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Volumn 34, Issue 1, 2009, Pages 81-92

Motor Mechanism for Protein Threading through Hsp104

Author keywords

PROTEINS

Indexed keywords

ADENOSINE 5' O (3 THIOTRIPHOSPHATE); ADENOSINE TRIPHOSPHATE; BINDING PROTEIN; HEAT SHOCK PROTEIN 104; PROTEIN NBD1; PROTEIN NBD2; TYROSINE; UNCLASSIFIED DRUG;

EID: 63849263045     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2009.02.026     Document Type: Article
Times cited : (81)

References (44)
  • 1
    • 27844460608 scopus 로고    scopus 로고
    • Biochemical coupling of the two nucleotide binding domains of ClpB: Covalent linkage is not a prerequisite for chaperone activity
    • Beinker P., Schlee S., Auvula R., and Reinstein J. Biochemical coupling of the two nucleotide binding domains of ClpB: Covalent linkage is not a prerequisite for chaperone activity. J. Biol. Chem. 280 (2005) 37965-37973
    • (2005) J. Biol. Chem. , vol.280 , pp. 37965-37973
    • Beinker, P.1    Schlee, S.2    Auvula, R.3    Reinstein, J.4
  • 4
    • 5344266886 scopus 로고    scopus 로고
    • Nucleotide-dependent substrate handoff from the SspB adaptor to the AAA+ ClpXP protease
    • Bolon D.N., Grant R.A., Baker T.A., and Sauer R.T. Nucleotide-dependent substrate handoff from the SspB adaptor to the AAA+ ClpXP protease. Mol. Cell 16 (2004) 343-350
    • (2004) Mol. Cell , vol.16 , pp. 343-350
    • Bolon, D.N.1    Grant, R.A.2    Baker, T.A.3    Sauer, R.T.4
  • 5
    • 31444442284 scopus 로고    scopus 로고
    • Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides
    • Bosl B., Grimminger V., and Walter S. Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides. J. Biol. Chem. 280 (2005) 38170-38176
    • (2005) J. Biol. Chem. , vol.280 , pp. 38170-38176
    • Bosl, B.1    Grimminger, V.2    Walter, S.3
  • 6
    • 46649111025 scopus 로고    scopus 로고
    • Analysis of nucleotide binding to P97 reveals the properties of a tandem AAA hexameric ATPase
    • Briggs L.C., Baldwin G.S., Miyata N., Kondo H., Zhang X., and Freemont P.S. Analysis of nucleotide binding to P97 reveals the properties of a tandem AAA hexameric ATPase. J. Biol. Chem. 283 (2008) 13745-13752
    • (2008) J. Biol. Chem. , vol.283 , pp. 13745-13752
    • Briggs, L.C.1    Baldwin, G.S.2    Miyata, N.3    Kondo, H.4    Zhang, X.5    Freemont, P.S.6
  • 7
    • 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. 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 (2002) 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
  • 9
    • 0141507032 scopus 로고    scopus 로고
    • Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains
    • DeLaBarre B., and Brunger A.T. Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains. Nat. Struct. Biol. 10 (2003) 856-863
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 856-863
    • DeLaBarre, B.1    Brunger, A.T.2
  • 10
    • 14644415865 scopus 로고    scopus 로고
    • Nucleotide dependent motion and mechanism of action of p97/VCP
    • DeLaBarre B., and Brunger A.T. Nucleotide dependent motion and mechanism of action of p97/VCP. J. Mol. Biol. 347 (2005) 437-452
    • (2005) J. Mol. Biol. , vol.347 , pp. 437-452
    • DeLaBarre, B.1    Brunger, A.T.2
  • 12
    • 33745041480 scopus 로고    scopus 로고
    • Evolutionary relationships and structural mechanisms of AAA+ proteins
    • Erzberger J.P., and Berger J.M. Evolutionary relationships and structural mechanisms of AAA+ proteins. Annu. Rev. Biophys. Biomol. Struct. 35 (2006) 93-114
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 93-114
    • Erzberger, J.P.1    Berger, J.M.2
  • 13
    • 4444226952 scopus 로고    scopus 로고
    • Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen
    • Gai D., Zhao R., Li D., Finkielstein C.V., and Chen X.S. Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen. Cell 119 (2004) 47-60
    • (2004) Cell , vol.119 , pp. 47-60
    • Gai, D.1    Zhao, R.2    Li, D.3    Finkielstein, C.V.4    Chen, X.S.5
  • 15
    • 44849138934 scopus 로고    scopus 로고
    • Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments
    • Haslberger T., Zdanowicz A., Brand I., Kirstein J., Turgay K., Mogk A., and Bukau B. Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments. Nat. Struct. Mol. Biol. 15 (2008) 641-650
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 641-650
    • Haslberger, T.1    Zdanowicz, A.2    Brand, I.3    Kirstein, J.4    Turgay, K.5    Mogk, A.6    Bukau, B.7
  • 16
    • 0037080611 scopus 로고    scopus 로고
    • Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants
    • Hattendorf D.A., and Lindquist S.L. Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants. EMBO J. 21 (2002) 12-21
    • (2002) EMBO J. , vol.21 , pp. 12-21
    • Hattendorf, D.A.1    Lindquist, S.L.2
  • 17
    • 21244482459 scopus 로고    scopus 로고
    • Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: Allosteric control of a protein machine
    • Hersch G.L., Burton R.E., Bolon D.N., Baker T.A., and Sauer R.T. Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: Allosteric control of a protein machine. Cell 121 (2005) 1017-1027
    • (2005) Cell , vol.121 , pp. 1017-1027
    • Hersch, G.L.1    Burton, R.E.2    Bolon, D.N.3    Baker, T.A.4    Sauer, R.T.5
  • 18
    • 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., and Horwich A.L. Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation. Cell 121 (2005) 1029-1041
    • (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
  • 19
    • 34547963061 scopus 로고    scopus 로고
    • ATP-induced structural transitions in PAN, the proteasome-regulatory ATPase complex in Archaea
    • Horwitz A.A., Navon A., Groll M., Smith D.M., Reis C., and Goldberg A.L. ATP-induced structural transitions in PAN, the proteasome-regulatory ATPase complex in Archaea. J. Biol. Chem. 282 (2007) 22921-22929
    • (2007) J. Biol. Chem. , vol.282 , pp. 22921-22929
    • Horwitz, A.A.1    Navon, A.2    Groll, M.3    Smith, D.M.4    Reis, C.5    Goldberg, A.L.6
  • 20
    • 33745419772 scopus 로고    scopus 로고
    • N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression
    • Hung G.C., and Masison D.C. N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression. Genetics 173 (2006) 611-620
    • (2006) Genetics , vol.173 , pp. 611-620
    • Hung, G.C.1    Masison, D.C.2
  • 21
    • 1242345623 scopus 로고    scopus 로고
    • The N-terminal substrate-binding domain of ClpA unfoldase is highly mobile and extends axially from the distal surface of ClpAP protease
    • Ishikawa T., Maurizi M.R., and Steven A.C. The N-terminal substrate-binding domain of ClpA unfoldase is highly mobile and extends axially from the distal surface of ClpAP protease. J. Struct. Biol. 146 (2004) 180-188
    • (2004) J. Struct. Biol. , vol.146 , pp. 180-188
    • Ishikawa, T.1    Maurizi, M.R.2    Steven, A.C.3
  • 22
    • 33947290033 scopus 로고    scopus 로고
    • Channel mutations in Hsp104 hexamer distinctively affect thermotolerance and prion-specific propagation
    • Kurahashi H., and Nakamura Y. Channel mutations in Hsp104 hexamer distinctively affect thermotolerance and prion-specific propagation. Mol. Microbiol. 63 (2007) 1669-1683
    • (2007) Mol. Microbiol. , vol.63 , pp. 1669-1683
    • Kurahashi, H.1    Nakamura, Y.2
  • 23
    • 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., and Tsai F.T.F. Visualizing the ATPase cycle in a protein disaggregating machine: Structural basis for substrate binding by ClpB. Mol. Cell 25 (2007) 261-271
    • (2007) Mol. Cell , vol.25 , pp. 261-271
    • Lee, S.1    Choi, J.-M.2    Tsai, F.T.F.3
  • 24
    • 0142227208 scopus 로고    scopus 로고
    • The structure of ClpB: A molecular chaperone that rescues proteins from an aggregated state
    • Lee S., Sowa M.E., Watanabe Y.H., Sigler P.B., Chiu W., Yoshida M., and Tsai F.T. The structure of ClpB: A molecular chaperone that rescues proteins from an aggregated state. Cell 115 (2003) 229-240
    • (2003) Cell , vol.115 , 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.7
  • 25
    • 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., and Glover J.R. Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. J. Biol. Chem. 279 (2004) 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
  • 26
    • 57649187079 scopus 로고    scopus 로고
    • Peptide and protein binding in the axial channel of Hsp104. Insights into the mechanism of protein unfolding
    • Lum R., Niggemann M., and Glover J.R. Peptide and protein binding in the axial channel of Hsp104. Insights into the mechanism of protein unfolding. J. Biol. Chem. 283 (2008) 30139-30150
    • (2008) J. Biol. Chem. , vol.283 , pp. 30139-30150
    • Lum, R.1    Niggemann, M.2    Glover, J.R.3
  • 27
    • 27144474906 scopus 로고    scopus 로고
    • Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines
    • Martin A., Baker T.A., and Sauer R.T. Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines. Nature 437 (2005) 1115-1120
    • (2005) Nature , vol.437 , pp. 1115-1120
    • Martin, A.1    Baker, T.A.2    Sauer, R.T.3
  • 28
    • 39549084936 scopus 로고    scopus 로고
    • Diverse pore loops of the AAA+ ClpX machine mediate unassisted and adaptor-dependent recognition of ssrA-tagged substrates
    • Martin A., Baker T.A., and Sauer R.T. Diverse pore loops of the AAA+ ClpX machine mediate unassisted and adaptor-dependent recognition of ssrA-tagged substrates. Mol. Cell 29 (2008) 441-450
    • (2008) Mol. Cell , vol.29 , pp. 441-450
    • Martin, A.1    Baker, T.A.2    Sauer, R.T.3
  • 29
    • 35348971984 scopus 로고    scopus 로고
    • ATPase site architecture and helicase mechanism of an archaeal MCM
    • Moreau M.J., McGeoch A.T., Lowe A.R., Itzhaki L.S., and Bell S.D. ATPase site architecture and helicase mechanism of an archaeal MCM. Mol. Cell 28 (2007) 304-314
    • (2007) Mol. Cell , vol.28 , pp. 304-314
    • Moreau, M.J.1    McGeoch, A.T.2    Lowe, A.R.3    Itzhaki, L.S.4    Bell, S.D.5
  • 30
    • 0033516473 scopus 로고    scopus 로고
    • Concurrent chaperone and protease activities of ClpAP and the requirement for the N-terminal ClpA ATP binding site for chaperone activity
    • Pak M., Hoskins J.R., Singh S.K., Maurizi M.R., and Wickner S. Concurrent chaperone and protease activities of ClpAP and the requirement for the N-terminal ClpA ATP binding site for chaperone activity. J. Biol. Chem. 274 (1999) 19316-19322
    • (1999) J. Biol. Chem. , vol.274 , pp. 19316-19322
    • Pak, M.1    Hoskins, J.R.2    Singh, S.K.3    Maurizi, M.R.4    Wickner, S.5
  • 31
    • 0027981247 scopus 로고
    • Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes
    • Parsell D.A., Kowal A.S., and Lindquist S. Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes. J. Biol. Chem. 269 (1994) 4480-4487
    • (1994) J. Biol. Chem. , vol.269 , pp. 4480-4487
    • Parsell, D.A.1    Kowal, A.S.2    Lindquist, S.3
  • 36
    • 0032546911 scopus 로고    scopus 로고
    • The ATPase activity of Hsp104, effects of environmental conditions and mutations
    • Schirmer E.C., Queitsch C., Kowal A.S., Parsell D.A., and Lindquist S. The ATPase activity of Hsp104, effects of environmental conditions and mutations. J. Biol. Chem. 273 (1998) 15546-15552
    • (1998) J. Biol. Chem. , vol.273 , pp. 15546-15552
    • Schirmer, E.C.1    Queitsch, C.2    Kowal, A.S.3    Parsell, D.A.4    Lindquist, S.5
  • 38
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • Singleton M.R., Sawaya M.R., Ellenberger T., and Wigley D.B. Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell 101 (2000) 589-600
    • (2000) Cell , vol.101 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 39
    • 40649098449 scopus 로고    scopus 로고
    • Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation
    • Tessarz P., Mogk A., and Bukau B. Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation. Mol. Microbiol. 68 (2008) 87-97
    • (2008) Mol. Microbiol. , vol.68 , pp. 87-97
    • Tessarz, P.1    Mogk, A.2    Bukau, B.3
  • 40
    • 0034632063 scopus 로고    scopus 로고
    • AAA proteins. Lords of the ring
    • Vale R.D. AAA proteins. Lords of the ring. J. Cell Biol. 150 (2000) F13-F19
    • (2000) J. Cell Biol. , vol.150
    • Vale, R.D.1
  • 43
    • 37449008520 scopus 로고    scopus 로고
    • Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104
    • Wendler P., Shorter J., Plisson C., Cashikar A.G., Lindquist S., and Saibil H.R. Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104. Cell 131 (2007) 1366-1377
    • (2007) Cell , vol.131 , pp. 1366-1377
    • Wendler, P.1    Shorter, J.2    Plisson, C.3    Cashikar, A.G.4    Lindquist, S.5    Saibil, H.R.6
  • 44
    • 41149169488 scopus 로고    scopus 로고
    • Coupling and dynamics of subunits in the hexameric AAA+ chaperone ClpB
    • Werbeck N.D., Schlee S., and Reinstein J. Coupling and dynamics of subunits in the hexameric AAA+ chaperone ClpB. J. Mol. Biol. 378 (2008) 178-190
    • (2008) J. Mol. Biol. , vol.378 , pp. 178-190
    • Werbeck, N.D.1    Schlee, S.2    Reinstein, J.3


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