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Volumn 8, Issue 5, 2013, Pages

Aggregate-Reactivation Activity of the Molecular Chaperone ClpB from Ehrlichia chaffeensis

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CASEIN; CHAPERONE; FIREFLY LUCIFERASE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; MESSENGER RNA; OLIGOMER; POLYLYSINE; PROTEIN CLPB;

EID: 84877158178     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0062454     Document Type: Article
Times cited : (29)

References (62)
  • 2
    • 0037240533 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis: a prototypical emerging pathogen
    • Paddock CD, Childs JE, (2003) Ehrlichia chaffeensis: a prototypical emerging pathogen. Clin Microbiol Rev 16: 37-64.
    • (2003) Clin Microbiol Rev , vol.16 , pp. 37-64
    • Paddock, C.D.1    Childs, J.E.2
  • 3
    • 0035867078 scopus 로고    scopus 로고
    • Ticks and tickborne bacterial diseases in humans: an emerging infectious threat
    • Parola P, Raoult D, (2001) Ticks and tickborne bacterial diseases in humans: an emerging infectious threat. Clin Infect Dis 32: 897-928.
    • (2001) Clin Infect Dis , vol.32 , pp. 897-928
    • Parola, P.1    Raoult, D.2
  • 4
    • 0026902092 scopus 로고
    • Susceptibility of dogs to infection with Ehrlichia chaffeensis, causative agent of human ehrlichiosis
    • Dawson JE, Ewing SA, (1992) Susceptibility of dogs to infection with Ehrlichia chaffeensis, causative agent of human ehrlichiosis. Am J Vet Res 53: 1322-1327.
    • (1992) Am J Vet Res , vol.53 , pp. 1322-1327
    • Dawson, J.E.1    Ewing, S.A.2
  • 5
    • 0029869430 scopus 로고    scopus 로고
    • Ehrlichia-like 16s rDNA sequence from wild white-tailed deer (Odocoileus virginianus)
    • Dawson JE, Warner CK, Baker V, Ewing SA, Stallknecht DE, et al. (1996) Ehrlichia-like 16s rDNA sequence from wild white-tailed deer (Odocoileus virginianus). J Parasitol 82: 52-58.
    • (1996) J Parasitol , vol.82 , pp. 52-58
    • Dawson, J.E.1    Warner, C.K.2    Baker, V.3    Ewing, S.A.4    Stallknecht, D.E.5
  • 6
    • 0029030449 scopus 로고
    • Isolation and characteriztion of a new strain of Ehrlichia chaffeensis from a patient with near-fatal monocytic ehrlichiosis
    • Dumler JS, Chen S-M, Asanovich k, Trigiani E, Popov VL, et al. (1995) Isolation and characteriztion of a new strain of Ehrlichia chaffeensis from a patient with near-fatal monocytic ehrlichiosis. J Clin Microbiol 33: 1704-1711.
    • (1995) J Clin Microbiol , vol.33 , pp. 1704-1711
    • Dumler, J.S.1    Chen, S.-M.2    Asanovich, K.3    Trigiani, E.4    Popov, V.L.5
  • 7
    • 0025789921 scopus 로고
    • Ehrlichia chaffeensis, a new species associated with human ehrlichiosis
    • Anderson BE, Dawson JE, Jones DC, Wilson KH, (1991) Ehrlichia chaffeensis, a new species associated with human ehrlichiosis. J Clin Microbiol 29: 2838-2842.
    • (1991) J Clin Microbiol , vol.29 , pp. 2838-2842
    • Anderson, B.E.1    Dawson, J.E.2    Jones, D.C.3    Wilson, K.H.4
  • 8
    • 54949092874 scopus 로고    scopus 로고
    • Emerging and re-emerging tick-transmitted rickettsial and ehrlichial infections
    • Walker DH, Paddock CD, Dumler JS, (2008) Emerging and re-emerging tick-transmitted rickettsial and ehrlichial infections. Med Clin North Am 92: 1345-1361.
    • (2008) Med Clin North Am , vol.92 , pp. 1345-1361
    • Walker, D.H.1    Paddock, C.D.2    Dumler, J.S.3
  • 9
    • 0029679613 scopus 로고    scopus 로고
    • Emergence of the ehrlichiosis as human health problems
    • Walker DH, Dumler JS, (1996) Emergence of the ehrlichiosis as human health problems. Emerg Infect Dis 2: 18-29.
    • (1996) Emerg Infect Dis , vol.2 , pp. 18-29
    • Walker, D.H.1    Dumler, J.S.2
  • 10
    • 0031957399 scopus 로고    scopus 로고
    • Human ehrlichioses: newly recognized infections transmitted by ticks
    • Dumler JS, Bakken JS, (1998) Human ehrlichioses: newly recognized infections transmitted by ticks. Annu Rev Med 49: 201-213.
    • (1998) Annu Rev Med , vol.49 , pp. 201-213
    • Dumler, J.S.1    Bakken, J.S.2
  • 11
    • 0028788919 scopus 로고
    • Ultrastructural variation of cultured Ehrlichia chaffeensis
    • Popov VL, Chen SM, Feng HM, Walker DH, (1995) Ultrastructural variation of cultured Ehrlichia chaffeensis. J Med Microbiol 43: 411-421.
    • (1995) J Med Microbiol , vol.43 , pp. 411-421
    • Popov, V.L.1    Chen, S.M.2    Feng, H.M.3    Walker, D.H.4
  • 12
    • 0031015273 scopus 로고    scopus 로고
    • Ultrastructural and antigenic characterization of a granulocytic ehrlichiosis agent directly isolated and stably cultivated from a patient in New York state
    • Rikihisa Y, Zhi N, Wormser GP, Wen B, Horowitz HW, et al. (1997) Ultrastructural and antigenic characterization of a granulocytic ehrlichiosis agent directly isolated and stably cultivated from a patient in New York state. J Infect Dis 175: 210-213.
    • (1997) J Infect Dis , vol.175 , pp. 210-213
    • Rikihisa, Y.1    Zhi, N.2    Wormser, G.P.3    Wen, B.4    Horowitz, H.W.5
  • 13
    • 33846934966 scopus 로고    scopus 로고
    • The developmental cycle of Ehrlichia chaffeensis in vertebrate cells
    • Zhang Jz, Popov VL, Gao S, Walker DH, Yu Xj, (2007) The developmental cycle of Ehrlichia chaffeensis in vertebrate cells. Cell Microbiol 9: 610-618.
    • (2007) Cell Microbiol , vol.9 , pp. 610-618
    • Zhang, J.1    Popov, V.L.2    Gao, S.3    Walker, D.H.4    Yu, X.5
  • 14
    • 84866177929 scopus 로고    scopus 로고
    • Transmission electron microscopy reveals distinct macrophage- and tick cell-specific morphological stages of Ehrlichia chaffeensis
    • Dedonder SE, Cheng C, Willard LH, Boyle DL, Ganta RR, (2012) Transmission electron microscopy reveals distinct macrophage- and tick cell-specific morphological stages of Ehrlichia chaffeensis. PLoS ONE 7: e36749.
    • (2012) PLoS ONE , vol.7
    • Dedonder, S.E.1    Cheng, C.2    Willard, L.H.3    Boyle, D.L.4    Ganta, R.R.5
  • 15
    • 63849101264 scopus 로고    scopus 로고
    • Molecular characterization of Ehrlichia interactions with tick cells and macrophages
    • Ganta RR, Peddireddi L, Seo GM, Dedonder SE, Cheng C, et al. (2009) Molecular characterization of Ehrlichia interactions with tick cells and macrophages. Front Biosci 14: 3259-3273.
    • (2009) Front Biosci , vol.14 , pp. 3259-3273
    • Ganta, R.R.1    Peddireddi, L.2    Seo, G.M.3    Dedonder, S.E.4    Cheng, C.5
  • 16
    • 3042818394 scopus 로고    scopus 로고
    • Heat-shock proteins and the host-pathogen interaction during bacterial infection
    • Stewart GR, Young DB, (2004) Heat-shock proteins and the host-pathogen interaction during bacterial infection. Curr Opin Immunol 16: 506-510.
    • (2004) Curr Opin Immunol , vol.16 , pp. 506-510
    • Stewart, G.R.1    Young, D.B.2
  • 17
    • 33745589526 scopus 로고    scopus 로고
    • Stress wars: the direct role of host and bacterial molecular chaperones in bacterial infection
    • Henderson B, Allan E, Coates AR, (2006) Stress wars: the direct role of host and bacterial molecular chaperones in bacterial infection. Infect Immun 74: 3693-3706.
    • (2006) Infect Immun , vol.74 , pp. 3693-3706
    • Henderson, B.1    Allan, E.2    Coates, A.R.3
  • 18
    • 57149123666 scopus 로고    scopus 로고
    • Molecular chaperones in pathogen virulence: emerging new targets for therapy
    • Neckers L, Tatu U, (2008) Molecular chaperones in pathogen virulence: emerging new targets for therapy. Cell Host Microbe 4: 519-527.
    • (2008) Cell Host Microbe , vol.4 , pp. 519-527
    • Neckers, L.1    Tatu, U.2
  • 19
    • 84863396434 scopus 로고    scopus 로고
    • Aggregate reactivation mediated by the Hsp100 chaperones
    • Zolkiewski M, Zhang T, Nagy M, (2012) Aggregate reactivation mediated by the Hsp100 chaperones. Arch Biochem Biophys 520: 1-6.
    • (2012) Arch Biochem Biophys , vol.520 , pp. 1-6
    • Zolkiewski, M.1    Zhang, T.2    Nagy, M.3
  • 20
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
    • Glover JR, Lindquist S, (1998) Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94: 73-82.
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 21
    • 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
  • 22
    • 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, (1999) Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones. Proc Natl Acad Sci U S A 96: 7184-7189.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 7184-7189
    • Motohashi, K.1    Watanabe, Y.2    Yohda, M.3    Yoshida, M.4
  • 23
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • Goloubinoff P, Mogk A, Zvi AP, Tomoyasu T, Bukau B, (1999) Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc Natl Acad Sci U S A 96: 13732-13737.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Zvi, A.P.3    Tomoyasu, T.4    Bukau, B.5
  • 24
    • 0032969563 scopus 로고    scopus 로고
    • AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
    • Neuwald AF, Aravind L, Spouge JL, Koonin EV, (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
  • 26
    • 0025799542 scopus 로고
    • ClpB is the Escherichia coli heat shock protein F84.1
    • Squires CL, Pedersen S, Ross BM, Squires C, (1991) ClpB is the Escherichia coli heat shock protein F84.1. J Bacteriol 173: 4254-4262.
    • (1991) J Bacteriol , vol.173 , pp. 4254-4262
    • Squires, C.L.1    Pedersen, S.2    Ross, B.M.3    Squires, C.4
  • 27
    • 0029950703 scopus 로고    scopus 로고
    • Heat-shock protein 104 expression is sufficient for thermotolerance in yeast
    • Lindquist S, Kim G, (1996) Heat-shock protein 104 expression is sufficient for thermotolerance in yeast. Proc Natl Acad Sci U S A 93: 5301-5306.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 5301-5306
    • Lindquist, S.1    Kim, G.2
  • 28
    • 38949159752 scopus 로고    scopus 로고
    • Role of the Clp system in stress tolerance, biofilm formation, and intracellular invasion in Porphyromonas gingivalis
    • Capestany CA, Tribble GD, Maeda K, Demuth DR, Lamont RJ, (2008) Role of the Clp system in stress tolerance, biofilm formation, and intracellular invasion in Porphyromonas gingivalis. J Bacteriol 190: 1436-1446.
    • (2008) J Bacteriol , vol.190 , pp. 1436-1446
    • Capestany, C.A.1    Tribble, G.D.2    Maeda, K.3    Demuth, D.R.4    Lamont, R.J.5
  • 29
    • 55849145095 scopus 로고    scopus 로고
    • Characterization of a unique ClpB protein of Mycoplasma pneumoniae and its impact on growth
    • Kannan TR, Musatovova O, Gowda P, Baseman JB, (2008) Characterization of a unique ClpB protein of Mycoplasma pneumoniae and its impact on growth. Infect Immun 76: 5082-5092.
    • (2008) Infect Immun , vol.76 , pp. 5082-5092
    • Kannan, T.R.1    Musatovova, O.2    Gowda, P.3    Baseman, J.B.4
  • 30
    • 39849093588 scopus 로고    scopus 로고
    • The heat-shock protein ClpB of Francisella tularensis is involved in stress tolerance and is required for multiplication in target organs of infected mice
    • Meibom KL, Dubail I, Dupuis M, Barel M, Lenco J, et al. (2008) The heat-shock protein ClpB of Francisella tularensis is involved in stress tolerance and is required for multiplication in target organs of infected mice. Mol Microbiol 67: 1384-1401.
    • (2008) Mol Microbiol , vol.67 , pp. 1384-1401
    • Meibom, K.L.1    Dubail, I.2    Dupuis, M.3    Barel, M.4    Lenco, J.5
  • 31
    • 79952274331 scopus 로고    scopus 로고
    • clpB, a class III heat-shock gene regulated by CtsR, is involved in thermotolerance and virulence of Enterococcus faecalis
    • de Oliveira NE, Abranches J, Gaca AO, Laport MS, Damaso CR, et al. (2011) clpB, a class III heat-shock gene regulated by CtsR, is involved in thermotolerance and virulence of Enterococcus faecalis. Microbiology 157: 656-665.
    • (2011) Microbiology , vol.157 , pp. 656-665
    • de Oliveira, N.E.1    Abranches, J.2    Gaca, A.O.3    Laport, M.S.4    Damaso, C.R.5
  • 32
    • 78049498592 scopus 로고    scopus 로고
    • ClgR regulation of chaperone and protease systems is essential for Mycobacterium tuberculosis parasitism of the macrophage
    • Estorninho M, Smith H, Thole J, Harders-Westerveen J, Kierzek A, et al. (2010) ClgR regulation of chaperone and protease systems is essential for Mycobacterium tuberculosis parasitism of the macrophage. Microbiology 156: 3445-3455.
    • (2010) Microbiology , vol.156 , pp. 3445-3455
    • Estorninho, M.1    Smith, H.2    Thole, J.3    Harders-Westerveen, J.4    Kierzek, A.5
  • 33
    • 80052307960 scopus 로고    scopus 로고
    • Inactivation of clpB in the pathogen Leptospira interrogans reduces virulence and resistance to stress conditions
    • Lourdault K, Cerqueira GM, Wunder EA, Picardeau M, (2011) Inactivation of clpB in the pathogen Leptospira interrogans reduces virulence and resistance to stress conditions. Infect Immun 79: 3711-3717.
    • (2011) Infect Immun , vol.79 , pp. 3711-3717
    • Lourdault, K.1    Cerqueira, G.M.2    Wunder, E.A.3    Picardeau, M.4
  • 34
    • 0032852245 scopus 로고    scopus 로고
    • A novel role for 100 kD heat shock proteins in the parasite Leishmania donovani
    • Krobitsch S, Clos J, (1999) A novel role for 100 kD heat shock proteins in the parasite Leishmania donovani. Cell Stress Chaperones 4: 191-198.
    • (1999) Cell Stress Chaperones , vol.4 , pp. 191-198
    • Krobitsch, S.1    Clos, J.2
  • 35
    • 58149181486 scopus 로고    scopus 로고
    • Hsp104 and ClpB: protein disaggregating machines
    • Doyle SM, Wickner S, (2009) Hsp104 and ClpB: protein disaggregating machines. Trends Biochem Sci 34: 40-48.
    • (2009) Trends Biochem Sci , vol.34 , pp. 40-48
    • Doyle, S.M.1    Wickner, S.2
  • 36
    • 84855207518 scopus 로고    scopus 로고
    • The elusive middle domain of Hsp104 and ClpB: location and function
    • Desantis ME, Shorter J, (2012) The elusive middle domain of Hsp104 and ClpB: location and function. Biochim Biophys Acta 1823: 29-39.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 29-39
    • Desantis, M.E.1    Shorter, J.2
  • 37
    • 27144456262 scopus 로고    scopus 로고
    • The amino-terminal domain of ClpB supports binding to strongly aggregated proteins
    • Barnett ME, Nagy M, Kedzierska S, Zolkiewski M, (2005) The amino-terminal domain of ClpB supports binding to strongly aggregated proteins. J Biol Chem 280: 34940-34945.
    • (2005) J Biol Chem , vol.280 , pp. 34940-34945
    • Barnett, M.E.1    Nagy, M.2    Kedzierska, S.3    Zolkiewski, M.4
  • 38
    • 84868204023 scopus 로고    scopus 로고
    • Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency
    • Zhang T, Ploetz EA, Nagy M, Doyle SM, Wickner S, et al. (2012) Flexible connection of the N-terminal domain in ClpB modulates substrate binding and the aggregate reactivation efficiency. Proteins 80: 2758-2768.
    • (2012) Proteins , vol.80 , pp. 2758-2768
    • Zhang, T.1    Ploetz, E.A.2    Nagy, M.3    Doyle, S.M.4    Wickner, S.5
  • 40
    • 53749099906 scopus 로고    scopus 로고
    • Laboratory maintenance of Ehrlichia chaffeensis and Ehrlichia canis and recovery of organisms for molecular biology and proteomics studies
    • Cheng C, Ganta RR, (2008) Laboratory maintenance of Ehrlichia chaffeensis and Ehrlichia canis and recovery of organisms for molecular biology and proteomics studies. Curr Protoc Microbiol 9: 3A.1.1-3A.1.21.
    • (2008) Curr Protoc Microbiol , vol.9 , pp. 1-21
    • Cheng, C.1    Ganta, R.R.2
  • 41
    • 0026747656 scopus 로고
    • Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile
    • Stafford WF, (1992) Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile. Anal Biochem 203: 295-301.
    • (1992) Anal Biochem , vol.203 , pp. 295-301
    • Stafford, W.F.1
  • 43
    • 0344629876 scopus 로고    scopus 로고
    • Structure and function of the middle domain of ClpB from Escherichia coli
    • Kedzierska S, Akoev V, Barnett ME, Zolkiewski M, (2003) Structure and function of the middle domain of ClpB from Escherichia coli. Biochemistry 42: 14242-14248.
    • (2003) Biochemistry , vol.42 , pp. 14242-14248
    • Kedzierska, S.1    Akoev, V.2    Barnett, M.E.3    Zolkiewski, M.4
  • 44
    • 77951097433 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum and Ehrlichia chaffeensis: subversive manipulators of host cells
    • Rikihisa Y, (2010) Anaplasma phagocytophilum and Ehrlichia chaffeensis: subversive manipulators of host cells. Nat Rev Microbiol 8: 328-339.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 328-339
    • Rikihisa, Y.1
  • 45
    • 14644445240 scopus 로고    scopus 로고
    • Monitoring dynamic expression of nuclear genes in Chlamydomonas reinhardtii by using a synthetic luciferase reporter gene
    • Fuhrmann M, Hausherr A, Ferbitz L, Schodl T, Heitzer M, et al. (2004) Monitoring dynamic expression of nuclear genes in Chlamydomonas reinhardtii by using a synthetic luciferase reporter gene. Plant Mol Biol 55: 869-881.
    • (2004) Plant Mol Biol , vol.55 , pp. 869-881
    • Fuhrmann, M.1    Hausherr, A.2    Ferbitz, L.3    Schodl, T.4    Heitzer, M.5
  • 46
    • 0034529228 scopus 로고    scopus 로고
    • Structure and activity of ClpB from Escherichia coli. Role of the amino-and -carboxyl-terminal domains
    • Barnett ME, Zolkiewska A, Zolkiewski M, (2000) Structure and activity of ClpB from Escherichia coli. Role of the amino-and-carboxyl-terminal domains. J Biol Chem 275: 37565-37571.
    • (2000) J Biol Chem , vol.275 , pp. 37565-37571
    • Barnett, M.E.1    Zolkiewska, A.2    Zolkiewski, M.3
  • 47
    • 1342268093 scopus 로고    scopus 로고
    • Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB
    • Akoev V, Gogol EP, Barnett ME, Zolkiewski M, (2004) Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB. Protein Sci 13: 567-574.
    • (2004) Protein Sci , vol.13 , pp. 567-574
    • Akoev, V.1    Gogol, E.P.2    Barnett, M.E.3    Zolkiewski, M.4
  • 48
    • 77949329710 scopus 로고    scopus 로고
    • Synergistic cooperation between two ClpB isoforms in aggregate reactivation
    • Nagy M, Guenther I, Akoyev V, Barnett ME, Zavodszky MI, et al. (2010) Synergistic cooperation between two ClpB isoforms in aggregate reactivation. J Mol Biol 396: 697-707.
    • (2010) J Mol Biol , vol.396 , pp. 697-707
    • Nagy, M.1    Guenther, I.2    Akoyev, V.3    Barnett, M.E.4    Zavodszky, M.I.5
  • 49
    • 0042858475 scopus 로고    scopus 로고
    • Characterization of a trap mutant of the AAA+ chaperone ClpB
    • Weibezahn J, Schlieker C, Bukau B, Mogk A, (2003) Characterization of a trap mutant of the AAA+ chaperone ClpB. J Biol Chem 278: 32608-32617.
    • (2003) J Biol Chem , vol.278 , pp. 32608-32617
    • Weibezahn, J.1    Schlieker, C.2    Bukau, B.3    Mogk, A.4
  • 50
    • 59949102118 scopus 로고    scopus 로고
    • Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpB
    • Nagy M, Wu HC, Liu Z, Kedzierska-Mieszkowska S, Zolkiewski M, (2009) Walker-A threonine couples nucleotide occupancy with the chaperone activity of the AAA+ ATPase ClpB. Protein Sci 18: 287-293.
    • (2009) Protein Sci , vol.18 , pp. 287-293
    • Nagy, M.1    Wu, H.C.2    Liu, Z.3    Kedzierska-Mieszkowska, S.4    Zolkiewski, M.5
  • 51
    • 3142657524 scopus 로고    scopus 로고
    • Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104
    • Lum R, Tkach JM, Vierling E, Glover JR, (2004) Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. J Biol Chem 279: 29139-29146.
    • (2004) J Biol Chem , vol.279 , pp. 29139-29146
    • Lum, R.1    Tkach, J.M.2    Vierling, E.3    Glover, J.R.4
  • 53
    • 0036349911 scopus 로고    scopus 로고
    • Conserved amino acid residues within the amino-terminal domain of ClpB are essential for the chaperone activity
    • Liu Z, Tek V, Akoev V, Zolkiewski M, (2002) Conserved amino acid residues within the amino-terminal domain of ClpB are essential for the chaperone activity. J Mol Biol 321: 111-120.
    • (2002) J Mol Biol , vol.321 , pp. 111-120
    • Liu, Z.1    Tek, V.2    Akoev, V.3    Zolkiewski, M.4
  • 54
    • 33846231395 scopus 로고    scopus 로고
    • M domains couple the ClpB threading motor with the DnaK chaperone activity
    • Haslberger T, Weibezahn J, Zahn R, Lee S, Tsai FT, et al. (2007) M domains couple the ClpB threading motor with the DnaK chaperone activity. Mol Cell 25: 247-260.
    • (2007) Mol Cell , vol.25 , pp. 247-260
    • Haslberger, T.1    Weibezahn, J.2    Zahn, R.3    Lee, S.4    Tsai, F.T.5
  • 55
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: folding, refolding, and degrading proteins
    • Wickner S, Maurizi MR, Gottesman S, (1999) Posttranslational quality control: folding, refolding, and degrading proteins. Science 286: 1888-1893.
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 56
    • 77956178634 scopus 로고    scopus 로고
    • The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner
    • Sielaff B, Tsai FT, (2010) The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner. J Mol Biol 402: 30-37.
    • (2010) J Mol Biol , vol.402 , pp. 30-37
    • Sielaff, B.1    Tsai, F.T.2
  • 57
    • 79955563304 scopus 로고    scopus 로고
    • Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation
    • Miot M, Reidy M, Doyle SM, Hoskins JR, Johnston DM, et al. (2011) Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation. Proc Natl Acad Sci U S A 108: 6915-6920.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 6915-6920
    • Miot, M.1    Reidy, M.2    Doyle, S.M.3    Hoskins, J.R.4    Johnston, D.M.5
  • 58
    • 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, (2006) Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation. J Biol Chem 281: 7022-7029.
    • (2006) J Biol Chem , vol.281 , pp. 7022-7029
    • Zietkiewicz, S.1    Lewandowska, A.2    Stocki, P.3    Liberek, K.4
  • 59
    • 84866438776 scopus 로고    scopus 로고
    • Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation
    • Winkler J, Tyedmers J, Bukau B, Mogk A, (2012) Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. The Journal of cell biology 198: 387-404.
    • (2012) The Journal of Cell Biology , vol.198 , pp. 387-404
    • Winkler, J.1    Tyedmers, J.2    Bukau, B.3    Mogk, A.4
  • 60
    • 8844251486 scopus 로고    scopus 로고
    • Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB
    • Weibezahn J, Tessarz P, Schlieker C, Zahn R, Maglica Z, et al. (2004) Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell 119: 653-665.
    • (2004) Cell , vol.119 , pp. 653-665
    • Weibezahn, J.1    Tessarz, P.2    Schlieker, C.3    Zahn, R.4    Maglica, Z.5
  • 61
    • 77958487260 scopus 로고    scopus 로고
    • Cellular strategies for controlling protein aggregation
    • Tyedmers J, Mogk A, Bukau B, (2010) Cellular strategies for controlling protein aggregation. Nat Rev Mol Cell Biol 11: 777-788.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 777-788
    • Tyedmers, J.1    Mogk, A.2    Bukau, B.3
  • 62
    • 69949145963 scopus 로고    scopus 로고
    • DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface
    • Acebron SP, Martin I, del Castillo U, Moro F, Muga A, (2009) DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface. FEBS Lett 583: 2991-2996.
    • (2009) FEBS Lett , vol.583 , pp. 2991-2996
    • Acebron, S.P.1    Martin, I.2    del Castillo, U.3    Moro, F.4    Muga, A.5


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