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• W2006420470 abstract "Chaperones of Thermus thermophiluscooperate in reactivation of heat-inactivated proteins. The protein, inactivated at a high temperature in a TDnaKJ-GrpE set, recovered its activity during subsequent incubation withTClpB at moderate temperature (Motohashi, K., Watanabe, Y., Yohda, M., and Yoshida, M. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 7184–7189). Here, we report that the addition of chaperonin (Tcpn) at moderate temperature improves the yield of the TDnaKJ-GrpE-ClpB-dependent reactivation. The trap-Tcpn, which binds substrate protein but does not release it, inhibits reactivation severely. Maximum recovery is gained at sub-stoichiometric amounts of each component ofTDnaKJ, TGrpE, and TClpB relative to the substrate monomer. These observations indicate that, driven by ATP hydrolysis, TDnaKJ-GrpE-ClpB chaperones catalytically cooperate and release heat-inactivated protein as a non-native, chaperonin-recognizable folding intermediate. Chaperones of Thermus thermophiluscooperate in reactivation of heat-inactivated proteins. The protein, inactivated at a high temperature in a TDnaKJ-GrpE set, recovered its activity during subsequent incubation withTClpB at moderate temperature (Motohashi, K., Watanabe, Y., Yohda, M., and Yoshida, M. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 7184–7189). Here, we report that the addition of chaperonin (Tcpn) at moderate temperature improves the yield of the TDnaKJ-GrpE-ClpB-dependent reactivation. The trap-Tcpn, which binds substrate protein but does not release it, inhibits reactivation severely. Maximum recovery is gained at sub-stoichiometric amounts of each component ofTDnaKJ, TGrpE, and TClpB relative to the substrate monomer. These observations indicate that, driven by ATP hydrolysis, TDnaKJ-GrpE-ClpB chaperones catalytically cooperate and release heat-inactivated protein as a non-native, chaperonin-recognizable folding intermediate. the trigonal complex of DnaK3DnaJ3DafA3 of T. thermophilus TDnaKJ complex +TGrpE TDnaKJ complex +TGrpE + TClpB glucose-6-phosphate dehydrogenase a complex of GroEL (tetradecamer) and GroES (heptamer) of T. thermophilus lactate dehydrogenase 4-morpholinepropanesulfonic acid Recently, the functional chaperone cooperation between Hsp70 and Hsp104 in reactivation of heat-inactivated proteins has been noticed. In eukaryotes, this cooperation enables yeast to recover from heat stress in vivo (1.Sanchez Y. Parsell D.A. Taulien J. Vogel J.L. Craig E.A. Lindquist S. J. Bacteriol. 1993; 175: 6484-6491Crossref PubMed Google Scholar, 2.Parsell D.A. Kowal A.S. Singer M.A. Lindquist S. Nature. 1994; 372: 475-478Crossref PubMed Scopus (728) Google Scholar) and reactivate proteins that had been chemically denatured and allowed to aggregate in vitro (3.Glover J.R. Lindquist S. Cell. 1998; 94: 73-82Abstract Full Text Full Text PDF PubMed Scopus (1081) Google Scholar). In prokaryotes, we have demonstrated that heat-inactivated proteins were rescued by the cooperation between DnaK (Hsp70)-DnaJ-GrpE and ClpB (Hsp104) from a thermophilic eubacteria, Thermus thermophilus (4.Motohashi K. Watanabe Y. Yohda M. Yoshida M. Proc. Natl. Acad. Sci. U. S. A. 1999; 96: 7184-7189Crossref PubMed Scopus (221) Google Scholar). Such a cooperation was also reported forEscherichia coli (5.Zolkiewski M. J. Biol. Chem. 1999; 274: 28083-28086Abstract Full Text Full Text PDF PubMed Scopus (296) Google Scholar). Here, we report the role of each component in this cooperation and relationship to Hsp60 (GroEL, chaperonin).E. coli DnaK, together with its co-chaperones, DnaJ and GrpE, can assist in the refolding of some proteins (6.Schroder H. Langer T. Hartl F.U. Bukau B. EMBO J. 1993; 12: 4137-4144Crossref PubMed Scopus (497) Google Scholar, 7.Ziemienowicz A. Skowyra D. Zeilstra-Ryalls J. Fayet O. Georgopoulos C. Zylicz M. J. Biol. Chem. 1993; 268: 25425-25431Abstract Full Text PDF PubMed Google Scholar, 8.Diamant S. Goloubinoff P. Biochemistry. 1998; 37: 9688-9694Crossref PubMed Scopus (59) Google Scholar). The binding and release of substrate proteins are regulated by ATP/ADP state of DnaK, which is under tight control with DnaJ and GrpE (9.Bukau B. Horwich A.L. Cell. 1998; 92: 351-366Abstract Full Text Full Text PDF PubMed Scopus (2401) Google Scholar, 10.Szabo A. Langer T. Schroder H. Flanagan J. Bukau B. Hartl F.U. Proc. Natl. Acad. Sci. U. S. A. 1994; 91: 10345-10349Crossref PubMed Scopus (443) Google Scholar, 11.McCarty J.S. Buchberger A. Reinstein J. Bukau B. J. Mol. Biol. 1995; 249: 126-137Crossref PubMed Scopus (349) Google Scholar); DnaJ accelerate the rate of ATP hydrolysis and GrpE promotes the ADP/ATP exchange (12.Liberek K. Marszalek J. Ang D. Georgopoulos C. Zylicz M. Proc. Natl. Acad. Sci. U. S. A. 1991; 88: 2874-2878Crossref PubMed Scopus (684) Google Scholar). Unlike in other bacteria, DnaK and DnaJ are purified only as a stable trigonal ring complex from T. thermophilus(13.Motohashi K. Taguchi H. Ishii N. Yoshida M. J. Biol. Chem. 1994; 269: 27074-27079Abstract Full Text PDF PubMed Google Scholar). This TDnaKJ1complex (hereafter, the prefix T designates proteins ofT. thermophilus) comprises three copies of eachTDnaK (69 kDa), TDnaJ (33 kDa), andTDafA and has a molecular mass of 330 kDa (14.Motohashi K. Yohda M. Endo I. Yoshida M. J. Biol. Chem. 1996; 271: 17343-17348Abstract Full Text Full Text PDF PubMed Scopus (56) Google Scholar).TDafA is a small (8 kDa) protein necessary for the assembly of TDnaK and TDnaJ. The TDnaKJ complex does not dissociate into individual components during interaction with ATP, TGrpE, and a model denatured protein (13.Motohashi K. Taguchi H. Ishii N. Yoshida M. J. Biol. Chem. 1994; 269: 27074-27079Abstract Full Text PDF PubMed Google Scholar, 14.Motohashi K. Yohda M. Endo I. Yoshida M. J. Biol. Chem. 1996; 271: 17343-17348Abstract Full Text Full Text PDF PubMed Scopus (56) Google Scholar, 15.Motohashi K. Yohda M. Odaka M. Yoshida M. FEBS Lett. 1997; 412: 633-636Crossref PubMed Scopus (24) Google Scholar).TGrpE (22 kDa) is isolated as a homodimer, and it stimulates ATPase turnover of the TDnaKJ complex (15.Motohashi K. Yohda M. Odaka M. Yoshida M. FEBS Lett. 1997; 412: 633-636Crossref PubMed Scopus (24) Google Scholar, 16.Klostermeier D. Seidel R. Reinstein J. J. Mol. Biol. 1998; 279: 841-853Crossref PubMed Scopus (42) Google Scholar, 17.Klostermeier D. Seidel R. Reinstein J. J. Mol. Biol. 1999; 287: 511-525Crossref PubMed Scopus (36) Google Scholar).TDnaKJ complex and TGrpE constitute a DnaK chaperone set (KJE set).As a member of the Hsp104 family, bacterial ClpB has two nucleotide binding domains, each displaying one set of consensus ATP-binding sequence motifs, and forms a homohexameric complex (18.Gottesman S. Squires C. Pichersky E. Carrington M. Hobbs M. Mattick J.S. Dalrymple B. Kuramitsu H. Shiroza T. Foster T. Clark W.P. Ross B. Squires C.L. Maurizi M.R. Proc. Natl. Acad. Sci. U. S. A. 1990; 87: 3513-3517Crossref PubMed Scopus (194) Google Scholar, 19.Parsell D.A. Sanchez Y. Stitzel J.D. Lindquist S. Nature. 1991; 353: 270-273Crossref PubMed Scopus (203) Google Scholar, 20.Parsell D.A. Kowal A.S. Lindquist S. J. Biol. Chem. 1994; 269: 4480-4487Abstract Full Text PDF PubMed Google Scholar, 21.Zolkiewski M. Kessel M. Ginsburg A. Maurizi M.R. Protein Sci. 1999; 8: 1899-1903Crossref PubMed Scopus (74) Google Scholar). LikeE. coli ClpB, TClpB (97 kDa) has an ATPase activity that is stimulated by the addition of a model denatured protein (4.Motohashi K. Watanabe Y. Yohda M. Yoshida M. Proc. Natl. Acad. Sci. U. S. A. 1999; 96: 7184-7189Crossref PubMed Scopus (221) Google Scholar, 22.Woo K.M. Kim K.I. Goldberg A.L. Ha D.B. Chung C.H. J. Biol. Chem. 1992; 267: 20429-20434Abstract Full Text PDF PubMed Google Scholar). TClpB shows chaperone activity only when combined with TDnaKJ complex and TGrpE. When thermophilic lactate dehydrogenase (LDH) is heat-inactivated at high temperature in the presence of the KJE set and ATP, the enzyme activity of LDH is recovered during subsequent incubation with TClpB at a moderate temperature (4.Motohashi K. Watanabe Y. Yohda M. Yoshida M. Proc. Natl. Acad. Sci. U. S. A. 1999; 96: 7184-7189Crossref PubMed Scopus (221) Google Scholar).Chaperonin (Hsp60) is another chaperone that plays a critical role in cells, even under condition without stress (23.Hartl F.U. Nature. 1996; 381: 571-579Crossref PubMed Scopus (3087) Google Scholar). E. colichaperonin, GroEL, is composed of 14 identical subunits forming two heptamer rings stacked back to back (24.Braig K. Otwinowski Z. Hegde R. Boisvert D.C. Joachimiak A. Horwich A.L. Sigler P.B. Nature. 1994; 371: 578-586Crossref PubMed Scopus (1182) Google Scholar). GroEL binds nonnative protein and sequesters it into the central cavity surrounded by the inside wall of a heptamer ring and capped by GroES, a co-chaperonin that also has a heptameric structure (25.Weissman J.S. Hohl C.M. Kovalenko O. Kashi Y. Chen S. Braig K. Saibil H.R. Fenton W.A. Horwich A.L. Cell. 1995; 83: 577-587Abstract Full Text PDF PubMed Scopus (387) Google Scholar, 26.Hunt J.F. Weaver A.J. Landry S.J. Gierasch L. Deisenhofer J. Nature. 1996; 379: 37-45Crossref PubMed Scopus (397) Google Scholar, 27.Sakikawa C. Taguchi H. Makino Y. Yoshida M. J. Biol. Chem. 1999; 274: 21251-21256Abstract Full Text Full Text PDF PubMed Scopus (96) Google Scholar). ATP hydrolysis provides a timer to give the encapsulated protein several seconds to fold without fear of aggregation, and then GroES dissociates from GroEL, allowing substrate protein to escape from the cavity (28.Rye H.S. Roseman A.M. Chen S. Furtak K. Fenton W.A. Saibil H.R. Horwich A.L. Cell. 1999; 97: 325-338Abstract Full Text Full Text PDF PubMed Scopus (285) Google Scholar). Unlike GroEL of E. coli, GroEL of T. thermophilus is purified as a complex of GroEL (tetradecamer) and GroES (heptamer) (Tcpn) (29.Taguchi H. Konishi J. Ishii N. Yoshida M. J. Biol. Chem. 1991; 266: 22411-22418Abstract Full Text PDF PubMed Google Scholar). It can protect substrate proteins from irreversible heat denaturation at high temperatures and reactivate them at moderate temperatures by the addition of ATP (30.Taguchi H. Yoshida M. J. Biol. Chem. 1993; 268: 5371-5375Abstract Full Text PDF PubMed Google Scholar).To obtain further insight into the DnaKJ-GrpE-ClpB (KJE-B)-dependent reactivation of heat-inactivated protein, we introduced Tcpn into the reaction and changed the concentrations of each chaperone component. The results indicate that KJE set and TClpB cooperate and release the substrate protein into the medium as a chaperonin-recognizable folding intermediate. Recently, the functional chaperone cooperation between Hsp70 and Hsp104 in reactivation of heat-inactivated proteins has been noticed. In eukaryotes, this cooperation enables yeast to recover from heat stress in vivo (1.Sanchez Y. Parsell D.A. Taulien J. Vogel J.L. Craig E.A. Lindquist S. J. Bacteriol. 1993; 175: 6484-6491Crossref PubMed Google Scholar, 2.Parsell D.A. Kowal A.S. Singer M.A. Lindquist S. Nature. 1994; 372: 475-478Crossref PubMed Scopus (728) Google Scholar) and reactivate proteins that had been chemically denatured and allowed to aggregate in vitro (3.Glover J.R. Lindquist S. Cell. 1998; 94: 73-82Abstract Full Text Full Text PDF PubMed Scopus (1081) Google Scholar). In prokaryotes, we have demonstrated that heat-inactivated proteins were rescued by the cooperation between DnaK (Hsp70)-DnaJ-GrpE and ClpB (Hsp104) from a thermophilic eubacteria, Thermus thermophilus (4.Motohashi K. Watanabe Y. Yohda M. Yoshida M. Proc. Natl. Acad. Sci. U. S. A. 1999; 96: 7184-7189Crossref PubMed Scopus (221) Google Scholar). Such a cooperation was also reported forEscherichia coli (5.Zolkiewski M. J. Biol. Chem. 1999; 274: 28083-28086Abstract Full Text Full Text PDF PubMed Scopus (296) Google Scholar). Here, we report the role of each component in this cooperation and relationship to Hsp60 (GroEL, chaperonin). E. coli DnaK, together with its co-chaperones, DnaJ and GrpE, can assist in the refolding of some proteins (6.Schroder H. Langer T. Hartl F.U. Bukau B. EMBO J. 1993; 12: 4137-4144Crossref PubMed Scopus (497) Google Scholar, 7.Ziemienowicz A. Skowyra D. Zeilstra-Ryalls J. Fayet O. Georgopoulos C. Zylicz M. J. Biol. Chem. 1993; 268: 25425-25431Abstract Full Text PDF PubMed Google Scholar, 8.Diamant S. Goloubinoff P. Biochemistry. 1998; 37: 9688-9694Crossref PubMed Scopus (59) Google Scholar). The binding and release of substrate proteins are regulated by ATP/ADP state of DnaK, which is under tight control with DnaJ and GrpE (9.Bukau B. Horwich A.L. Cell. 1998; 92: 351-366Abstract Full Text Full Text PDF PubMed Scopus (2401) Google Scholar, 10.Szabo A. Langer T. Schroder H. Flanagan J. Bukau B. Hartl F.U. Proc. Natl. Acad. Sci. U. S. A. 1994; 91: 10345-10349Crossref PubMed Scopus (443) Google Scholar, 11.McCarty J.S. Buchberger A. Reinstein J. Bukau B. J. Mol. Biol. 1995; 249: 126-137Crossref PubMed Scopus (349) Google Scholar); DnaJ accelerate the rate of ATP hydrolysis and GrpE promotes the ADP/ATP exchange (12.Liberek K. Marszalek J. Ang D. Georgopoulos C. Zylicz M. Proc. Natl. Acad. Sci. U. S. A. 1991; 88: 2874-2878Crossref PubMed Scopus (684) Google Scholar). Unlike in other bacteria, DnaK and DnaJ are purified only as a stable trigonal ring complex from T. thermophilus(13.Motohashi K. Taguchi H. Ishii N. Yoshida M. J. Biol. Chem. 1994; 269: 27074-27079Abstract Full Text PDF PubMed Google Scholar). This TDnaKJ1complex (hereafter, the prefix T designates proteins ofT. thermophilus) comprises three copies of eachTDnaK (69 kDa), TDnaJ (33 kDa), andTDafA and has a molecular mass of 330 kDa (14.Motohashi K. Yohda M. Endo I. Yoshida M. J. Biol. Chem. 1996; 271: 17343-17348Abstract Full Text Full Text PDF PubMed Scopus (56) Google Scholar).TDafA is a small (8 kDa) protein necessary for the assembly of TDnaK and TDnaJ. The TDnaKJ complex does not dissociate into individual components during interaction with ATP, TGrpE, and a model denatured protein (13.Motohashi K. Taguchi H. Ishii N. Yoshida M. J. Biol. Chem. 1994; 269: 27074-27079Abstract Full Text PDF PubMed Google Scholar, 14.Motohashi K. Yohda M. Endo I. Yoshida M. J. Biol. Chem. 1996; 271: 17343-17348Abstract Full Text Full Text PDF PubMed Scopus (56) Google Scholar, 15.Motohashi K. Yohda M. Odaka M. Yoshida M. FEBS Lett. 1997; 412: 633-636Crossref PubMed Scopus (24) Google Scholar).TGrpE (22 kDa) is isolated as a homodimer, and it stimulates ATPase turnover of the TDnaKJ complex (15.Motohashi K. Yohda M. Odaka M. Yoshida M. FEBS Lett. 1997; 412: 633-636Crossref PubMed Scopus (24) Google Scholar, 16.Klostermeier D. Seidel R. Reinstein J. J. Mol. Biol. 1998; 279: 841-853Crossref PubMed Scopus (42) Google Scholar, 17.Klostermeier D. Seidel R. Reinstein J. J. Mol. Biol. 1999; 287: 511-525Crossref PubMed Scopus (36) Google Scholar).TDnaKJ complex and TGrpE constitute a DnaK chaperone set (KJE set). As a member of the Hsp104 family, bacterial ClpB has two nucleotide binding domains, each displaying one set of consensus ATP-binding sequence motifs, and forms a homohexameric complex (18.Gottesman S. Squires C. Pichersky E. Carrington M. Hobbs M. Mattick J.S. Dalrymple B. Kuramitsu H. Shiroza T. Foster T. Clark W.P. Ross B. Squires C.L. Maurizi M.R. Proc. Natl. Acad. Sci. U. S. A. 1990; 87: 3513-3517Crossref PubMed Scopus (194) Google Scholar, 19.Parsell D.A. Sanchez Y. Stitzel J.D. Lindquist S. Nature. 1991; 353: 270-273Crossref PubMed Scopus (203) Google Scholar, 20.Parsell D.A. Kowal A.S. Lindquist S. J. Biol. Chem. 1994; 269: 4480-4487Abstract Full Text PDF PubMed Google Scholar, 21.Zolkiewski M. Kessel M. Ginsburg A. Maurizi M.R. Protein Sci. 1999; 8: 1899-1903Crossref PubMed Scopus (74) Google Scholar). LikeE. coli ClpB, TClpB (97 kDa) has an ATPase activity that is stimulated by the addition of a model denatured protein (4.Motohashi K. Watanabe Y. Yohda M. Yoshida M. Proc. Natl. Acad. Sci. U. S. A. 1999; 96: 7184-7189Crossref PubMed Scopus (221) Google Scholar, 22.Woo K.M. Kim K.I. Goldberg A.L. Ha D.B. Chung C.H. J. Biol. Chem. 1992; 267: 20429-20434Abstract Full Text PDF PubMed Google Scholar). TClpB shows chaperone activity only when combined with TDnaKJ complex and TGrpE. When thermophilic lactate dehydrogenase (LDH) is heat-inactivated at high temperature in the presence of the KJE set and ATP, the enzyme activity of LDH is recovered during subsequent incubation with TClpB at a moderate temperature (4.Motohashi K. Watanabe Y. Yohda M. Yoshida M. Proc. Natl. Acad. Sci. U. S. A. 1999; 96: 7184-7189Crossref PubMed Scopus (221) Google Scholar). Chaperonin (Hsp60) is another chaperone that plays a critical role in cells, even under condition without stress (23.Hartl F.U. Nature. 1996; 381: 571-579Crossref PubMed Scopus (3087) Google Scholar). E. colichaperonin, GroEL, is composed of 14 identical subunits forming two heptamer rings stacked back to back (24.Braig K. Otwinowski Z. Hegde R. Boisvert D.C. Joachimiak A. Horwich A.L. Sigler P.B. Nature. 1994; 371: 578-586Crossref PubMed Scopus (1182) Google Scholar). GroEL binds nonnative protein and sequesters it into the central cavity surrounded by the inside wall of a heptamer ring and capped by GroES, a co-chaperonin that also has a heptameric structure (25.Weissman J.S. Hohl C.M. Kovalenko O. Kashi Y. Chen S. Braig K. Saibil H.R. Fenton W.A. Horwich A.L. Cell. 1995; 83: 577-587Abstract Full Text PDF PubMed Scopus (387) Google Scholar, 26.Hunt J.F. Weaver A.J. Landry S.J. Gierasch L. Deisenhofer J. Nature. 1996; 379: 37-45Crossref PubMed Scopus (397) Google Scholar, 27.Sakikawa C. Taguchi H. Makino Y. Yoshida M. J. Biol. Chem. 1999; 274: 21251-21256Abstract Full Text Full Text PDF PubMed Scopus (96) Google Scholar). ATP hydrolysis provides a timer to give the encapsulated protein several seconds to fold without fear of aggregation, and then GroES dissociates from GroEL, allowing substrate protein to escape from the cavity (28.Rye H.S. Roseman A.M. Chen S. Furtak K. Fenton W.A. Saibil H.R. Horwich A.L. Cell. 1999; 97: 325-338Abstract Full Text Full Text PDF PubMed Scopus (285) Google Scholar). Unlike GroEL of E. coli, GroEL of T. thermophilus is purified as a complex of GroEL (tetradecamer) and GroES (heptamer) (Tcpn) (29.Taguchi H. Konishi J. Ishii N. Yoshida M. J. Biol. Chem. 1991; 266: 22411-22418Abstract Full Text PDF PubMed Google Scholar). It can protect substrate proteins from irreversible heat denaturation at high temperatures and reactivate them at moderate temperatures by the addition of ATP (30.Taguchi H. Yoshida M. J. Biol. Chem. 1993; 268: 5371-5375Abstract Full Text PDF PubMed Google Scholar). To obtain further insight into the DnaKJ-GrpE-ClpB (KJE-B)-dependent reactivation of heat-inactivated protein, we introduced Tcpn into the reaction and changed the concentrations of each chaperone component. The results indicate that KJE set and TClpB cooperate and release the substrate protein into the medium as a chaperonin-recognizable folding intermediate." @default.
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• W2006420470 title "Heat-inactivated Proteins Managed by DnaKJ-GrpE-ClpB Chaperones Are Released as a Chaperonin-recognizable Non-native Form" @default.
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• W2006420470 cites W2010474671 @default.
• W2006420470 cites W2011562799 @default.
• W2006420470 cites W2017886114 @default.
• W2006420470 cites W2022796050 @default.
• W2006420470 cites W2036398011 @default.
• W2006420470 cites W2038347400 @default.
• W2006420470 cites W2040795144 @default.
• W2006420470 cites W2043481076 @default.
• W2006420470 cites W2043693325 @default.
• W2006420470 cites W2051884335 @default.
• W2006420470 cites W2059277971 @default.
• W2006420470 cites W2069831492 @default.
• W2006420470 cites W2072744250 @default.
• W2006420470 cites W2082329995 @default.
• W2006420470 cites W2086922403 @default.
• W2006420470 cites W2088405438 @default.
• W2006420470 cites W2088890018 @default.
• W2006420470 cites W2119999468 @default.
• W2006420470 cites W2136560136 @default.
• W2006420470 cites W2150041704 @default.
• W2006420470 cites W2150315266 @default.
• W2006420470 cites W391993344 @default.
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