로고    scopus 로고
    • Evolutionary stabilization of the gene-3-protein of phage fd reveals the principles that govern the thermodynamic stability of two-domain proteins
    • Martin, A. & Schmid, F.X. Evolutionary stabilization of the gene-3-protein of phage fd reveals the principles that govern the thermodynamic stability of two-domain proteins. J. Mol. Biol. 328, 863-875 (2003).
    • (2003) J. Mol. Biol , vol.328 , pp. 863-875
    • Martin, A.1    Schmid, F.X.2
  • 23
    • 0022429145 scopus 로고
    • Thermodynamic study of domain organization in troponin C and calmodulin
    • Tsalkova, T.N. & Privalov, P.L. Thermodynamic study of domain organization in troponin C and calmodulin. J. Mol. Biol. 181, 533-544 (1985).
    • (1985) J. Mol. Biol , vol.181 , pp. 533-544
    • Tsalkova, T.N.1    Privalov, P.L.2
  • 24
    • 0033569476 scopus 로고    scopus 로고
    • 2+-binding βγ-crystallin homolog protein S from Myxococcus xanthus: Intrinsic stability and mutual stabilization of domains
    • 2+-binding βγ-crystallin homolog protein S from Myxococcus xanthus: intrinsic stability and mutual stabilization of domains. J. Mol. Biol. 293, 117-124 (1999).
    • (1999) J. Mol. Biol , vol.293 , pp. 117-124
    • Wenk, M.1    Jaenicke, R.2
  • 25
    • 0028942167 scopus 로고
    • Cold denaturation of yeast phosphoglycerate kinase: Which domain is more stable?
    • Gast, K. et al. Cold denaturation of yeast phosphoglycerate kinase: which domain is more stable? FEBS Lett. 358, 247-250 (1995).
    • (1995) FEBS Lett , vol.358 , pp. 247-250
    • Gast, K.1
  • 26
    • 0037308999 scopus 로고    scopus 로고
    • Protein unfolding-an important process in vivo?
    • Matouschek, A. Protein unfolding-an important process in vivo? Curr. Opin. Struct. Biol. 13, 98-109 (2003).
    • (2003) Curr. Opin. Struct. Biol , vol.13 , pp. 98-109
    • Matouschek, A.1
  • 27
    • 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. & Horwich, A.L. Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature 401, 90-93 (1999).
    • (1999) Nature , vol.401 , pp. 90-93
    • Weber-Ban, E.U.1    Reid, B.G.2    Miranker, A.D.3    Horwich, A.L.4
  • 28
    • 0142227208 scopus 로고    scopus 로고
    • The structure of ClpB. A molecular chaperone that rescues proteins from an aggregated state
    • Lee, S. et al. The structure of ClpB. A molecular chaperone that rescues proteins from an aggregated state. Cell 115, 229-240 (2003).
    • (2003) Cell , vol.115 , pp. 229-240
    • Lee, S.1
  • 29
    • 33846188909 scopus 로고    scopus 로고
    • Visualizing the ATPase cycle in a protein disaggregating machine: Structural basis for substrate binding by ClpB
    • Lee, S., Choi, J.M. & Tsai, F.T. Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB. Mol. Cell 25, 261-271 (2007).
    • (2007) Mol. Cell , vol.25 , pp. 261-271
    • Lee, S.1    Choi, J.M.2    Tsai, F.T.3
  • 30
    • 0028951190 scopus 로고
    • Methotrexate inhibits proteolysis of dihydrofolate reductase by the N-end rule pathway
    • Johnston, J.A., Johnson, E.S., Waller, P.R. & Varshavsky, A. Methotrexate inhibits proteolysis of dihydrofolate reductase by the N-end rule pathway. J. Biol. Chem. 270, 8172-8178 (1995).
    • (1995) J. Biol. Chem , vol.270 , pp. 8172-8178
    • Johnston, J.A.1    Johnson, E.S.2    Waller, P.R.3    Varshavsky, A.4
  • 31
    • 0035266072 scopus 로고    scopus 로고
    • ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
    • Lee, C., Schwartz, M.P., Prakash, S., Iwakura, M. & Matouschek, A. ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal. Mol. Cell 7, 627-637 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 627-637
    • Lee, C.1    Schwartz, M.P.2    Prakash, S.3    Iwakura, M.4    Matouschek, A.5
  • 32
    • 27744581873 scopus 로고    scopus 로고
    • Ligand binding modulates the mechanical stability of dihydrofolate reductase
    • Ainavarapu, S.R., Li, L., Badilla, C.L. & Fernandez, J.M. Ligand binding modulates the mechanical stability of dihydrofolate reductase. Biophys. J. 89, 3337-3344 (2005).
    • (2005) Biophys. J , vol.89 , pp. 3337-3344
    • Ainavarapu, S.R.1    Li, L.2    Badilla, C.L.3    Fernandez, J.M.4
  • 33
    • 0042858475 scopus 로고    scopus 로고
    • Characterization of a trap mutant of the AAA+ chaperone ClpB
    • Weibezahn, J., Schlieker, C., Bukau, B. & Mogk, A. Characterization of a trap mutant of the AAA+ chaperone ClpB. J. Biol. Chem. 278, 32608-32617 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 32608-32617
    • Weibezahn, J.1    Schlieker, C.2    Bukau, B.3    Mogk, A.4
  • 34
    • 0031030242 scopus 로고    scopus 로고
    • Biochemical characterization of a molecular switch involving the heat shock protein ClpC, which controls the activity of ComK, the competence transcription factor of Bacillus subtilis
    • Turgay, K., Hamoen, L.W., Venema, G. & Dubnau, D. Biochemical characterization of a molecular switch involving the heat shock protein ClpC, which controls the activity of ComK, the competence transcription factor of Bacillus subtilis. Genes Dev. 11, 119-128 (1997).
    • (1997) Genes Dev , vol.11 , pp. 119-128
    • Turgay, K.1    Hamoen, L.W.2    Venema, G.3    Dubnau, D.4
  • 35
    • 0032538886 scopus 로고    scopus 로고
    • Competence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor
    • Turgay, K., Hahn, J., Burghoorn, J. & Dubnau, D. Competence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor. EMBO J. 17, 6730-6738 (1998).
    • (1998) EMBO J , vol.17 , pp. 6730-6738
    • Turgay, K.1    Hahn, J.2    Burghoorn, J.3    Dubnau, D.4
  • 37
    • 37449008520 scopus 로고    scopus 로고
    • Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104
    • Wendler, P. et al. Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104. Cell 131, 1366-1377 (2007).
    • (2007) Cell , vol.131 , pp. 1366-1377
    • Wendler, P.1
  • 38
    • 0037143697 scopus 로고    scopus 로고
    • ClpAP and ClpXP degrade proteins with tags located in the interior of the primary sequence
    • Hoskins, J.R., Yanagihara, K., Mizuuchi, K. & Wickner, S. ClpAP and ClpXP degrade proteins with tags located in the interior of the primary sequence. Proc. Natl. Acad. Sci. USA 99, 11037-11042 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11037-11042
    • Hoskins, J.R.1    Yanagihara, K.2    Mizuuchi, K.3    Wickner, S.4
  • 39
    • 0037144567 scopus 로고    scopus 로고
    • Concurrent translocation of multiple polypeptide chains through the proteasomal degradation channel
    • Lee, C., Prakash, S. & Matouschek, A. Concurrent translocation of multiple polypeptide chains through the proteasomal degradation channel. J. Biol. Chem. 277, 34760-34765 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 34760-34765
    • Lee, C.1    Prakash, S.2    Matouschek, A.3
  • 40
    • 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. & Sauer, R.T. Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine. EMBO J. 20, 3092-3100 (2001).
    • (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
  • 41
    • 33746786326 scopus 로고    scopus 로고
    • Proteasome-mediated protein processing by bidirectional degradation initiated from an internal site
    • Piwko, W. & Jentsch, S. Proteasome-mediated protein processing by bidirectional degradation initiated from an internal site. Nat. Struct. Mol. Biol. 13, 691-697 (2006).
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 691-697
    • Piwko, W.1    Jentsch, S.2
  • 42
    • 0034268493 scopus 로고    scopus 로고
    • Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing
    • Hoppe, T. et al. Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Cell 102, 577-586 (2000).
    • (2000) Cell , vol.102 , pp. 577-586
    • Hoppe, T.1
  • 43
    • 28544434064 scopus 로고    scopus 로고
    • A conserved processing mechanism regulates the activity of transcription factors Cubitus interruptus and NF-κB
    • Tian, L., Holmgren, R.A. & Matouschek, A. A conserved processing mechanism regulates the activity of transcription factors Cubitus interruptus and NF-κB. Nat. Struct. Mol. Biol. 12, 1045-1053 (2005).
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 1045-1053
    • Tian, L.1    Holmgren, R.A.2    Matouschek, A.3
  • 44
    • 0032954038 scopus 로고    scopus 로고
    • Structural motifs involved in ubiquitin-mediated processing of the NF-κB precursor p105: Roles of the glycine-rich region and a downstream ubiquitination domain
    • Orian, A. et al. Structural motifs involved in ubiquitin-mediated processing of the NF-κB precursor p105: roles of the glycine-rich region and a downstream ubiquitination domain. Mol. Cell. Biol. 19, 3664-3673 (1999).
    • (1999) Mol. Cell. Biol , vol.19 , pp. 3664-3673
    • Orian, A.1
  • 45
    • 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, 14906-14915 (1999).
    • (1999) Biochemistry , vol.38 , pp. 14906-14915
    • Singh, S.K.1    Guo, F.2    Maurizi, M.R.3
  • 46
    • 34249734248 scopus 로고    scopus 로고
    • Assembly pathway of an AAA+ protein: Tracking ClpA and ClpAP complex formation in real time
    • Kress, W., Mutschler, H. & Weber-Ban, E. Assembly pathway of an AAA+ protein: tracking ClpA and ClpAP complex formation in real time. Biochemistry 46, 6183-6193 (2007).
    • (2007) Biochemistry , vol.46 , pp. 6183-6193
    • Kress, W.1    Mutschler, H.2    Weber-Ban, E.3
  • 47
    • 7244247277 scopus 로고    scopus 로고
    • Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation
    • Zietkiewicz, S., Krzewska, J. & Liberek, K. Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation. J. Biol. Chem. 279, 44376-44383 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 44376-44383
    • Zietkiewicz, S.1    Krzewska, J.2    Liberek, K.3
  • 48
    • 33646354916 scopus 로고    scopus 로고
    • Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation
    • Zietkiewicz, S., Lewandowska, A., Stocki, P. & Liberek, K. Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation. J. Biol. Chem. 281, 7022-7029 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 7022-7029
    • Zietkiewicz, S.1    Lewandowska, A.2    Stocki, P.3    Liberek, K.4
  • 49
    • 18244398660 scopus 로고    scopus 로고
    • Localization of chaperones DnaK and GroEL in bacterial inclusion bodies
    • Carrio, M.M. & Villaverde, A. Localization of chaperones DnaK and GroEL in bacterial inclusion bodies. J. Bacteriol. 187, 3599-3601 (2005).
    • (2005) J. Bacteriol , vol.187 , pp. 3599-3601
    • Carrio, M.M.1    Villaverde, A.2
  • 50
    • 33645741669 scopus 로고    scopus 로고
    • Adaptor protein controlled oligomerization activates the AAA+ protein ClpC
    • Kirstein, J. et al. Adaptor protein controlled oligomerization activates the AAA+ protein ClpC. EMBO J. 25, 1481-1491 (2006).
    • (2006) EMBO J , vol.25 , pp. 1481-1491
    • Kirstein, J.1


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