메뉴 건너뛰기




Volumn 48, Issue 6, 2012, Pages 863-874

Structure and Dynamics of the ATP-Bound Open Conformation of Hsp70 Chaperones

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; HEAT SHOCK PROTEIN 70; NUCLEOTIDE; PROTEIN DNAK;

EID: 84871689599     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2012.09.023     Document Type: Article
Times cited : (329)

References (40)
  • 1
    • 0042204157 scopus 로고    scopus 로고
    • Role of region C in regulation of the heat shock gene-specific sigma factor of Escherichia coli, sigma32
    • Arsène F., Tomoyasu T., Mogk A., Schirra C., Schulze-Specking A., Bukau B. Role of region C in regulation of the heat shock gene-specific sigma factor of Escherichia coli, sigma32. J. Bacteriol. 1999, 181:3552-3561.
    • (1999) J. Bacteriol. , vol.181 , pp. 3552-3561
    • Arsène, F.1    Tomoyasu, T.2    Mogk, A.3    Schirra, C.4    Schulze-Specking, A.5    Bukau, B.6
  • 2
    • 0034837025 scopus 로고    scopus 로고
    • ATPase-defective derivatives of Escherichia coli DnaK that behave differently with respect to ATP-induced conformational change and peptide release
    • Barthel T.K., Zhang J., Walker G.C. ATPase-defective derivatives of Escherichia coli DnaK that behave differently with respect to ATP-induced conformational change and peptide release. J. Bacteriol. 2001, 183:5482-5490.
    • (2001) J. Bacteriol. , vol.183 , pp. 5482-5490
    • Barthel, T.K.1    Zhang, J.2    Walker, G.C.3
  • 3
    • 64649094781 scopus 로고    scopus 로고
    • Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate
    • Bertelsen E.B., Chang L., Gestwicki J.E., Zuiderweg E.R.P. Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate. Proc. Natl. Acad. Sci. USA 2009, 106:8471-8476.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 8471-8476
    • Bertelsen, E.B.1    Chang, L.2    Gestwicki, J.E.3    Zuiderweg, E.R.P.4
  • 4
    • 0028297010 scopus 로고
    • The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171
    • Buchberger A., Valencia A., McMacken R., Sander C., Bukau B. The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171. EMBO J. 1994, 13:1687-1695.
    • (1994) EMBO J. , vol.13 , pp. 1687-1695
    • Buchberger, A.1    Valencia, A.2    McMacken, R.3    Sander, C.4    Bukau, B.5
  • 6
    • 0025048776 scopus 로고
    • Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone
    • Bukau B., Walker G.C. Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone. EMBO J. 1990, 9:4027-4036.
    • (1990) EMBO J. , vol.9 , pp. 4027-4036
    • Bukau, B.1    Walker, G.C.2
  • 7
    • 33745762927 scopus 로고    scopus 로고
    • Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
    • Dragovic Z., Broadley S.A., Shomura Y., Bracher A., Hartl F.U. Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J. 2006, 25:2519-2528.
    • (2006) EMBO J. , vol.25 , pp. 2519-2528
    • Dragovic, Z.1    Broadley, S.A.2    Shomura, Y.3    Bracher, A.4    Hartl, F.U.5
  • 8
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • Flaherty K.M., DeLuca-Flaherty C., McKay D.B. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 1990, 346:623-628.
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1    DeLuca-Flaherty, C.2    McKay, D.B.3
  • 9
    • 0028240468 scopus 로고
    • Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment
    • Flaherty K.M., Wilbanks S.M., DeLuca-Flaherty C., McKay D.B. Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment. J. Biol. Chem. 1994, 269:12899-12907.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12899-12907
    • Flaherty, K.M.1    Wilbanks, S.M.2    DeLuca-Flaherty, C.3    McKay, D.B.4
  • 10
    • 0035980016 scopus 로고    scopus 로고
    • Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor
    • Gässler C.S., Wiederkehr T., Brehmer D., Bukau B., Mayer M.P. Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor. J. Biol. Chem. 2001, 276:32538-32544.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32538-32544
    • Gässler, C.S.1    Wiederkehr, T.2    Brehmer, D.3    Bukau, B.4    Mayer, M.P.5
  • 11
    • 62049084010 scopus 로고    scopus 로고
    • Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine
    • Graf C., Stankiewicz M., Kramer G., Mayer M.P. Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine. EMBO J. 2009, 28:602-613.
    • (2009) EMBO J. , vol.28 , pp. 602-613
    • Graf, C.1    Stankiewicz, M.2    Kramer, G.3    Mayer, M.P.4
  • 12
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl F.U., Bracher A., Hayer-Hartl M. Molecular chaperones in protein folding and proteostasis. Nature 2011, 475:324-332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 13
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: J proteins as drivers of functional specificity
    • Kampinga H.H., Craig E.A. The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat. Rev. Mol. Cell Biol. 2010, 11:579-592.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 14
    • 15844372190 scopus 로고    scopus 로고
    • A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein
    • Karzai A.W., McMacken R. A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein. J. Biol. Chem. 1996, 271:11236-11246.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11236-11246
    • Karzai, A.W.1    McMacken, R.2
  • 15
    • 0025888264 scopus 로고
    • Efficient site-directed mutagenesis using uracil-containing DNA
    • Kunkel T.A., Bebenek K., McClary J. Efficient site-directed mutagenesis using uracil-containing DNA. Methods Enzymol. 1991, 204:125-139.
    • (1991) Methods Enzymol. , vol.204 , pp. 125-139
    • Kunkel, T.A.1    Bebenek, K.2    McClary, J.3
  • 17
    • 34848869936 scopus 로고    scopus 로고
    • Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1
    • Liu Q., Hendrickson W.A. Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1. Cell 2007, 131:106-120.
    • (2007) Cell , vol.131 , pp. 106-120
    • Liu, Q.1    Hendrickson, W.A.2
  • 18
    • 79551632223 scopus 로고    scopus 로고
    • Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions
    • Marcinowski M., Höller M., Feige M.J., Baerend D., Lamb D.C., Buchner J. Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Nat. Struct. Mol. Biol. 2011, 18:150-158.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 150-158
    • Marcinowski, M.1    Höller, M.2    Feige, M.J.3    Baerend, D.4    Lamb, D.C.5    Buchner, J.6
  • 19
    • 0029100702 scopus 로고
    • A new set of useful cloning and expression vectors derived from pBlueScript
    • Mayer M.P. A new set of useful cloning and expression vectors derived from pBlueScript. Gene 1995, 163:41-46.
    • (1995) Gene , vol.163 , pp. 41-46
    • Mayer, M.P.1
  • 20
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: cellular functions and molecular mechanism
    • Mayer M.P., Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci. 2005, 62:670-684.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 21
    • 0033020519 scopus 로고    scopus 로고
    • Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy
    • Mayer M.P., Laufen T., Paal K., McCarty J.S., Bukau B. Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy. J. Mol. Biol. 1999, 289:1131-1144.
    • (1999) J. Mol. Biol. , vol.289 , pp. 1131-1144
    • Mayer, M.P.1    Laufen, T.2    Paal, K.3    McCarty, J.S.4    Bukau, B.5
  • 22
    • 0033783190 scopus 로고    scopus 로고
    • Molecular basis for interactions of the DnaK chaperone with substrates
    • Mayer M.P., Rüdiger S., Bukau B. Molecular basis for interactions of the DnaK chaperone with substrates. Biol. Chem. 2000, 381:877-885.
    • (2000) Biol. Chem. , vol.381 , pp. 877-885
    • Mayer, M.P.1    Rüdiger, S.2    Bukau, B.3
  • 24
    • 0029013908 scopus 로고
    • The role of ATP in the functional cycle of the DnaK chaperone system
    • McCarty J.S., Buchberger A., Reinstein J., Bukau B. The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol. 1995, 249:126-137.
    • (1995) J. Mol. Biol. , vol.249 , pp. 126-137
    • McCarty, J.S.1    Buchberger, A.2    Reinstein, J.3    Bukau, B.4
  • 25
    • 0037413822 scopus 로고    scopus 로고
    • Interdomain interaction through helices A and B of DnaK peptide binding domain
    • Moro F., Fernández V., Muga A. Interdomain interaction through helices A and B of DnaK peptide binding domain. FEBS Lett. 2003, 533:119-123.
    • (2003) FEBS Lett. , vol.533 , pp. 119-123
    • Moro, F.1    Fernández, V.2    Muga, A.3
  • 26
    • 0033598667 scopus 로고    scopus 로고
    • Importance of F1-ATPase residue alpha-Arg-376 for catalytic transition state stabilization
    • Nadanaciva S., Weber J., Wilke-Mounts S., Senior A.E. Importance of F1-ATPase residue alpha-Arg-376 for catalytic transition state stabilization. Biochemistry 1999, 38:15493-15499.
    • (1999) Biochemistry , vol.38 , pp. 15493-15499
    • Nadanaciva, S.1    Weber, J.2    Wilke-Mounts, S.3    Senior, A.E.4
  • 27
    • 0030018744 scopus 로고    scopus 로고
    • Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis
    • O'Brien M.C., Flaherty K.M., McKay D.B. Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis. J. Biol. Chem. 1996, 271:15874-15878.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15874-15878
    • O'Brien, M.C.1    Flaherty, K.M.2    McKay, D.B.3
  • 28
    • 0032564386 scopus 로고    scopus 로고
    • Sequence-specific rates of interaction of target peptides with the molecular chaperones DnaK and DnaJ
    • Pierpaoli E.V., Gisler S.M., Christen P. Sequence-specific rates of interaction of target peptides with the molecular chaperones DnaK and DnaJ. Biochemistry 1998, 37:16741-16748.
    • (1998) Biochemistry , vol.37 , pp. 16741-16748
    • Pierpaoli, E.V.1    Gisler, S.M.2    Christen, P.3
  • 29
    • 33745749328 scopus 로고    scopus 로고
    • Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor
    • Raviol H., Sadlish H., Rodriguez F., Mayer M.P., Bukau B. Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J. 2006, 25:2510-2518.
    • (2006) EMBO J. , vol.25 , pp. 2510-2518
    • Raviol, H.1    Sadlish, H.2    Rodriguez, F.3    Mayer, M.P.4    Bukau, B.5
  • 30
    • 33745183353 scopus 로고    scopus 로고
    • Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation
    • Rist W., Graf C., Bukau B., Mayer M.P. Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation. J. Biol. Chem. 2006, 281:16493-16501.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16493-16501
    • Rist, W.1    Graf, C.2    Bukau, B.3    Mayer, M.P.4
  • 32
    • 79952364237 scopus 로고    scopus 로고
    • Mechanics of Hsp70 chaperones enables differential interaction with client proteins
    • Schlecht R., Erbse A.H., Bukau B., Mayer M.P. Mechanics of Hsp70 chaperones enables differential interaction with client proteins. Nat. Struct. Mol. Biol. 2011, 18:345-351.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 345-351
    • Schlecht, R.1    Erbse, A.H.2    Bukau, B.3    Mayer, M.P.4
  • 33
  • 35
    • 34047268015 scopus 로고    scopus 로고
    • Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker
    • Swain J.F., Dinler G., Sivendran R., Montgomery D.L., Stotz M., Gierasch L.M. Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker. Mol. Cell 2007, 26:27-39.
    • (2007) Mol. Cell , vol.26 , pp. 27-39
    • Swain, J.F.1    Dinler, G.2    Sivendran, R.3    Montgomery, D.L.4    Stotz, M.5    Gierasch, L.M.6
  • 37
    • 33846020582 scopus 로고    scopus 로고
    • Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker
    • Vogel M., Mayer M.P., Bukau B. Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker. J. Biol. Chem. 2006, 281:38705-38711.
    • (2006) J. Biol. Chem. , vol.281 , pp. 38705-38711
    • Vogel, M.1    Mayer, M.P.2    Bukau, B.3
  • 38
    • 0028938819 scopus 로고
    • How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site
    • Wilbanks S.M., McKay D.B. How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site. J. Biol. Chem. 1995, 270:2251-2257.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2251-2257
    • Wilbanks, S.M.1    McKay, D.B.2
  • 39
    • 0028287525 scopus 로고
    • Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants
    • Wilbanks S.M., DeLuca-Flaherty C., McKay D.B. Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants. J. Biol. Chem. 1994, 269:12893-12898.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12893-12898
    • Wilbanks, S.M.1    DeLuca-Flaherty, C.2    McKay, D.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.