메뉴 건너뛰기




Volumn 110, Issue 46, 2013, Pages

Substrate protein switches GroE chaperonins from asymmetric to symmetric cycling by catalyzing nucleotide exchange

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONIN; CHAPERONIN GROEL; CHAPERONIN GROES; NUCLEOTIDE; PI PROTEIN; PROTEIN; SUBSTRATE PROTEIN; UNCLASSIFIED DRUG;

EID: 84887469924     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1317702110     Document Type: Article
Times cited : (55)

References (45)
  • 1
    • 33746265142 scopus 로고    scopus 로고
    • GroEL-mediated protein folding: Making the impossible, possible
    • DOI 10.1080/10409230600760382, PII M315627H22375T33
    • Lin Z, Rye HS (2006) GroEL-mediated protein folding: Making the impossible, possible. Crit Rev Biochem Mol Biol 41(4):211-239. (Pubitemid 44100582)
    • (2006) Critical Reviews in Biochemistry and Molecular Biology , vol.41 , Issue.4 , pp. 211-239
    • Lin, Z.1    Rye, H.2
  • 4
    • 0024820705 scopus 로고
    • Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
    • DOI 10.1038/342884a0
    • Goloubinoff P, Christeller JT, Gatenby AA, Lorimer GH (1989) Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP. Nature 342(6252):884-889. (Pubitemid 20021332)
    • (1989) Nature , vol.342 , Issue.6252 , pp. 884-889
    • Goloubinoff, P.1    Christeller, J.T.2    Gatenby, A.A.3    Lorimer, G.H.4
  • 5
    • 0027943510 scopus 로고
    • The crystal structure of the bacterial chaperonin GroEL at 2.8 A
    • Braig K, et al. (1994) The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Nature 371(6498):578-586.
    • (1994) Nature , vol.371 , Issue.6498 , pp. 578-586
    • Braig, K.1
  • 6
    • 0028885711 scopus 로고
    • Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution
    • Braig K, Adams PD, Brünger AT (1995) Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution. Nat Struct Biol 2(12):1083-1094.
    • (1995) Nat Struct Biol , vol.2 , Issue.12 , pp. 1083-1094
    • Braig, K.1    Adams, P.D.2    Brünger, A.T.3
  • 7
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • DOI 10.1038/41944
    • Xu Z, Horwich AL, Sigler PB (1997) The crystal structure of the asymmetric GroEL-GroES- (ADP)7 chaperonin complex. Nature 388(6644):741-750. (Pubitemid 27375147)
    • (1997) Nature , vol.388 , Issue.6644 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 8
    • 0028031345 scopus 로고
    • Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding
    • Todd MJ, Viitanen PV, Lorimer GH (1994) Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding. Science 265(5172):659-666. (Pubitemid 24268276)
    • (1994) Science , vol.265 , Issue.5172 , pp. 659-666
    • Todd, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 9
    • 0030766287 scopus 로고    scopus 로고
    • Protein folding. Folding with a two-stroke motor
    • Lorimer G (1997) Protein folding. Folding with a two-stroke motor. Nature 388(6644):720-721, 723.
    • (1997) Nature , vol.388 , Issue.6644
    • Lorimer, G.1
  • 10
    • 56249136290 scopus 로고    scopus 로고
    • Setting the chaperonin timer: A two-stroke, two-speed, protein machine
    • Grason JP, Gresham JS, Lorimer GH (2008) Setting the chaperonin timer: A two-stroke, two-speed, protein machine. Proc Natl Acad Sci USA 105(45):17339-17344.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.45 , pp. 17339-17344
    • Grason, J.P.1    Gresham, J.S.2    Lorimer, G.H.3
  • 11
    • 56249100422 scopus 로고    scopus 로고
    • Setting the chaperonin timer: The effects of K+ and substrate protein on ATP hydrolysis
    • Grason JP, Gresham JS, Widjaja L, Wehri SC, Lorimer GH (2008) Setting the chaperonin timer: The effects of K+ and substrate protein on ATP hydrolysis. Proc Natl Acad Sci USA 105(45):17334-17338.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.45 , pp. 17334-17338
    • Grason, J.P.1    Gresham, J.S.2    Widjaja, L.3    Wehri, S.C.4    Lorimer, G.H.5
  • 12
    • 73949133922 scopus 로고    scopus 로고
    • GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state
    • Tyagi NK, Fenton WA, Horwich AL (2009) GroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state. Proc Natl Acad Sci USA 106(48):20264-20269.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.48 , pp. 20264-20269
    • Tyagi, N.K.1    Fenton, W.A.2    Horwich, A.L.3
  • 13
    • 76749127971 scopus 로고    scopus 로고
    • ATP-triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP7 is not the rate-limiting step of the GroEL/GroES reaction cycle
    • Tyagi NK, Fenton WA, Horwich AL (2010) ATP-triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP7 is not the rate-limiting step of the GroEL/GroES reaction cycle. FEBS Lett 584(5):951-953.
    • (2010) FEBS Lett , vol.584 , Issue.5 , pp. 951-953
    • Tyagi, N.K.1    Fenton, W.A.2    Horwich, A.L.3
  • 14
    • 80053999780 scopus 로고    scopus 로고
    • Protein folding in the cell: An inside story
    • Horwich AL (2011) Protein folding in the cell: An inside story. Nat Med 17(10):1211-1216.
    • (2011) Nat Med , vol.17 , Issue.10 , pp. 1211-1216
    • Horwich, A.L.1
  • 15
    • 0029112696 scopus 로고
    • Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes
    • Engel A, et al. (1995) Functional significance of symmetrical versus asymmetrical GroEL-GroES chaperonin complexes. Science 269(5225):832-836.
    • (1995) Science , vol.269 , Issue.5225 , pp. 832-836
    • Engel, A.1
  • 16
    • 0029157195 scopus 로고
    • Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding
    • Hayer-Hartl MK, Martin J, Hartl FU (1995) Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding. Science 269(5225):836-841.
    • (1995) Science , vol.269 , Issue.5225 , pp. 836-841
    • Hayer-Hartl, M.K.1    Martin, J.2    Hartl, F.U.3
  • 17
    • 0032997061 scopus 로고    scopus 로고
    • On the role of symmetrical and asymmetrical chaperonin complexes in assisted protein folding
    • DOI 10.1515/BC.1999.068
    • Hayer-Hartl MK, Ewalt KL, Hartl FU (1999) On the role of symmetrical and asymmetrical chaperonin complexes in assisted protein folding. Biol Chem 380(5):531-540. (Pubitemid 29248441)
    • (1999) Biological Chemistry , vol.380 , Issue.5 , pp. 531-540
    • Hayer-Hartl, M.K.1    Ewalt, K.L.2    Hartl, F.U.3
  • 19
    • 0029583647 scopus 로고
    • The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 hetero-oligomer
    • Azem A, Diamant S, Kessel M, Weiss C, Goloubinoff P (1995) The protein-folding activity of chaperonins correlates with the symmetric GroEL14(GroES7)2 hetero-oligomer. Proc Natl Acad Sci USA 92(26):12021-12025.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.26 , pp. 12021-12025
    • Azem, A.1    Diamant, S.2    Kessel, M.3    Weiss, C.4    Goloubinoff, P.5
  • 20
    • 0028340341 scopus 로고
    • The formation of symmetrical GroEL-GroES complexes in the presence of ATP
    • DOI 10.1016/0014-5793(94)00432-3
    • Llorca O, Marco S, Carrascosa JL, Valpuesta JM (1994) The formation of symmetrical GroEL-GroES complexes in the presence of ATP. FEBS Lett 345(2-3):181-186. (Pubitemid 24188921)
    • (1994) FEBS Letters , vol.345 , Issue.2-3 , pp. 181-186
    • Llorca, O.1    Marco, S.2    Carrascosa, J.L.3    Valpuesta, J.M.4
  • 21
    • 0030902005 scopus 로고    scopus 로고
    • Symmetric GroEL-GroES complexes can contain substrate simultaneously in both GroEL rings
    • DOI 10.1016/S0014-5793(97)00186-5, PII S0014579397001865
    • Llorca O, Marco S, Carrascosa JL, Valpuesta JM (1997) Symmetric GroEL-GroES complexes can contain substrate simultaneously in both GroEL rings. FEBS Lett 405(2):195-199. (Pubitemid 27136510)
    • (1997) FEBS Letters , vol.405 , Issue.2 , pp. 195-199
    • Llorca, O.1    Marco, S.2    Carrascosa, J.L.3    Valpuesta, J.M.4
  • 22
    • 0030334841 scopus 로고    scopus 로고
    • 2 complexes in molecular chaperone activity
    • Corrales FJ, Fersht AR (1996) Kinetic significance of GroEL14.(GroES7)2 complexes in molecular chaperone activity. Fold Des 1(4):265-273. (Pubitemid 126748184)
    • (1996) Folding and Design , vol.1 , Issue.4 , pp. 265-273
    • Corrales, F.J.1    Fersht, A.R.2
  • 24
    • 0032509224 scopus 로고    scopus 로고
    • GroEL traps dimeric and monomeric unfolding intermediates of citrate synthase
    • DOI 10.1074/jbc.273.50.33305
    • Grallert H, Rutkat K, Buchner J (1998) GroEL traps dimeric and monomeric unfolding intermediates of citrate synthase. J Biol Chem 273(50):33305-33310. (Pubitemid 29005706)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.50 , pp. 33305-33310
    • Grallert, H.1    Rutkat, K.2    Buchner, J.3
  • 25
    • 0038933540 scopus 로고    scopus 로고
    • Catalysis, commitment and encapsulation during GroE-mediated folding
    • DOI 10.1006/jmbi.1999.2780
    • Beissinger M, Rutkat K, Buchner J (1999) Catalysis, commitment and encapsulation during GroE-mediated folding. J Mol Biol 289(4):1075-1092. (Pubitemid 29306671)
    • (1999) Journal of Molecular Biology , vol.289 , Issue.4 , pp. 1075-1092
    • Beissinger, M.1    Rutkat, K.2    Buchner, J.3
  • 26
    • 8544241796 scopus 로고    scopus 로고
    • x stops the chaperonin cycle of GroEL-GroES and generates a complex with double folding chambers
    • DOI 10.1074/jbc.M406795200
    • Taguchi H, Tsukuda K, Motojima F, Koike-Takeshita A, Yoshida M (2004) BeF(x) stops the chaperonin cycle of GroEL-GroES and generates a complex with double folding chambers. J Biol Chem 279(44):45737-45743. (Pubitemid 39491564)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.44 , pp. 45737-45743
    • Taguchi, H.1    Tsukuda, K.2    Motojima, F.3    Koike-Takeshita, A.4    Yoshida, M.5
  • 27
    • 2442482377 scopus 로고    scopus 로고
    • GroEL mediates protein folding with a two successive timer mechanism
    • DOI 10.1016/S1097-2765(04)00261-8, PII S1097276504002618
    • Ueno T, Taguchi H, Tadakuma H, Yoshida M, Funatsu T (2004) GroEL mediates protein folding with a two successive timer mechanism. Mol Cell 14(4):423-434. (Pubitemid 38648796)
    • (2004) Molecular Cell , vol.14 , Issue.4 , pp. 423-434
    • Ueno, T.1    Taguchi, H.2    Tadakuma, H.3    Yoshida, M.4    Funatsu, T.5
  • 28
    • 53049103895 scopus 로고    scopus 로고
    • Revisiting the GroEL-GroES reaction cycle via the symmetric intermediate implied by novel aspects of the GroEL(D398A) mutant
    • Koike-Takeshita A, Yoshida M, Taguchi H (2008) Revisiting the GroEL-GroES reaction cycle via the symmetric intermediate implied by novel aspects of the GroEL(D398A) mutant. J Biol Chem 283(35):23774-23781.
    • (2008) J Biol Chem , vol.283 , Issue.35 , pp. 23774-23781
    • Koike-Takeshita, A.1    Yoshida, M.2    Taguchi, H.3
  • 29
    • 53049090990 scopus 로고    scopus 로고
    • Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle
    • Sameshima T, et al. (2008) Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle. J Biol Chem 283(35):23765-23773.
    • (2008) J Biol Chem , vol.283 , Issue.35 , pp. 23765-23773
    • Sameshima, T.1
  • 30
    • 77952779174 scopus 로고    scopus 로고
    • Denatured proteins facilitate the formation of the football-shaped GroEL-(GroES)2 complex
    • Sameshima T, Iizuka R, Ueno T, Funatsu T (2010) Denatured proteins facilitate the formation of the football-shaped GroEL-(GroES)2 complex. Biochem J 427(2):247-254.
    • (2010) Biochem J , vol.427 , Issue.2 , pp. 247-254
    • Sameshima, T.1    Iizuka, R.2    Ueno, T.3    Funatsu, T.4
  • 31
    • 84870369344 scopus 로고    scopus 로고
    • Single-molecule observation of protein folding in symmetric GroEL-(GroES)2 complexes
    • Takei Y, Iizuka R, Ueno T, Funatsu T (2012) Single-molecule observation of protein folding in symmetric GroEL-(GroES)2 complexes. J Biol Chem 287(49):41118-41125.
    • (2012) J Biol Chem , vol.287 , Issue.49 , pp. 41118-41125
    • Takei, Y.1    Iizuka, R.2    Ueno, T.3    Funatsu, T.4
  • 32
    • 58149265291 scopus 로고    scopus 로고
    • Ion transport and osmotic adjustment in Escherichia coli in response to ionic and non-ionic osmotica
    • Shabala L, et al. (2009) Ion transport and osmotic adjustment in Escherichia coli in response to ionic and non-ionic osmotica. Environ Microbiol 11(1):137-148.
    • (2009) Environ Microbiol , vol.11 , Issue.1 , pp. 137-148
    • Shabala, L.1
  • 33
    • 33744463129 scopus 로고    scopus 로고
    • Glu257 in GroEL is a sensor involved in coupling polypeptide substrate binding to stimulation of ATP hydrolysis
    • DOI 10.1110/ps.062100606
    • Danziger O, Shimon L, Horovitz A (2006) Glu257 in GroEL is a sensor involved in coupling polypeptide substrate binding to stimulation of ATP hydrolysis. Protein Sci 15(6):1270-1276. (Pubitemid 43800000)
    • (2006) Protein Science , vol.15 , Issue.6 , pp. 1270-1276
    • Danziger, O.1    Shimon, L.2    Horovitz, A.3
  • 34
    • 0032932922 scopus 로고    scopus 로고
    • Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: Evidence for noncooperative nucleotide binding
    • DOI 10.1016/S0167-4838(99)00049-7, PII S0167483899000497
    • Terada TP, Kuwajima K (1999) Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: Evidence for non-cooperative nucleotide binding. Biochim Biophys Acta 1431(2):269-281. (Pubitemid 29231982)
    • (1999) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1431 , Issue.2 , pp. 269-281
    • Terada, T.P.1    Kuwajima, K.2
  • 35
    • 0029995319 scopus 로고    scopus 로고
    • Allosteric control by ATP of non-folded protein binding to GroEL
    • DOI 10.1006/jmbi.1996.0028
    • Yifrach O, Horovitz A (1996) Allosteric control by ATP of non-folded protein binding to GroEL. J Mol Biol 255(3):356-361. (Pubitemid 26105559)
    • (1996) Journal of Molecular Biology , vol.255 , Issue.3 , pp. 356-361
    • Yifrach, O.1    Horovitz, A.2
  • 36
    • 0034849193 scopus 로고    scopus 로고
    • Application of fluorescence resonance energy transfer to the GroEL-GroES chaperonin reaction
    • Rye HS (2001) Application of fluorescence resonance energy transfer to the GroEL-GroES chaperonin reaction. Methods 24(3):278-288.
    • (2001) Methods , vol.24 , Issue.3 , pp. 278-288
    • Rye, H.S.1
  • 37
    • 0033617129 scopus 로고    scopus 로고
    • GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings
    • DOI 10.1016/S0092-8674(00)80742-4
    • Rye HS, et al. (1999) GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings. Cell 97(3):325-338. (Pubitemid 29214589)
    • (1999) Cell , vol.97 , Issue.3 , pp. 325-338
    • Rye, H.S.1    Roseman, A.M.2    Chen, S.3    Furtak, K.4    Fenton, W.A.5    Saibil, H.R.6    Horwich, A.L.7
  • 38
    • 0029016593 scopus 로고
    • The origins and consequences of asymmetry in the chaperonin reaction cycle
    • Burston SG, Ranson NA, Clarke AR (1995) The origins and consequences of asymmetry in the chaperonin reaction cycle. J Mol Biol 249(1):138-152.
    • (1995) J Mol Biol , vol.249 , Issue.1 , pp. 138-152
    • Burston, S.G.1    Ranson, N.A.2    Clarke, A.R.3
  • 39
    • 0037418665 scopus 로고    scopus 로고
    • 14 at 2.0 A resolution
    • DOI 10.1016/S0022-2836(03)00184-0
    • Wang J, Boisvert DC (2003) Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0A resolution. J Mol Biol 327(4):843-855. (Pubitemid 36315923)
    • (2003) Journal of Molecular Biology , vol.327 , Issue.4 , pp. 843-855
    • Wang, J.1    Boisvert, D.C.2
  • 41
    • 84881466449 scopus 로고    scopus 로고
    • Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 A resolution
    • Fei X, Yang D, Laronde-Leblanc N, Lorimer GH (2013) Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 A resolution. Proc Natl Acad Sci USA 110(32):E2958-E2966.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.32
    • Fei, X.1    Yang, D.2    Laronde-Leblanc, N.3    Lorimer, G.H.4
  • 42
    • 77950890438 scopus 로고    scopus 로고
    • Out-of-equilibrium conformational cycling of GroEL under saturating ATP concentrations
    • Frank GA, et al. (2010) Out-of-equilibrium conformational cycling of GroEL under saturating ATP concentrations. Proc Natl Acad Sci USA 107(14):6270-6274.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.14 , pp. 6270-6274
    • Frank, G.A.1
  • 43
    • 84879725730 scopus 로고    scopus 로고
    • Measuring how much work the chaperone GroEL can do
    • Corsepius NC, Lorimer GH (2013) Measuring how much work the chaperone GroEL can do. Proc Natl Acad Sci USA 110(27):E2451-E2459.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.27
    • Corsepius, N.C.1    Lorimer, G.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.