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Volumn 17, Issue 3, 2012, Pages 361-373

Role of a conserved aspartic acid in nucleotide binding domain 1 (NBD1) of Hsp100 chaperones in their activities

Author keywords

Chaperone dependent protein disaggregation; Hsp100; Hsp70; Prion curing agent guanidine hydrochloride; Protein aggregation

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ASPARTIC ACID; CHAPERONE; GUANIDINE; HEAT SHOCK PROTEIN 100; HEAT SHOCK PROTEIN 104; PROTEIN CLPB; SERINE;

EID: 84863572519     PISSN: 13558145     EISSN: 14661268     Source Type: Journal    
DOI: 10.1007/s12192-011-0312-4     Document Type: Article
Times cited : (8)

References (41)
  • 1
    • 33749244758 scopus 로고    scopus 로고
    • The molecular chaperone Hsp104-A molecular machine for protein disaggregation
    • DOI 10.1016/j.jsb.2006.02.004, PII S1047847706000505, AAA + Proteins
    • Bösl B, Grimminger V, Walter S (2006) The molecular chaperone Hsp104-a molecular machine for protein disaggregation. J StructBiol 156:139-148 (Pubitemid 44486053)
    • (2006) Journal of Structural Biology , vol.156 , Issue.1 , pp. 139-148
    • Bosl, B.1    Grimminger, V.2    Walter, S.3
  • 2
    • 0029052468 scopus 로고
    • Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]
    • Chernoff YO, Lindquist SL, Ono B, Inge-Vechtomov SG, Liebman SW (1995) Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science 268:880-884
    • (1995) Science , vol.268 , pp. 880-884
    • Chernoff, Y.O.1    Lindquist, S.L.2    Ono, B.3    Inge-Vechtomov, S.G.4    Liebman, S.W.5
  • 3
    • 0028360726 scopus 로고
    • Differential regulation of Hsp70 subfamilies by the eukaryotic DnaJ homologue Ydj1
    • Cyr D, Douglas MG (1994) Differential regulation of Hsp70 sub- families by the eukaryotic DnaJ homologue YDJ1. J Biol Chem 269:9798-9804 (Pubitemid 24196586)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.13 , pp. 9798-9804
    • Cyr, D.M.1    Douglas, M.G.2
  • 5
    • 0034932879 scopus 로고    scopus 로고
    • The elimination of the yeast [PSI+] prion by guanidine hydrochlo- ride is the result of Hsp104 inactivation
    • Ferreira PC, Ness F, Edwards SR, Cox BS, Tuite MF (2001) The elimination of the yeast [PSI+] prion by guanidine hydrochlo- ride is the result of Hsp104 inactivation. Mol Microbiol 40:1375-1369
    • (2001) Mol Microbiol , vol.40 , pp. 1375-1369
    • Ferreira, P.C.1    Ness, F.2    Edwards, S.R.3    Cox, B.S.4    Tuite, M.F.5
  • 6
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • DOI 10.1016/S0092-8674(00)81223-4
    • Glover JR, Lindquist S (1998) Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94:73-82 (Pubitemid 28347471)
    • (1998) Cell , vol.94 , Issue.1 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 7
    • 1542380028 scopus 로고    scopus 로고
    • The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104
    • DOI 10.1074/jbc.M312403200
    • Grimminger V, Richter K, Imhof A, Buchner J, Walter S (2004) The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104. J Biol Chem 279:7378-7383 (Pubitemid 38294613)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 7378-7383
    • Grimminger, V.1    Richter, K.2    Imhof, A.3    Buchner, J.4    Walter, S.5
  • 8
    • 0034974996 scopus 로고    scopus 로고
    • Guanidine hydrochloride inhibits Hsp104 activity in vivo: A possible explanation for its effect in curing yeast prions
    • DOI 10.1007/s002840010251
    • Jung G, Masison DC (2001) Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions. Curr Microbiol 43:7-10 (Pubitemid 32549917)
    • (2001) Current Microbiology , vol.43 , Issue.1 , pp. 7-10
    • Jung, G.1    Masison, D.C.2
  • 9
  • 10
    • 0025768061 scopus 로고
    • Expression of ClpB, an analog of the ATP-dependent protease regulatory subunit in Escherichia coli, is controlled by a heat shock sigma factor (sigma 32
    • Kitagawa M, Wada C, Yoshioka S, Yura T (1991) Expression of ClpB, an analog of the ATP-dependent protease regulatory subunit in Escherichia coli, is controlled by a heat shock sigma factor (sigma 32). J Bacteriol 173:4247-4253
    • (1991) J Bacteriol , vol.173 , pp. 4247-4253
    • Kitagawa, M.1    Wada, C.2    Yoshioka, S.3    Yura, T.4
  • 11
    • 0035824878 scopus 로고    scopus 로고
    • Importance of two ATP-binding sites for oligomerization, ATPase activity and chaperone function of mitochondrial Hsp78 protein
    • DOI 10.1006/jmbi.2001.5190
    • Krzewska J, Konopa G, Liberek K (2001a) Importance of two ATP-binding sites for oligomerization, ATPase activity and chaperone function of mitochondrial Hsp78 protein. J Mol Biol 314:901-910 (Pubitemid 34087856)
    • (2001) Journal of Molecular Biology , vol.314 , Issue.4 , pp. 901-910
    • Krzewska, J.1    Konopa, G.2    Liberek, K.3
  • 12
    • 0035951385 scopus 로고    scopus 로고
    • Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding
    • DOI 10.1016/S0014-5793(00)02423-6, PII S0014579300024236
    • Krzewska J, Langer T, Liberek K (2001b) Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding. FEBS Lett 489:92-96 (Pubitemid 32176012)
    • (2001) FEBS Letters , vol.489 , Issue.1 , pp. 92-96
    • Krzewska, J.1    Langer, T.2    Liberek, K.3
  • 13
    • 0029852402 scopus 로고    scopus 로고
    • Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro
    • Laskowska E, Kuczynska-Wisnik D, Skórko-Glonek J, Taylor A (1996) Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro. Mol Microbiol 22:555-571 (Pubitemid 26373839)
    • (1996) Molecular Microbiology , vol.22 , Issue.3 , pp. 555-571
    • Laskowska, E.1    Kuczynska-Wisnik, D.2    Skorko-Glonek, J.3    Taylor, A.4
  • 14
    • 0142227208 scopus 로고    scopus 로고
    • The structure of ClpB: A molecular chaperone that rescues proteins from an aggregated state
    • DOI 10.1016/S0092-8674(03)00807-9
    • Lee S, Sowa ME, Watanabe YH, Sigler PB, Chiu W, Yoshida M, Tsai FTF (2003) The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Cell 115:229-240 (Pubitemid 37329586)
    • (2003) Cell , vol.115 , Issue.2 , pp. 229-240
    • Lee, S.1    Sowa, M.E.2    Watanabe, Y.-H.3    Sigler, P.B.4    Chiu, W.5    Yoshida, M.6    Tsai, F.T.F.7
  • 15
    • 77952353727 scopus 로고    scopus 로고
    • CryoEM structure ofHsp104 and its mechanistic implication for protein disaggregation
    • Lee S, SielaffB, Lee J, Tsai FTF (2010) CryoEM structure ofHsp104 and its mechanistic implication for protein disaggregation. Proc Natl Acad Sci USA 107:8135-8140
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 8135-8140
    • Lee, S.1    Sielaffb Lee, J.2    Ftf, T.3
  • 16
    • 38549119467 scopus 로고    scopus 로고
    • Chaperones in control of protein disaggregation
    • DOI 10.1038/sj.emboj.7601970, PII 7601970
    • Liberek K, Lewandowska A, Zitkiewicz S (2008) Chaperones in control of protein disaggregation. EMBO J 27:328-335 (Pubitemid 351161659)
    • (2008) EMBO Journal , vol.27 , Issue.2 , pp. 328-335
    • Liberek, K.1    Lewandowska, A.2    Zietkiewicz, S.3
  • 17
    • 27144474906 scopus 로고    scopus 로고
    • Rebuilt AAA+ motors reveal operating principles for ATP-fuelled machines
    • DOI 10.1038/nature04031, PII N04031
    • Martin A, Baker T, Sauer RT (2005) Rebuilt AAA+ motors reveal operating principles for ATP-fuelled machines. Nature 437:1115-1120 (Pubitemid 41509343)
    • (2005) Nature , vol.437 , Issue.7062 , pp. 1115-1120
    • Martin, A.1    Baker, T.A.2    Sauer, R.T.3
  • 18
    • 0033573135 scopus 로고    scopus 로고
    • Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB
    • Mogk A, Tomoyasu T, Goloubinoff P, Rüdiger S, Röder D, Langen H, Bukau B (1999) Identification ofthermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J 18:6934-6949 (Pubitemid 30000447)
    • (1999) EMBO Journal , vol.18 , Issue.24 , pp. 6934-6949
    • Mogk, A.1    Tomoyasu, T.2    Goloubinoff, P.3    Rudiger, S.4    Roder, D.5    Langen, H.6    Bukau, B.7
  • 19
    • 0037705402 scopus 로고    scopus 로고
    • Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity
    • DOI 10.1074/jbc.M209686200
    • Mogk A, Schlieker C, Strub C, Rist W, Weibezahn J, Bukau B (2003) Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity. J Biol Chem 278:17615-17624 (Pubitemid 36799363)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.20 , pp. 17615-17624
    • Mogk, A.1    Schlieker, C.2    Strub, C.3    Rist, W.4    Weibezahn, J.5    Bukau, B.6
  • 21
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell DA, Kowal AS, Singer MA, Lindquist S (1994a) Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372:475-478
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 22
    • 0027981247 scopus 로고
    • Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes
    • Parsell DA, Kowal AS, Lindquist S (1994b) Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes. J Biol Chem 269:4480-4487
    • (1994) J Biol Chem , vol.269 , pp. 4480-4487
    • Parsell, D.A.1    Kowal, A.S.2    Lindquist, S.3
  • 23
    • 0035822538 scopus 로고    scopus 로고
    • 2+ -linked oligomerization modulates the catalytic activity of the Lon (La) protease from Mycobacterium smegmatis
    • DOI 10.1021/bi0102508
    • Rudyak SG, Brenowitz M, Shrader TE (2001) Mg2+-linked oligomer- ization modulates the catalytic activity of the Lon (La) protease fromMycobacterium smegmatis. Biochemistry 40:9317-9323 (Pubitemid 32730053)
    • (2001) Biochemistry , vol.40 , Issue.31 , pp. 9317-9323
    • Rudyak, S.G.1    Brenowitz, M.2    Shrader, T.E.3
  • 24
    • 0025193343 scopus 로고
    • HSP104 required for induced thermo- tolerance
    • Sanchez Y Lindquist S (1990) HSP104 required for induced thermo- tolerance. Science 248:1112-1115
    • (1990) Science , vol.248 , pp. 1112-1115
    • Sanchez, Y.1    Lindquist, S.2
  • 26
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman F (1991) Getting started with yeast. Methods Enzymol 194:3-21
    • (1991) Methods Enzymol , vol.194 , pp. 3-21
    • Sherman, F.1
  • 27
    • 0033969457 scopus 로고    scopus 로고
    • Rnq1: An epigenetic modifier of protein function in yeast
    • Sondheimer N, Lindquist S (2000) Rnq1: an epigenetic modifier of protein function in yeast. Mol Cell 5:163-172 (Pubitemid 30105445)
    • (2000) Molecular Cell , vol.5 , Issue.1 , pp. 163-172
    • Sondheimer, N.1    Lindquist, S.2
  • 28
    • 0025799542 scopus 로고
    • ClpB is the Escherichia coli heat shock protein F84.1
    • Squires CL, Pendersen S, Ross B, 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    Pendersen, S.2    Ross, B.3    Squires, C.4
  • 29
    • 0019604156 scopus 로고
    • Agents that cause a high frequency ofgenetic change from [psi+] to [psi-] in Saccharomyces cerevisiae
    • Tuite MF, Mundy CR, Cox BS (1981) Agents that cause a high frequency ofgenetic change from [psi+] to [psi-] in Saccharomyces cerevisiae. Genetics 98:691-711
    • (1981) Genetics , vol.98 , pp. 691-711
    • Tuite, M.F.1    Mundy, C.R.2    Cox, B.S.3
  • 30
    • 0034632063 scopus 로고    scopus 로고
    • AAA proteins. Lords of the ring
    • Vale RD (2000) AAA proteins. Lords of the ring. J Cell Biol 150:F13-F19
    • (2000) J Cell Biol , vol.150
    • Vale, R.D.1
  • 31
    • 0037155139 scopus 로고    scopus 로고
    • Roles of the two ATP binding sites of ClpB from Thermus thermophilus
    • DOI 10.1074/jbc.M109349200
    • Watanabe Y, Motohashi K, Yoshida M (2002) Roles of the two ATP binding sites of ClpB from Thermus thermophilus. J Biol Chem 277:5804-5809 (Pubitemid 34968358)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.8 , pp. 5804-5809
    • Watanabe, Y.-H.1    Motohashi, K.2    Yoshida, M.3
  • 33
    • 0042858475 scopus 로고    scopus 로고
    • Characterization of a trap mutant of the AAA+ chaperone ClpB
    • DOI 10.1074/jbc.M303653200
    • 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 (Pubitemid 37055699)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.35 , pp. 32608-32617
    • Weibezahn, J.1    Schlieker, C.2    Bukau, B.3    Mogk, A.4
  • 35
    • 0028308104 scopus 로고
    • [URE3] as an altered URE2 protein: Evidence for a prion analog in Saccharomyces cerevisiae
    • Wickner RB (1994) [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264:566-569 (Pubitemid 24185861)
    • (1994) Science , vol.264 , Issue.5158 , pp. 566-569
    • Wickner, R.B.1
  • 36
    • 0001592716 scopus 로고
    • The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase
    • Woo KM, Kim KI, Goldberg AL, Ha DB, Chung CH (1992) The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase. J Biol Chem 267:20429-20434
    • (1992) J Biol Chem , vol.267 , pp. 20429-20434
    • Woo, K.M.1    Kim, K.I.2    Goldberg, A.L.3    Ha, D.B.4    Chung, C.H.5
  • 37
    • 0028921261 scopus 로고
    • The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates
    • Ziegelhoffer T, Lopes-Buesa P, Craig EA (1995) The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J Biol Chem 270:10412-10419
    • (1995) J Biol Chem , vol.270 , pp. 10412-10419
    • Ziegelhoffer, T.1    Lopes-Buesa, P.2    Craig, E.A.3
  • 38
    • 7244247277 scopus 로고    scopus 로고
    • Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation
    • DOI 10.1074/jbc.M402405200
    • Zitkiewicz S, Krzewska J, Liberek K (2004) Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation. J Biol Chem 279:44376-44383 (Pubitemid 39430842)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.43 , pp. 44376-44383
    • Zietkiewicz, S.1    Krzewska, J.2    Liberek, K.3
  • 39
    • 33646354916 scopus 로고    scopus 로고
    • Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation
    • DOI 10.1074/jbc.M507893200
    • Zitkiewicz 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 (Pubitemid 43847465)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.11 , pp. 7022-7029
    • Zietkiewicz, S.1    Lewandowska, A.2    Stocki, P.3    Liberek, K.4
  • 40
    • 73649102024 scopus 로고    scopus 로고
    • Conformational stability of the full-atom hexameric model of the ClpB chaperone from Escherichia coli
    • Zitkiewicz S, Ślusarz MJ, Ślusarz R, Liberek K, Rodziewicz-Motowidło S (2010) Conformational stability of the full-atom hexameric model of the ClpB chaperone from Escherichia coli. Biopolymers 93:47-60
    • (2010) Biopolymers , vol.93 , pp. 47-60
    • Zitkiewicz, S.1    Ślusarz, M.J.2    Ślusarz, R.3    Liberek, K.4    Rodziewicz-Motowidło, S.5
  • 41
    • 0024316732 scopus 로고
    • Initiation of λ DNA replication with purified host- and bacteriophage-encoded proteins: The role of the dnaK, dnaJ and grpE heat shock proteins
    • Zylicz M, Ang D, Liberek K, Georgopoulos C (1989) Initiation of lambda DNA replication with purified host- and bacteriophage-encoded proteins: the role of the dnaK, dnaJ and grpE heat shock proteins. EMBO J 8:1601-1608 (Pubitemid 19274387)
    • (1989) EMBO Journal , vol.8 , Issue.5 , pp. 1601-1608
    • Zylicz, M.1    Ang, D.2    Liberek, K.3    Georgopoulos, C.4


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