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Volumn 329, Issue 1, 2003, Pages 121-134

The allosteric transition of GroEL induced by metal fluoride-ADP complexes

Author keywords

Allosteric effect; Chaperonin; Cooperativity; Phosphate analog; X ray scattering

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ALUMINUM; BERYLLIUM; CHAPERONIN; FLUORIDE ION; FLUORINE; GALLIUM; METAL COMPLEX; OXYGEN; PHOSPHATE; PHOSPHORUS; PYRENE; SCANDIUM; TRANSITION ELEMENT; VANADIC ACID; VANADIUM;

EID: 0038369870     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00409-1     Document Type: Article
Times cited : (19)

References (39)
  • 1
    • 0035715944 scopus 로고    scopus 로고
    • Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding
    • Saibil H.R., Horwich A.L., Fenton W.A. Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding. Advan. Protein Chem. 59:2001;45-72.
    • (2001) Advan. Protein Chem. , vol.59 , pp. 45-72
    • Saibil, H.R.1    Horwich, A.L.2    Fenton, W.A.3
  • 3
    • 0029004759 scopus 로고
    • Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL
    • Yifrach O., Horovitz A. Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL. Biochemistry. 34:1995;5303-5308.
    • (1995) Biochemistry , vol.34 , pp. 5303-5308
    • Yifrach, O.1    Horovitz, A.2
  • 4
    • 0035830681 scopus 로고    scopus 로고
    • Nucleotide binding to the chaperonin GroEL: Non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP
    • Inobe T., Makio T., Takasu-Ishikawa E., Terada T.P., Kuwajima K. Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP. Biochim. Biophys. Acta. 1545:2001;160-173.
    • (2001) Biochim. Biophys. Acta. , vol.1545 , pp. 160-173
    • Inobe, T.1    Makio, T.2    Takasu-Ishikawa, E.3    Terada, T.P.4    Kuwajima, K.5
  • 5
    • 0037436402 scopus 로고    scopus 로고
    • Equilibrium and kinetics of the allosteric transition of GroEL studied by solution X-ray scattering and fluorescence spectroscopy
    • Inobe T., Arai M., Nakao M., Ito K., Kamagata K., Makio T., et al. Equilibrium and kinetics of the allosteric transition of GroEL studied by solution X-ray scattering and fluorescence spectroscopy. J. Mol. Biol. 327:2003;183-191.
    • (2003) J. Mol. Biol. , vol.327 , pp. 183-191
    • Inobe, T.1    Arai, M.2    Nakao, M.3    Ito, K.4    Kamagata, K.5    Makio, T.6
  • 6
    • 0025191377 scopus 로고
    • Aluminofluoride and beryllofluoride complexes: New phosphate analogs in enzymology
    • Chabre M. Aluminofluoride and beryllofluoride complexes: new phosphate analogs in enzymology. Trends Biochem. Sci. 15:1990;6-10.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 6-10
    • Chabre, M.1
  • 7
    • 0031001328 scopus 로고    scopus 로고
    • Mechanism for coupling free energy in ATPase to the myosin active site
    • Park S., Ajtai K., Burghardt T.P. Mechanism for coupling free energy in ATPase to the myosin active site. Biochemistry. 36:1997;3368-3372.
    • (1997) Biochemistry , vol.36 , pp. 3368-3372
    • Park, S.1    Ajtai, K.2    Burghardt, T.P.3
  • 10
    • 0022870880 scopus 로고
    • The chemistry of aluminum as related to biology and medicine
    • Martin R.B. The chemistry of aluminum as related to biology and medicine. Clin. Chem. 32:1986;1797-1806.
    • (1986) Clin. Chem. , vol.32 , pp. 1797-1806
    • Martin, R.B.1
  • 11
    • 0027250447 scopus 로고
    • Hydrolysis of adenosine 5′-triphosphate by Escherichia coli GroEL: Effects of GroES and potassium ion
    • Todd M.J., Viitanen P.V., Lorimer G.H. Hydrolysis of adenosine 5′-triphosphate by Escherichia coli GroEL: effects of GroES and potassium ion. Biochemistry. 32:1993;8560-8567.
    • (1993) Biochemistry , vol.32 , pp. 8560-8567
    • Todd, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 13
    • 0023821030 scopus 로고
    • 4-reversibly inhibits 'P'-type cation-transport ATPases, possibly by interacting with the phosphate-binding site of the ATPase
    • 4-reversibly inhibits 'P'-type cation-transport ATPases, possibly by interacting with the phosphate-binding site of the ATPase. Biochem. J. 253:1988;827-833.
    • (1988) Biochem. J. , vol.253 , pp. 827-833
    • Missiaen, L.1    Wuytack, F.2    De Smedt, H.3    Vrolix, M.4    Casteels, R.5
  • 15
    • 0032932922 scopus 로고    scopus 로고
    • Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: Evidence for non-cooperative nucleotide binding
    • Terada T.P., Kuwajima K. Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: evidence for non-cooperative nucleotide binding. Biochim. Biophys. Acta. 1431:1999;269-281.
    • (1999) Biochim. Biophys. Acta. , vol.1431 , pp. 269-281
    • Terada, T.P.1    Kuwajima, K.2
  • 16
    • 0026498425 scopus 로고
    • Small-angle synchrotron X-ray scattering reveals distinct shape changes of the myosin head during hydrolysis of ATP
    • Wakabayashi K., Tokunaga M., Kohno I., Sugimoto Y., Hamanaka T., Takezawa Y., et al. Small-angle synchrotron X-ray scattering reveals distinct shape changes of the myosin head during hydrolysis of ATP. Science. 258:1992;443-447.
    • (1992) Science , vol.258 , pp. 443-447
    • Wakabayashi, K.1    Tokunaga, M.2    Kohno, I.3    Sugimoto, Y.4    Hamanaka, T.5    Takezawa, Y.6
  • 18
    • 0034329452 scopus 로고    scopus 로고
    • Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23
    • Young J.C., Hartl F.U. Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23. EMBO J. 19:2000;5930-5940.
    • (2000) EMBO J. , vol.19 , pp. 5930-5940
    • Young, J.C.1    Hartl, F.U.2
  • 19
    • 0023096422 scopus 로고
    • The effect of activating ligands on the intrinsic fluorescence of guanine nucleotide-binding regulatory proteins
    • Higashijima T., Ferguson K.M., Sternweis P.C., Ross E.M., Smigel M.D., Gilman A.G. The effect of activating ligands on the intrinsic fluorescence of guanine nucleotide-binding regulatory proteins. J. Biol. Chem. 262:1987;752-756.
    • (1987) J. Biol. Chem. , vol.262 , pp. 752-756
    • Higashijima, T.1    Ferguson, K.M.2    Sternweis, P.C.3    Ross, E.M.4    Smigel, M.D.5    Gilman, A.G.6
  • 20
    • 33947086153 scopus 로고
    • Coordination chemistry of scandium. V. Crystal and molecular structure of tris(acetylacetonato)scandium(III)
    • Anderson T.J., Neuman M.A., Melson G.A. Coordination chemistry of scandium. V. Crystal and molecular structure of tris(acetylacetonato)scandium(III). Inorg. Chem. 12:1973;927-930.
    • (1973) Inorg. Chem. , vol.12 , pp. 927-930
    • Anderson, T.J.1    Neuman, M.A.2    Melson, G.A.3
  • 21
    • 0015236388 scopus 로고
    • Adenylyl imidodiphosphate, an adenosine triphosphate analog containing a P-N-P linkage
    • Yount R.G., Babcock D., Ballantyne W., Ojala D. Adenylyl imidodiphosphate, an adenosine triphosphate analog containing a P-N-P linkage. Biochemistry. 10:1971;2484-2489.
    • (1971) Biochemistry , vol.10 , pp. 2484-2489
    • Yount, R.G.1    Babcock, D.2    Ballantyne, W.3    Ojala, D.4
  • 25
    • 0030592538 scopus 로고    scopus 로고
    • The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
    • Roseman A.M., Chen S., White H., Braig K., Saibil H.R. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell. 87:1996;241-251.
    • (1996) Cell , vol.87 , pp. 241-251
    • Roseman, A.M.1    Chen, S.2    White, H.3    Braig, K.4    Saibil, H.R.5
  • 27
    • 0037195147 scopus 로고    scopus 로고
    • Φ value analysis of heterogeneity in pathways of allosteric transitions: Evidence for parallel pathways of ATP-induced conformational changes in a GroEL ring
    • Horovitz A., Amir A., Danziger O., Kafri G. Φ value analysis of heterogeneity in pathways of allosteric transitions: evidence for parallel pathways of ATP-induced conformational changes in a GroEL ring. Proc. Natl Acad. Sci. USA. 99:2002;14095-14097.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 14095-14097
    • Horovitz, A.1    Amir, A.2    Danziger, O.3    Kafri, G.4
  • 28
    • 0032546571 scopus 로고    scopus 로고
    • Transient kinetic analysis of adenosine 5′-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL
    • Yifrach O., Horovitz A. Transient kinetic analysis of adenosine 5′-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL. Biochemistry. 37:1998;7083-7088.
    • (1998) Biochemistry , vol.37 , pp. 7083-7088
    • Yifrach, O.1    Horovitz, A.2
  • 30
    • 0035929338 scopus 로고    scopus 로고
    • Nucleotide-induced transition of GroEL from the high-affinity to the low-affinity state for a target protein: Effects of ATP and ADP on the GroEL-affected refolding of α-lactalbumin
    • Makio T., Takasu-Ishikawa E., Kuwajima K. Nucleotide-induced transition of GroEL from the high-affinity to the low-affinity state for a target protein: effects of ATP and ADP on the GroEL-affected refolding of α-lactalbumin. J. Mol. Biol. 312:2001;555-567.
    • (2001) J. Mol. Biol. , vol.312 , pp. 555-567
    • Makio, T.1    Takasu-Ishikawa, E.2    Kuwajima, K.3
  • 31
    • 0027419011 scopus 로고
    • Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: Implications for the mechanism of assisted protein folding
    • Jackson G.S., Staniforth R.A., Halsall D.J., Atkinson T., Holbrook J.J., Clarke A.R., Burston S.G. Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding. Biochemistry. 32:1993;2554-2563.
    • (1993) Biochemistry , vol.32 , pp. 2554-2563
    • Jackson, G.S.1    Staniforth, R.A.2    Halsall, D.J.3    Atkinson, T.4    Holbrook, J.J.5    Clarke, A.R.6    Burston, S.G.7
  • 32
    • 0029875083 scopus 로고    scopus 로고
    • The mitochondrial protein import motor: Dissociation of mitochondrial Hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysis
    • Horst M., Oppliger W., Feifel B., Schatz G., Glick B.S. The mitochondrial protein import motor: dissociation of mitochondrial Hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysis. Protein Sci. 5:1996;759-767.
    • (1996) Protein Sci. , vol.5 , pp. 759-767
    • Horst, M.1    Oppliger, W.2    Feifel, B.3    Schatz, G.4    Glick, B.S.5
  • 34
    • 0036349865 scopus 로고    scopus 로고
    • Fast compaction of α-lactalbumin during folding studied by stopped-flow X-ray scattering
    • Arai M., Ito K., Inobe T., Nakao M., Maki K., Kamagata K., et al. Fast compaction of α-lactalbumin during folding studied by stopped-flow X-ray scattering. J. Mol. Biol. 321:2002;121-132.
    • (2002) J. Mol. Biol. , vol.321 , pp. 121-132
    • Arai, M.1    Ito, K.2    Inobe, T.3    Nakao, M.4    Maki, K.5    Kamagata, K.6
  • 35
    • 0029249356 scopus 로고
    • Large-aperture TV detector with a beryllium-windowed image intensifier for X-ray diffraction
    • Amemiya Y., Ito K., Yagi N., Asano Y., Wakabayashi K., Ueki T., Endo T. Large-aperture TV detector with a beryllium-windowed image intensifier for X-ray diffraction. Rev. Sci. Instrum. 66:1995;2290-2294.
    • (1995) Rev. Sci. Instrum. , vol.66 , pp. 2290-2294
    • Amemiya, Y.1    Ito, K.2    Yagi, N.3    Asano, Y.4    Wakabayashi, K.5    Ueki, T.6    Endo, T.7
  • 36
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:1996;51-53.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-53
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 38
    • 0004009372 scopus 로고
    • F. Cotton, & G. Wilkinson. New York: Wiley
    • Cotton F., Wilkinson G. Advanced Inorganic Chemistry. 1962;Wiley, New York.
    • (1962) Advanced Inorganic Chemistry
  • 39
    • 0039838636 scopus 로고
    • Stereochemistry of dioxovanadium (V) complexes. I. The crystal and molecular structure of triammonium bis(oxalato)dioxovanadate(V) dihydrate
    • Scheidt W., Tsai C.-, Hoard J. Stereochemistry of dioxovanadium (V) complexes. I. The crystal and molecular structure of triammonium bis(oxalato)dioxovanadate(V) dihydrate. J. Am. Chem. Soc. 93:1971;3867.
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 3867
    • Scheidt, W.1    Tsai C.-2    Hoard, J.3


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