메뉴 건너뛰기




Volumn 1784, Issue 12, 2008, Pages 2071-2078

The conserved Cys254 plays a crucial role in creatine kinase refolding under non-reduced conditions but not in its activity or stability

Author keywords

Creatine kinase; Folding kinetic; Oxidative stress; Protein aggregation; Reduced condition

Indexed keywords

CREATINE KINASE; CYSTEINE; PROTEIN;

EID: 54549089754     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.08.018     Document Type: Article
Times cited : (7)

References (47)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen C.B. Principles that govern the folding of protein chains. Science 181 (1973) 223-230
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 3
    • 0028017704 scopus 로고
    • Creatine-kinase in nonmuscle tissues and cells
    • Wallimann T., and Hemmer W. Creatine-kinase in nonmuscle tissues and cells. Mol. Cell. Biochem. 133 (1994) 193-220
    • (1994) Mol. Cell. Biochem. , vol.133 , pp. 193-220
    • Wallimann, T.1    Hemmer, W.2
  • 4
    • 0026585611 scopus 로고
    • Intracellular compartmentation, structure and function of creatine kinase isozymes in tissues with high and fluctuating energy demands: the "phosphocreatine circuit" for cellular energy homeostasis
    • Wallimann T., Wyss M., Brdiczka D., Nicolay K., and Eppenberger H.M. Intracellular compartmentation, structure and function of creatine kinase isozymes in tissues with high and fluctuating energy demands: the "phosphocreatine circuit" for cellular energy homeostasis. Biochem. J. 281 (1992) 21-40
    • (1992) Biochem. J. , vol.281 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 5
    • 0028050777 scopus 로고
    • Dissecting the role of creatine kinase
    • Wallimann T. Dissecting the role of creatine kinase. Curr. Biol. 4 (1994) 42-46
    • (1994) Curr. Biol. , vol.4 , pp. 42-46
    • Wallimann, T.1
  • 8
    • 33845227579 scopus 로고    scopus 로고
    • Effects of the single point genetic mutation D54G on muscle creatine kinase activity, structure and stability
    • Feng S., Zhao T.-J., Zhou H.-M., and Yan Y.-B. Effects of the single point genetic mutation D54G on muscle creatine kinase activity, structure and stability. Int. J. Biochem. Cell Biol. 39 (2007) 392-401
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 392-401
    • Feng, S.1    Zhao, T.-J.2    Zhou, H.-M.3    Yan, Y.-B.4
  • 11
    • 34548202723 scopus 로고    scopus 로고
    • Role of the linker between the N- and C-terminal domains in the stability and folding of rabbit muscle creatine kinase
    • He H.-W., Feng S., Pang M., Zhou H.-M., and Yan Y.-B. Role of the linker between the N- and C-terminal domains in the stability and folding of rabbit muscle creatine kinase. Int. J. Biochem. Cell Biol. 39 (2007) 1816-1827
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 1816-1827
    • He, H.-W.1    Feng, S.2    Pang, M.3    Zhou, H.-M.4    Yan, Y.-B.5
  • 12
    • 0002046465 scopus 로고
    • Adenosinetriphosphate-creatine transphosphorylase. I. Isolation of the crystalline enzyme from rabbit muscle
    • Kuby S.A., Noda L., and Lardy H.A. Adenosinetriphosphate-creatine transphosphorylase. I. Isolation of the crystalline enzyme from rabbit muscle. J. Biol. Chem. 209 (1954) 191-201
    • (1954) J. Biol. Chem. , vol.209 , pp. 191-201
    • Kuby, S.A.1    Noda, L.2    Lardy, H.A.3
  • 13
    • 0022645377 scopus 로고
    • Comparison of activity and conformation changes during refolding of urea-denatured creatine kinase
    • Zhou H.-M., and Tsou C.-L. Comparison of activity and conformation changes during refolding of urea-denatured creatine kinase. Biochim. Biophys. Acta 869 (1986) 69-74
    • (1986) Biochim. Biophys. Acta , vol.869 , pp. 69-74
    • Zhou, H.-M.1    Tsou, C.-L.2
  • 14
    • 0023656720 scopus 로고
    • Monoclonal antibody studies of creatine kinase: antibody-binding sites in the N-terminal region of creatine kinase and effects of antibody on enzyme refolding
    • Morris G.E., Frost L.C., Newport P.A., and Hudson N. Monoclonal antibody studies of creatine kinase: antibody-binding sites in the N-terminal region of creatine kinase and effects of antibody on enzyme refolding. Biochem. J. 248 (1987) 53-59
    • (1987) Biochem. J. , vol.248 , pp. 53-59
    • Morris, G.E.1    Frost, L.C.2    Newport, P.A.3    Hudson, N.4
  • 15
    • 0031672564 scopus 로고    scopus 로고
    • Unfolding and refolding of dimeric creatine kinase equilibrium and kinetic studies
    • Fan Y.X., Zhou J.M., Kihara H., and Tsou C.L. Unfolding and refolding of dimeric creatine kinase equilibrium and kinetic studies. Protein Sci. 7 (1998) 2631-2641
    • (1998) Protein Sci. , vol.7 , pp. 2631-2641
    • Fan, Y.X.1    Zhou, J.M.2    Kihara, H.3    Tsou, C.L.4
  • 16
    • 0032535663 scopus 로고    scopus 로고
    • Evidence for kinetic intermediate states during the refolding of GdnHCl-denatured MM-creatine kinase. Characterization of a trapped monomeric species
    • Leydier C., Clottes E., Couthon F., Marcillat O., Ebel C., and Vial C. Evidence for kinetic intermediate states during the refolding of GdnHCl-denatured MM-creatine kinase. Characterization of a trapped monomeric species. Biochemistry 37 (1998) 17579-17589
    • (1998) Biochemistry , vol.37 , pp. 17579-17589
    • Leydier, C.1    Clottes, E.2    Couthon, F.3    Marcillat, O.4    Ebel, C.5    Vial, C.6
  • 17
    • 0031033159 scopus 로고    scopus 로고
    • Protease digestion studies of an equilibrium intermediate in the unfolding of creatine kinase
    • Webb T., Jackson P.J., and Morris G.E. Protease digestion studies of an equilibrium intermediate in the unfolding of creatine kinase. Biochem. J. 321 (1997) 83-88
    • (1997) Biochem. J. , vol.321 , pp. 83-88
    • Webb, T.1    Jackson, P.J.2    Morris, G.E.3
  • 18
    • 0035255007 scopus 로고    scopus 로고
    • Structure of an intermediate in the unfolding of creatine kinase
    • Webb T.I., and Morris G.E. Structure of an intermediate in the unfolding of creatine kinase. Prot. Struct. Funct. Genet. 42 (2001) 269-278
    • (2001) Prot. Struct. Funct. Genet. , vol.42 , pp. 269-278
    • Webb, T.I.1    Morris, G.E.2
  • 19
    • 0034881136 scopus 로고    scopus 로고
    • Folding pathway for partially folded rabbit muscle creatine kinase
    • Park Y.D., Ou W.B., Yu T.W., and Zhou H.M. Folding pathway for partially folded rabbit muscle creatine kinase. Biochem. Cell Biol. 79 (2001) 479-487
    • (2001) Biochem. Cell Biol. , vol.79 , pp. 479-487
    • Park, Y.D.1    Ou, W.B.2    Yu, T.W.3    Zhou, H.M.4
  • 21
    • 0035847059 scopus 로고    scopus 로고
    • Identification of equilibrium and kinetic intermediates involved in folding of urea-denatured creatine kinase
    • Zhu L., Fan Y.-X., and Zhou J.-M. Identification of equilibrium and kinetic intermediates involved in folding of urea-denatured creatine kinase. Biochim. Biophys. Acta-Protein Struct. Mol. Enzymol. 1544 (2001) 320-332
    • (2001) Biochim. Biophys. Acta-Protein Struct. Mol. Enzymol. , vol.1544 , pp. 320-332
    • Zhu, L.1    Fan, Y.-X.2    Zhou, J.-M.3
  • 22
    • 0034811760 scopus 로고    scopus 로고
    • Relationship between kinetic and equilibrium folding intermediates of creatine kinase
    • Zhu L., Fan Y.X., Perrett S., and Zhou J.M. Relationship between kinetic and equilibrium folding intermediates of creatine kinase. Biochem. Biophys. Res. Commun. 285 (2001) 857-862
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , pp. 857-862
    • Zhu, L.1    Fan, Y.X.2    Perrett, S.3    Zhou, J.M.4
  • 23
    • 0037199455 scopus 로고    scopus 로고
    • Role of C-terminal sequences in the folding of muscle creatine kinase
    • Mazon H., Marcillat O., Vial C., and Clottes E. Role of C-terminal sequences in the folding of muscle creatine kinase. Biochemistry 41 (2002) 9646-9653
    • (2002) Biochemistry , vol.41 , pp. 9646-9653
    • Mazon, H.1    Marcillat, O.2    Vial, C.3    Clottes, E.4
  • 24
    • 33745389201 scopus 로고    scopus 로고
    • Impact of intra-subunit domain-domain interactions on creatine kinase activity and stability
    • Zhao T.-J., Feng S., Wang Y.-L., Liu Y., Luo X.-C., Zhou H.-M., and Yan Y.-B. Impact of intra-subunit domain-domain interactions on creatine kinase activity and stability. FEBS Lett. 580 (2006) 3835-3840
    • (2006) FEBS Lett. , vol.580 , pp. 3835-3840
    • Zhao, T.-J.1    Feng, S.2    Wang, Y.-L.3    Liu, Y.4    Luo, X.-C.5    Zhou, H.-M.6    Yan, Y.-B.7
  • 25
    • 0033532615 scopus 로고    scopus 로고
    • Reactivation and refolding of a partially folded creatine kinase modified by 5,5′-dithio-bis(2-nitrobenzoic acid)
    • Yang Y., Park Y.D., Yu T.W., and Zhou H.M. Reactivation and refolding of a partially folded creatine kinase modified by 5,5′-dithio-bis(2-nitrobenzoic acid). Biochem. Biophys. Res. Commun. 259 (1999) 450-454
    • (1999) Biochem. Biophys. Res. Commun. , vol.259 , pp. 450-454
    • Yang, Y.1    Park, Y.D.2    Yu, T.W.3    Zhou, H.M.4
  • 26
    • 0036994809 scopus 로고    scopus 로고
    • Subunit interaction slows the unfolding of the N-terminal domain of creatine kinase in urea
    • Guo Z., Wang Z., and Wang X.C. Subunit interaction slows the unfolding of the N-terminal domain of creatine kinase in urea. Biochemistry (Moscow) 67 (2002) 1388-1394
    • (2002) Biochemistry (Moscow) , vol.67 , pp. 1388-1394
    • Guo, Z.1    Wang, Z.2    Wang, X.C.3
  • 27
    • 25844454859 scopus 로고    scopus 로고
    • Conformational change in the C-terminal domain is responsible for the initiation of creatine kinase thermal aggregation
    • He H.-W., Zhang J., Zhou H.-M., and Yan Y.-B. Conformational change in the C-terminal domain is responsible for the initiation of creatine kinase thermal aggregation. Biophys. J. 89 (2005) 2650-2658
    • (2005) Biophys. J. , vol.89 , pp. 2650-2658
    • He, H.-W.1    Zhang, J.2    Zhou, H.-M.3    Yan, Y.-B.4
  • 29
    • 33646595045 scopus 로고    scopus 로고
    • The evolution from asparagine or threonine to cysteine in position 146 contributes to generation of a more efficient and stable form of muscle creatine kinase in higher vertebrates
    • Zhao T.-J., Liu Y., Chen Z., Yan Y.-B., and Zhou H.-M. The evolution from asparagine or threonine to cysteine in position 146 contributes to generation of a more efficient and stable form of muscle creatine kinase in higher vertebrates. Int. J. Biochem. Cell Biol. 38 (2006) 1614-1623
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 1614-1623
    • Zhao, T.-J.1    Liu, Y.2    Chen, Z.3    Yan, Y.-B.4    Zhou, H.-M.5
  • 31
    • 0346888757 scopus 로고    scopus 로고
    • Consequences of a six residual deletion from the N-terminal of rabbit muscle creatine kinase
    • Guo S.Y., Wang Z., Ni S.W., and Wang X.C. Consequences of a six residual deletion from the N-terminal of rabbit muscle creatine kinase. Biochimie 85 (2003) 999-1005
    • (2003) Biochimie , vol.85 , pp. 999-1005
    • Guo, S.Y.1    Wang, Z.2    Ni, S.W.3    Wang, X.C.4
  • 32
    • 34249730006 scopus 로고    scopus 로고
    • The generation of the oxidized form of creatine kinase is a negative regulation on muscle creatine kinase
    • Zhao T.-J., Yan Y.-B., Liu Y., and Zhou H.-M. The generation of the oxidized form of creatine kinase is a negative regulation on muscle creatine kinase. J. Biol. Chem. 282 (2007) 12022-12029
    • (2007) J. Biol. Chem. , vol.282 , pp. 12022-12029
    • Zhao, T.-J.1    Yan, Y.-B.2    Liu, Y.3    Zhou, H.-M.4
  • 33
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 0020344240 scopus 로고
    • A comparison of denaturation and inactivation rates of creatine kinase in guanidine solutions
    • Yao Q.-Z., Zhou H.-M., Hou L.-X., and Tsou C.-L. A comparison of denaturation and inactivation rates of creatine kinase in guanidine solutions. Sci. Sin. 25B (1982) 1296-1302
    • (1982) Sci. Sin. , vol.25 B , pp. 1296-1302
    • Yao, Q.-Z.1    Zhou, H.-M.2    Hou, L.-X.3    Tsou, C.-L.4
  • 36
    • 0030951992 scopus 로고    scopus 로고
    • Catalysis of the refolding of urea denatured creatine kinase by peptidyl-prolyl cis-trans isomerase
    • Yang H.P., Zhong H.N., and Zhou H.M. Catalysis of the refolding of urea denatured creatine kinase by peptidyl-prolyl cis-trans isomerase. Biochim. Biophys. Acta 1338 (1997) 147-150
    • (1997) Biochim. Biophys. Acta , vol.1338 , pp. 147-150
    • Yang, H.P.1    Zhong, H.N.2    Zhou, H.M.3
  • 37
    • 0034774703 scopus 로고    scopus 로고
    • Chaperone-like activity of peptidyl-prolyl cis-trans isomerase during creatine kinase refolding
    • Ou W.B., Luo W., Park Y.D., and Zhou H.M. Chaperone-like activity of peptidyl-prolyl cis-trans isomerase during creatine kinase refolding. Protein Sci. 10 (2001) 2346-2353
    • (2001) Protein Sci. , vol.10 , pp. 2346-2353
    • Ou, W.B.1    Luo, W.2    Park, Y.D.3    Zhou, H.M.4
  • 38
    • 0034877118 scopus 로고    scopus 로고
    • Decomposition of protein tryptophan fluorescence spectra into log-normal components. III. Correlation between fluorescence and microenvironment parameters of individual tryptophan residues
    • Reshetnyak Y.K., Koshevnik Y., and Burstein E.A. Decomposition of protein tryptophan fluorescence spectra into log-normal components. III. Correlation between fluorescence and microenvironment parameters of individual tryptophan residues. Biophys. J. 81 (2001) 1735-1758
    • (2001) Biophys. J. , vol.81 , pp. 1735-1758
    • Reshetnyak, Y.K.1    Koshevnik, Y.2    Burstein, E.A.3
  • 39
    • 40649100038 scopus 로고    scopus 로고
    • Blocking creatine kinase refolding by trace amounts of copper ions
    • Feng S., Xu Z., and Yan Y.-B. Blocking creatine kinase refolding by trace amounts of copper ions. J. Inorg. Biochem. 102 (2008) 928-935
    • (2008) J. Inorg. Biochem. , vol.102 , pp. 928-935
    • Feng, S.1    Xu, Z.2    Yan, Y.-B.3
  • 40
    • 0027502655 scopus 로고
    • Conformational changes at the active site of creatine kinase at low concentrations of guanidinium chloride
    • Zhou H.-M., Zhang X.-H., Yin Y., and Tsou C.-L. Conformational changes at the active site of creatine kinase at low concentrations of guanidinium chloride. Biochem. J. 291 (1993) 103-107
    • (1993) Biochem. J. , vol.291 , pp. 103-107
    • Zhou, H.-M.1    Zhang, X.-H.2    Yin, Y.3    Tsou, C.-L.4
  • 41
    • 41149180748 scopus 로고    scopus 로고
    • Effects of glycerol on the compaction and stability of the wild type and mutated rabbit muscle creatine kinase
    • Feng S., and Yan Y.-B. Effects of glycerol on the compaction and stability of the wild type and mutated rabbit muscle creatine kinase. Proteins: Struct, Funct, Bioinform. 71 (2008) 844-854
    • (2008) Proteins: Struct, Funct, Bioinform. , vol.71 , pp. 844-854
    • Feng, S.1    Yan, Y.-B.2
  • 42
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson C.M. Protein folding and misfolding. Nature 426 (2003) 884-890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 44
    • 0141567459 scopus 로고    scopus 로고
    • Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation
    • Chi E.Y., Krishnan S., Randolph T.W., and Carpenter J.F. Physical stability of proteins in aqueous solution: mechanism and driving forces in nonnative protein aggregation. Pharm. Res. 20 (2003) 1325-1336
    • (2003) Pharm. Res. , vol.20 , pp. 1325-1336
    • Chi, E.Y.1    Krishnan, S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 45
    • 0035880007 scopus 로고    scopus 로고
    • Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins
    • Butterfield D.A., and Kanski J. Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins. Mech. Ageing Dev. 122 (2001) 945-962
    • (2001) Mech. Ageing Dev. , vol.122 , pp. 945-962
    • Butterfield, D.A.1    Kanski, J.2
  • 46
    • 0034237719 scopus 로고    scopus 로고
    • Energetics in the pathogenesis of neurodegenerative diseases
    • Beal M.F. Energetics in the pathogenesis of neurodegenerative diseases. Trends Neurosci. 23 (2000) 298-304
    • (2000) Trends Neurosci. , vol.23 , pp. 298-304
    • Beal, M.F.1
  • 47
    • 0032515099 scopus 로고    scopus 로고
    • Crystal structure of rabbit muscle creatine kinase
    • Rao J.K., Bujacz G., and Wlodawer A. Crystal structure of rabbit muscle creatine kinase. FEBS Lett. 439 (1998) 133-137
    • (1998) FEBS Lett. , vol.439 , pp. 133-137
    • Rao, J.K.1    Bujacz, G.2    Wlodawer, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.