메뉴 건너뛰기




Volumn 423, Issue 3, 2012, Pages 462-471

From a ratchet mechanism to random fluctuations evolution of Hsp90's mechanochemical cycle

Author keywords

chaperone; FRET; Hsp90; HtpG; single molecule

Indexed keywords

HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 90; HTPG PROTEIN; NUCLEOTIDE; UNCLASSIFIED DRUG;

EID: 84867051420     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.07.026     Document Type: Article
Times cited : (44)

References (26)
  • 2
    • 77955506092 scopus 로고    scopus 로고
    • Gymnastics of molecular chaperones
    • M.P. Mayer Gymnastics of molecular chaperones Mol. Cell 39 2010 321 331
    • (2010) Mol. Cell , vol.39 , pp. 321-331
    • Mayer, M.P.1
  • 4
    • 41149111451 scopus 로고    scopus 로고
    • The Hsp90 molecular chaperone: An open and shut case for treatment
    • L.H. Pearl, C. Prodromou, and P. Workman The Hsp90 molecular chaperone: an open and shut case for treatment Biochem. J. 410 2008 439 453
    • (2008) Biochem. J. , vol.410 , pp. 439-453
    • Pearl, L.H.1    Prodromou, C.2    Workman, P.3
  • 6
    • 33746660802 scopus 로고    scopus 로고
    • Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organisms
    • B. Chen, D.B. Zhong, and A. Monteiro Comparative genomics and evolution of the HSP90 family of genes across all kingdoms of organisms BMC Genomics 7 2006 19
    • (2006) BMC Genomics , vol.7 , pp. 19
    • Chen, B.1    Zhong, D.B.2    Monteiro, A.3
  • 7
    • 61949349758 scopus 로고    scopus 로고
    • Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90
    • M. Hessling, K. Richter, and J. Buchner Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90 Nat. Struct. Mol. Biol. 16 2009 287 293
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 287-293
    • Hessling, M.1    Richter, K.2    Buchner, J.3
  • 8
    • 61949212626 scopus 로고    scopus 로고
    • The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis
    • M. Mickler, M. Hessling, C. Ratzke, J. Buchner, and T. Hugel The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis Nat. Struct. Mol. Biol. 16 2009 281 286
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 281-286
    • Mickler, M.1    Hessling, M.2    Ratzke, C.3    Buchner, J.4    Hugel, T.5
  • 9
    • 77958005847 scopus 로고    scopus 로고
    • Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle
    • C. Ratzke, M. Mickler, B. Hellenkamp, J. Buchner, and T. Hugel Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle Proc. Natl Acad. Sci. USA 107 2010 16101 16106
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 16101-16106
    • Ratzke, C.1    Mickler, M.2    Hellenkamp, B.3    Buchner, J.4    Hugel, T.5
  • 10
    • 33750008686 scopus 로고    scopus 로고
    • Structural analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements
    • A.K. Shiau, S.F. Harris, D.R. Southworth, and D.A. Agard Structural analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements Cell 127 2006 329 340
    • (2006) Cell , vol.127 , pp. 329-340
    • Shiau, A.K.1    Harris, S.F.2    Southworth, D.R.3    Agard, D.A.4
  • 11
    • 62049084010 scopus 로고    scopus 로고
    • Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine
    • C. Graf, M. Stankiewicz, G. Kramer, and M.P. Mayer Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine EMBO J. 28 2009 602 613
    • (2009) EMBO J. , vol.28 , pp. 602-613
    • Graf, C.1    Stankiewicz, M.2    Kramer, G.3    Mayer, M.P.4
  • 12
    • 33749983958 scopus 로고    scopus 로고
    • Hsp90: Twist and fold
    • K. Richter, and J. Buchner Hsp90: twist and fold Cell 127 2006 251 253
    • (2006) Cell , vol.127 , pp. 251-253
    • Richter, K.1    Buchner, J.2
  • 13
    • 36849083947 scopus 로고    scopus 로고
    • Dimerization of Hsp90 is required for in vivo function. Design and analysis of monomers and dimers
    • N. Wayne, and D.N. Bolon Dimerization of Hsp90 is required for in vivo function. Design and analysis of monomers and dimers. J. Biol. Chem. 282 2007 35386 35395
    • (2007) J. Biol. Chem. , vol.282 , pp. 35386-35395
    • Wayne, N.1    Bolon, D.N.2
  • 15
    • 84856022421 scopus 로고    scopus 로고
    • Hsp90's mechano-chemical cycle is dominated by thermal fluctuations
    • C. Ratzke, F. Berkemeier, and T. Hugel Hsp90's mechano-chemical cycle is dominated by thermal fluctuations Proc. Natl Acad. Sci. USA 109 2012 161
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 161
    • Ratzke, C.1    Berkemeier, F.2    Hugel, T.3
  • 16
    • 42949147146 scopus 로고    scopus 로고
    • Multiple conformations of E. coli Hsp90 in solution: Insights into the conformational dynamics of Hsp90
    • K.A. Krukenberg, F. Forster, L.M. Rice, A. Sali, and D.A. Agard Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90 Structure 16 2008 755 765
    • (2008) Structure , vol.16 , pp. 755-765
    • Krukenberg, K.A.1    Forster, F.2    Rice, L.M.3    Sali, A.4    Agard, D.A.5
  • 17
    • 13444291091 scopus 로고    scopus 로고
    • Three-color single-molecule fluorescence resonance energy transfer
    • J.P. Clamme, and A.A. Deniz Three-color single-molecule fluorescence resonance energy transfer ChemPhysChem 6 2005 74 77
    • (2005) ChemPhysChem , vol.6 , pp. 74-77
    • Clamme, J.P.1    Deniz, A.A.2
  • 18
    • 70350488396 scopus 로고    scopus 로고
    • SSB protein diffusion on single-stranded DNA stimulates RecA filament formation
    • R. Roy, A.G. Kozlov, T.M. Lohman, and T. Ha SSB protein diffusion on single-stranded DNA stimulates RecA filament formation Nature 461 2009 1092 1097
    • (2009) Nature , vol.461 , pp. 1092-1097
    • Roy, R.1    Kozlov, A.G.2    Lohman, T.M.3    Ha, T.4
  • 19
    • 33646176246 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex
    • M.M. Ali, S.M. Roe, C.K. Vaughan, P. Meyer, B. Panaretou, and P.W. Piper Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex Nature 440 2006 1013 1017
    • (2006) Nature , vol.440 , pp. 1013-1017
    • Ali, M.M.1    Roe, S.M.2    Vaughan, C.K.3    Meyer, P.4    Panaretou, B.5    Piper, P.W.6
  • 22
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • W.J. Netzer, and F.U. Hartl Recombination of protein domains facilitated by co-translational folding in eukaryotes Nature 388 1997 343 349
    • (1997) Nature , vol.388 , pp. 343-349
    • Netzer, W.J.1    Hartl, F.U.2
  • 23
    • 79953308070 scopus 로고    scopus 로고
    • Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone
    • T.O. Street, L.A. Lavery, and D.A. Agard Substrate binding drives large-scale conformational changes in the Hsp90 molecular chaperone Mol. Cell 42 2011 96 105
    • (2011) Mol. Cell , vol.42 , pp. 96-105
    • Street, T.O.1    Lavery, L.A.2    Agard, D.A.3
  • 24
    • 0037593900 scopus 로고    scopus 로고
    • Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone
    • G.P. Lotz, H. Lin, A. Harst, and W.M. Obermann Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone J. Biol. Chem. 278 2003 17228 17235
    • (2003) J. Biol. Chem. , vol.278 , pp. 17228-17235
    • Lotz, G.P.1    Lin, H.2    Harst, A.3    Obermann, W.M.4
  • 25
    • 4444291743 scopus 로고    scopus 로고
    • The co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle
    • K. Richter, S. Walter, and J. Buchner The co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle J. Mol. Biol. 342 2004 1403 1413
    • (2004) J. Mol. Biol. , vol.342 , pp. 1403-1413
    • Richter, K.1    Walter, S.2    Buchner, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.