메뉴 건너뛰기




Volumn 401, Issue 4, 2010, Pages 553-563

Action of the chaperonin GroEL/ES on a non-native substrate observed with single-molecule FRET

Author keywords

Conformational change; FRET; GroEL; Single molecule fluorescence; VHL

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONIN; FLUORESCENT DYE; NUCLEOTIDE BINDING OLIGOMERIZATION DOMAIN LIKE RECEPTOR; POLYPEPTIDE; PROTEIN GROEL; PROTIEN GROES; UNCLASSIFIED DRUG; VON HIPPEL LINDAU PROTEIN;

EID: 77955312026     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.06.050     Document Type: Article
Times cited : (16)

References (52)
  • 1
    • 0026416043 scopus 로고
    • Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
    • Martin J., Langer T., Boteva R., Schramel A., Horwich A.L., Hartl F.U. Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature 1991, 352:36-42.
    • (1991) Nature , vol.352 , pp. 36-42
    • Martin, J.1    Langer, T.2    Boteva, R.3    Schramel, A.4    Horwich, A.L.5    Hartl, F.U.6
  • 2
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl F.U. Molecular chaperones in cellular protein folding. Nature 1996, 381:571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 3
    • 0035783192 scopus 로고    scopus 로고
    • Review: cellular substrates of the eukaryotic chaperonin TRiC/CCT
    • Dunn A.Y., Melville M.W., Frydman J. Review: cellular substrates of the eukaryotic chaperonin TRiC/CCT. J. Struct. Biol. 2001, 135:176-184.
    • (2001) J. Struct. Biol. , vol.135 , pp. 176-184
    • Dunn, A.Y.1    Melville, M.W.2    Frydman, J.3
  • 4
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: from nascent chain to folded protein
    • Hartl F.U., Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 2002, 295:1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 5
    • 0344738987 scopus 로고    scopus 로고
    • Chaperonin-mediated protein folding: fate of substrate polypeptide
    • Fenton W.A., Horwich A.L. Chaperonin-mediated protein folding: fate of substrate polypeptide. Q. Rev. Biophys. 2003, 36:229-256.
    • (2003) Q. Rev. Biophys. , vol.36 , pp. 229-256
    • Fenton, W.A.1    Horwich, A.L.2
  • 6
    • 7444231693 scopus 로고    scopus 로고
    • Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets
    • Spiess C., Meyer A.S., Reissmann S., Frydman J. Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. Trends Cell Biol. 2004, 14:598-604.
    • (2004) Trends Cell Biol. , vol.14 , pp. 598-604
    • Spiess, C.1    Meyer, A.S.2    Reissmann, S.3    Frydman, J.4
  • 7
    • 33646907087 scopus 로고    scopus 로고
    • GroEL-GroES-mediated protein folding
    • Horwich A.L., Farr G.W., Fenton W.A. GroEL-GroES-mediated protein folding. Chem. Rev. 2006, 106:1917-1930.
    • (2006) Chem. Rev. , vol.106 , pp. 1917-1930
    • Horwich, A.L.1    Farr, G.W.2    Fenton, W.A.3
  • 9
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B., Horwich A.L. The Hsp70 and Hsp60 chaperone machines. Cell 1998, 92:351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 10
    • 0033617129 scopus 로고    scopus 로고
    • GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings
    • Rye H.S., Roseman A.M., Chen S., Furtak K., Fenton W.A., Saibil H.R., Horwich A.L. GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings. Cell 1999, 97:325-338.
    • (1999) Cell , vol.97 , 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
  • 11
    • 0032478545 scopus 로고    scopus 로고
    • Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT
    • Ditzel L., Löwe J., Stock D., Stetter K., Huber H., Huber R., Steinbacher S. Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT. Cell 1998, 93:125-138.
    • (1998) Cell , vol.93 , pp. 125-138
    • Ditzel, L.1    Löwe, J.2    Stock, D.3    Stetter, K.4    Huber, H.5    Huber, R.6    Steinbacher, S.7
  • 12
    • 0038737003 scopus 로고    scopus 로고
    • Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis
    • Meyer A.S., Gillespie J.R., Walther D., Millet I.S., Doniach S., Frydman J. Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis. Cell 2003, 113:369-381.
    • (2003) Cell , vol.113 , pp. 369-381
    • Meyer, A.S.1    Gillespie, J.R.2    Walther, D.3    Millet, I.S.4    Doniach, S.5    Frydman, J.6
  • 13
    • 33746265142 scopus 로고    scopus 로고
    • GroEL-mediated protein folding: making the impossible, possible
    • Lin Z., Rye H.S. GroEL-mediated protein folding: making the impossible, possible. Crit. Rev. Biochem. Mol. Biol. 2006, 41:211-239.
    • (2006) Crit. Rev. Biochem. Mol. Biol. , vol.41 , pp. 211-239
    • Lin, Z.1    Rye, H.S.2
  • 14
    • 0027933369 scopus 로고
    • GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
    • Weissman J.S., Kashi Y., Fenton W.A., Horwich A.L GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms. Cell 1994, 78:693-702.
    • (1994) Cell , vol.78 , pp. 693-702
    • Weissman, J.S.1    Kashi, Y.2    Fenton, W.A.3    Horwich, A.L.4
  • 15
    • 38049125649 scopus 로고    scopus 로고
    • Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution
    • Horst R., Fenton W.A., Englander S.W., Wuthrich K., Horwich A.L. Folding trajectories of human dihydrofolate reductase inside the GroEL GroES chaperonin cavity and free in solution. Proc. Natl Acad. Sci. USA 2007, 104:20788-20792.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 20788-20792
    • Horst, R.1    Fenton, W.A.2    Englander, S.W.3    Wuthrich, K.4    Horwich, A.L.5
  • 16
    • 41149089882 scopus 로고    scopus 로고
    • Monitoring protein conformation along the pathway of chaperonin-assisted folding
    • Sharma S., Chakraborty K., Muller B.K., Astola N., Tang Y.C., Lamb D.C., et al. Monitoring protein conformation along the pathway of chaperonin-assisted folding. Cell 2008, 133:142-153.
    • (2008) Cell , vol.133 , pp. 142-153
    • Sharma, S.1    Chakraborty, K.2    Muller, B.K.3    Astola, N.4    Tang, Y.C.5    Lamb, D.C.6
  • 17
    • 33847777828 scopus 로고    scopus 로고
    • Disulfide formation as a probe of folding in GroEL-GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones
    • Park E.S., Fenton W.A., Horwich A.L. Disulfide formation as a probe of folding in GroEL-GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones. Proc. Natl Acad. Sci. USA 2007, 104:2145-2150.
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 2145-2150
    • Park, E.S.1    Fenton, W.A.2    Horwich, A.L.3
  • 18
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • Fenton W.A., Kashi Y., Furtak K., Horwich A.L. Residues in chaperonin GroEL required for polypeptide binding and release. Nature 1994, 371:614-619.
    • (1994) Nature , vol.371 , pp. 614-619
    • Fenton, W.A.1    Kashi, Y.2    Furtak, K.3    Horwich, A.L.4
  • 20
    • 2442482377 scopus 로고    scopus 로고
    • GroEL mediates protein folding with a two successive timer mechanism
    • Ueno T., Taguchi H., Tadakuma H., Yoshida M., Funatsu T. GroEL mediates protein folding with a two successive timer mechanism. Mol. Cell 2004, 14:423-434.
    • (2004) Mol. Cell , vol.14 , pp. 423-434
    • Ueno, T.1    Taguchi, H.2    Tadakuma, H.3    Yoshida, M.4    Funatsu, T.5
  • 21
    • 8544241796 scopus 로고    scopus 로고
    • BeFx stops the chaperonin cycle of GroEL-GroES and generates a complex with double folding chambers
    • Taguchi H., Tsukuda K., Motojima F., Koike-Takeshita A., Yoshida M. BeFx stops the chaperonin cycle of GroEL-GroES and generates a complex with double folding chambers. J. Biol. Chem. 2004, 279:45737-45743.
    • (2004) J. Biol. Chem. , vol.279 , pp. 45737-45743
    • Taguchi, H.1    Tsukuda, K.2    Motojima, F.3    Koike-Takeshita, A.4    Yoshida, M.5
  • 22
    • 0033400674 scopus 로고    scopus 로고
    • Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC
    • Feldman D.E., Thulasiraman V., Ferreyra R.G., Frydman J. Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC. Mol. Cell 1999, 4:1051-1061.
    • (1999) Mol. Cell , vol.4 , pp. 1051-1061
    • Feldman, D.E.1    Thulasiraman, V.2    Ferreyra, R.G.3    Frydman, J.4
  • 23
    • 0345708112 scopus 로고    scopus 로고
    • Tumorigenic mutations in VHL disrupt folding in vivo by interfering with chaperonin binding
    • Feldman D.E., Spiess C., Howard D.E., Frydman J. Tumorigenic mutations in VHL disrupt folding in vivo by interfering with chaperonin binding. Mol. Cell 2003, 12:1213-1224.
    • (2003) Mol. Cell , vol.12 , pp. 1213-1224
    • Feldman, D.E.1    Spiess, C.2    Howard, D.E.3    Frydman, J.4
  • 24
    • 0037404423 scopus 로고    scopus 로고
    • The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex
    • Melville M.W., McClellan A.J., Meyer A.S., Darveau A., Frydman J. The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex. Mol. Cell. Biol. 2003, 23:3141-3151.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3141-3151
    • Melville, M.W.1    McClellan, A.J.2    Meyer, A.S.3    Darveau, A.4    Frydman, J.5
  • 25
    • 33749080319 scopus 로고    scopus 로고
    • Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins
    • Spiess C., Miller E.J., McClellan A.J., Frydman J. Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins. Mol. Cell 2006, 24:25-37.
    • (2006) Mol. Cell , vol.24 , pp. 25-37
    • Spiess, C.1    Miller, E.J.2    McClellan, A.J.3    Frydman, J.4
  • 26
    • 0033574737 scopus 로고    scopus 로고
    • Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function
    • Stebbins C.E., Kaelin W.G., Pavletich N.P. Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function. Science 1999, 284:455-461.
    • (1999) Science , vol.284 , pp. 455-461
    • Stebbins, C.E.1    Kaelin, W.G.2    Pavletich, N.P.3
  • 27
    • 0017795758 scopus 로고
    • Fluorescence energy-transfer as a spectroscopic ruler
    • Stryer L. Fluorescence energy-transfer as a spectroscopic ruler. Annu. Rev. Biochem. 1978, 47:819-846.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 819-846
    • Stryer, L.1
  • 28
    • 0034807927 scopus 로고    scopus 로고
    • Single-molecule fluorescence resonant energy transfer
    • Ha T. Single-molecule fluorescence resonant energy transfer. Methods 2001, 25:78-86.
    • (2001) Methods , vol.25 , pp. 78-86
    • Ha, T.1
  • 31
    • 33746823043 scopus 로고    scopus 로고
    • Coil-globule transition in the denatured state of a small protein
    • Sherman E., Haran G. Coil-globule transition in the denatured state of a small protein. Proc. Natl Acad. Sci. USA 2006, 103:11539-11543.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 11539-11543
    • Sherman, E.1    Haran, G.2
  • 32
    • 30344461602 scopus 로고    scopus 로고
    • Probing the sequence of conformationally-induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopy
    • Kim S.Y., Semyonov A.N., Twieg R.J., Horwich A.L., Frydman J., Moerner W.E. Probing the sequence of conformationally-induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopy. J. Phys. Chem. B 2005, 109:24517-24525.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 24517-24525
    • Kim, S.Y.1    Semyonov, A.N.2    Twieg, R.J.3    Horwich, A.L.4    Frydman, J.5    Moerner, W.E.6
  • 34
    • 34548096938 scopus 로고    scopus 로고
    • Theory of photon statistics in single-molecule Forster resonance energy transfer
    • Gopich I., Szabo A. Theory of photon statistics in single-molecule Forster resonance energy transfer. J. Chem. Phys. 2005, 122:14707.
    • (2005) J. Chem. Phys. , vol.122 , pp. 14707
    • Gopich, I.1    Szabo, A.2
  • 36
    • 0028785583 scopus 로고
    • Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES
    • Weissman J.S., Hohl C.M., Kovalenko O., Kashi Y., Chen S., Braig K., et al. Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. Cell 1995, 83:577-587.
    • (1995) Cell , vol.83 , pp. 577-587
    • Weissman, J.S.1    Hohl, C.M.2    Kovalenko, O.3    Kashi, Y.4    Chen, S.5    Braig, K.6
  • 37
    • 4944221602 scopus 로고    scopus 로고
    • Expansion and compression of a protein folding intermediate by GroEL
    • Lin Z., Rye H.S. Expansion and compression of a protein folding intermediate by GroEL. Mol. Cell 2004, 16:23-34.
    • (2004) Mol. Cell , vol.16 , pp. 23-34
    • Lin, Z.1    Rye, H.S.2
  • 38
    • 0034880923 scopus 로고    scopus 로고
    • Folding of malate dehydrogenase inside the GroEL-GroES cavity
    • Chen J., Walter S., Horwich A.L., Smith D.L. Folding of malate dehydrogenase inside the GroEL-GroES cavity. Nat. Struct. Biol. 2001, 8:721-728.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 721-728
    • Chen, J.1    Walter, S.2    Horwich, A.L.3    Smith, D.L.4
  • 39
    • 13844299260 scopus 로고    scopus 로고
    • No evidence for a forced-unfolding mechanism during ATP/GroES binding to substrate-bound GroEL: no observable protection of metastable Rubisco intermediate or GroEL-bound Rubisco from tritium exchange
    • Park E.S., Fenton W.A., Horwich A.L. No evidence for a forced-unfolding mechanism during ATP/GroES binding to substrate-bound GroEL: no observable protection of metastable Rubisco intermediate or GroEL-bound Rubisco from tritium exchange. FEBS Lett. 2005, 579:1183-1186.
    • (2005) FEBS Lett. , vol.579 , pp. 1183-1186
    • Park, E.S.1    Fenton, W.A.2    Horwich, A.L.3
  • 40
    • 55949101455 scopus 로고    scopus 로고
    • Potential for modulation of the hydrophobic effect inside chaperonins
    • England J.L., Pande V.S. Potential for modulation of the hydrophobic effect inside chaperonins. Biophys. J. 2008, 95:3391-3399.
    • (2008) Biophys. J. , vol.95 , pp. 3391-3399
    • England, J.L.1    Pande, V.S.2
  • 41
    • 33646897305 scopus 로고    scopus 로고
    • Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein
    • Tang Y.C., Chang H.C., Roeben A., Wischnewski D., Wischnewski N., Kerner M.J., et al. Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein. Cell 2006, 125:903-914.
    • (2006) Cell , vol.125 , pp. 903-914
    • Tang, Y.C.1    Chang, H.C.2    Roeben, A.3    Wischnewski, D.4    Wischnewski, N.5    Kerner, M.J.6
  • 42
    • 51749084427 scopus 로고    scopus 로고
    • A role for confined water in chaperonin function
    • England J.L., Lucent D., Pande V.S. A role for confined water in chaperonin function. J. Am. Chem. Soc. 2008, 130:11838-11839.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 11838-11839
    • England, J.L.1    Lucent, D.2    Pande, V.S.3
  • 43
    • 33746713745 scopus 로고    scopus 로고
    • Real-time observation of RecA filament dynamics with single monomer resolution
    • Joo C., McKinney S.A., Nakamura M., Rasnik I., Ha T. Real-time observation of RecA filament dynamics with single monomer resolution. Cell 2006, 126:515-527.
    • (2006) Cell , vol.126 , pp. 515-527
    • Joo, C.1    McKinney, S.A.2    Nakamura, M.3    Rasnik, I.4    Ha, T.5
  • 44
    • 0041876386 scopus 로고    scopus 로고
    • Methods of single-molecule fluorescence spectroscopy and microscopy
    • Moerner W.E., Fromm D.P. Methods of single-molecule fluorescence spectroscopy and microscopy. Rev. Sci. Instrum. 2003, 74:3597-3619.
    • (2003) Rev. Sci. Instrum. , vol.74 , pp. 3597-3619
    • Moerner, W.E.1    Fromm, D.P.2
  • 45
    • 0033168388 scopus 로고    scopus 로고
    • Optical methods for exploring dynamics of single copies of green fluorescent protein
    • Moerner W.E., Peterman E.J.G., Brasselet S., Kummer S., Dickson R.M. Optical methods for exploring dynamics of single copies of green fluorescent protein. Cytometry 1999, 36:232-238.
    • (1999) Cytometry , vol.36 , pp. 232-238
    • Moerner, W.E.1    Peterman, E.J.G.2    Brasselet, S.3    Kummer, S.4    Dickson, R.M.5
  • 46
    • 20644431583 scopus 로고    scopus 로고
    • Single-molecule fluorescence resonant energy transfer in calcium concentration dependent cameleon
    • Brasselet S., Peterman E.J.G., Miyawaki A., Moerner W.E. Single-molecule fluorescence resonant energy transfer in calcium concentration dependent cameleon. J. Phys. Chem. B 2000, 104:3676-3682.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 3676-3682
    • Brasselet, S.1    Peterman, E.J.G.2    Miyawaki, A.3    Moerner, W.E.4
  • 47
    • 0001147955 scopus 로고    scopus 로고
    • Two-photon fluorescence excitation cross sections of biomolecular probes from 690 to 960 nm
    • Albota M.A., Xu C., Webb W.W. Two-photon fluorescence excitation cross sections of biomolecular probes from 690 to 960 nm. Appl. Opt. 1998, 37:7352-7356.
    • (1998) Appl. Opt. , vol.37 , pp. 7352-7356
    • Albota, M.A.1    Xu, C.2    Webb, W.W.3
  • 48
    • 33947094704 scopus 로고
    • Absolute quantum yield determination by thermal blooming
    • Brannon J.H., Magde D. Absolute quantum yield determination by thermal blooming. Fluorescein. J. Phys. Chem. 1978, 82:705-709.
    • (1978) Fluorescein. J. Phys. Chem. , vol.82 , pp. 705-709
    • Brannon, J.H.1    Magde, D.2
  • 49
    • 0010104094 scopus 로고    scopus 로고
    • PhotochemCAD: a computer-aided design and research tool in photochemistry
    • Du H., Fuh R.-A., Li J., Corkan L.A., Lindsey J.S. PhotochemCAD: a computer-aided design and research tool in photochemistry. Photochem. Photobiol. 1998, 68:141-142.
    • (1998) Photochem. Photobiol. , vol.68 , pp. 141-142
    • Du, H.1    Fuh, R.-A.2    Li, J.3    Corkan, L.A.4    Lindsey, J.S.5
  • 50
    • 0036751701 scopus 로고    scopus 로고
    • Alexa and Oregon green dyes as fluorescence anisotropy probes for measuring protein-protein and protein-nucleic acid interactions
    • Rusinova E., Tretyachenko-Ladokhina V., Vele O.E., Senear D.F., Alexander Ross J.B. Alexa and Oregon green dyes as fluorescence anisotropy probes for measuring protein-protein and protein-nucleic acid interactions. Anal. Biochem. 2002, 308:18-25.
    • (2002) Anal. Biochem. , vol.308 , pp. 18-25
    • Rusinova, E.1    Tretyachenko-Ladokhina, V.2    Vele, O.E.3    Senear, D.F.4    Alexander Ross, J.B.5
  • 51
    • 0029009727 scopus 로고
    • The molecular chaperonin cpn60 displays local flexibility that is reduced after binding with an unfolded protein
    • Gorovits B.M., Horowitz P.M. The molecular chaperonin cpn60 displays local flexibility that is reduced after binding with an unfolded protein. J. Biol. Chem. 1995, 270:13057-13062.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13057-13062
    • Gorovits, B.M.1    Horowitz, P.M.2
  • 52
    • 33746969931 scopus 로고    scopus 로고
    • Revealing two-state protein-protein interactions of calmodulin by single-molecule spectroscopy
    • Liu R., Hu D., Tan X., Lu H.P. Revealing two-state protein-protein interactions of calmodulin by single-molecule spectroscopy. J. Am. Chem. Soc. 2006, 128:10034-10042.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 10034-10042
    • Liu, R.1    Hu, D.2    Tan, X.3    Lu, H.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.