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Volumn 47, Issue 8, 2008, Pages 2510-2517

Raman optical activity and circular dichroism reveal dramatic differences in the influence of divalent copper and manganese ions on prion protein folding

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING SITES; DICHROISM; MANGANESE COMPOUNDS;

EID: 39749155839     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7022893     Document Type: Article
Times cited : (42)

References (55)
  • 1
    • 0032506187 scopus 로고    scopus 로고
    • Prusiner, S. B. (1998) Prions, Proc. Natl. Acad. Sci. U.S.A. 95, 13363-13383.
    • Prusiner, S. B. (1998) Prions, Proc. Natl. Acad. Sci. U.S.A. 95, 13363-13383.
  • 2
    • 0031711595 scopus 로고    scopus 로고
    • Pathologic conformations of prion proteins
    • Cohen, F. E., and Prusiner, S. B. (1998) Pathologic conformations of prion proteins, Annu. Rev. Biochem. 67, 793-819.
    • (1998) Annu. Rev. Biochem , vol.67 , pp. 793-819
    • Cohen, F.E.1    Prusiner, S.B.2
  • 3
    • 33749822624 scopus 로고    scopus 로고
    • The Emerging Principles of Mammalian Prion Propagation and Transmissibility Barriers: Insight from Studies in Vitro
    • Surewicz, W. K., Jones, E. M., and Apetri, A. C. (2006) The Emerging Principles of Mammalian Prion Propagation and Transmissibility Barriers: Insight from Studies in Vitro, Accs. Chem. Res. 39, 654-662.
    • (2006) Accs. Chem. Res , vol.39 , pp. 654-662
    • Surewicz, W.K.1    Jones, E.M.2    Apetri, A.C.3
  • 4
    • 33749839721 scopus 로고    scopus 로고
    • Prions and Transmissible Spongiform Encephalopathy (TSE) Chemotherapeutics: A Common Mechanism for Anti-TSE Compounds
    • Caughey, B., Caughey, W. S., Kocisko, D. A., Lee, K. S., Silveira, J. R., and Morrey, J. D. (2006) Prions and Transmissible Spongiform Encephalopathy (TSE) Chemotherapeutics: A Common Mechanism for Anti-TSE Compounds, Acc. Chem. Res. 39, 646-653.
    • (2006) Acc. Chem. Res , vol.39 , pp. 646-653
    • Caughey, B.1    Caughey, W.S.2    Kocisko, D.A.3    Lee, K.S.4    Silveira, J.R.5    Morrey, J.D.6
  • 6
    • 0029914594 scopus 로고    scopus 로고
    • Semipreparative chromatographic method to purify the normal cellular isoform of the prion protein in nondenatured form
    • Pergamini, P., Jaffe, H., and Safar, J. (1996) Semipreparative chromatographic method to purify the normal cellular isoform of the prion protein in nondenatured form, Anal. Biochem. 236, 63-73.
    • (1996) Anal. Biochem , vol.236 , pp. 63-73
    • Pergamini, P.1    Jaffe, H.2    Safar, J.3
  • 7
    • 0034931126 scopus 로고    scopus 로고
    • Three-dimensional structures of prion proteins
    • Wüthrich, K., and Riek, R. (2001) Three-dimensional structures of prion proteins, Adv. Prot. Chem. 57, 55-82.
    • (2001) Adv. Prot. Chem , vol.57 , pp. 55-82
    • Wüthrich, K.1    Riek, R.2
  • 9
    • 0033485880 scopus 로고    scopus 로고
    • Prion protein expression aids cellular uptake and veratridine-induced release of copper
    • Brown, D. R. (1999) Prion protein expression aids cellular uptake and veratridine-induced release of copper, J. Neurosci. Res. 58, 717-725.
    • (1999) J. Neurosci. Res , vol.58 , pp. 717-725
    • Brown, D.R.1
  • 11
    • 0035158321 scopus 로고    scopus 로고
    • Anti-oxidant activity related to copper binding of native prion protein
    • Brown, D. R., Clive, C., and Haswell, S. (2001) Anti-oxidant activity related to copper binding of native prion protein, J. Neurochem. 76, 69-76.
    • (2001) J. Neurochem , vol.76 , pp. 69-76
    • Brown, D.R.1    Clive, C.2    Haswell, S.3
  • 12
    • 34249941302 scopus 로고    scopus 로고
    • Copper and the prion protein: Methods, structures, function, and disease
    • Millhauser, G. L. (2006) Copper and the prion protein: methods, structures, function, and disease, Ann. Rev. Phys. Chem. 58, 299-320.
    • (2006) Ann. Rev. Phys. Chem. 58 , pp. 299-320
    • Millhauser, G.L.1
  • 14
    • 0037083888 scopus 로고    scopus 로고
    • Metal imbalance and compromised antioxidant function are early changes in prion disease
    • Thackray, A. M., Knight, R., Haswell, S. J., Bujdoso, R., and Brown, D. R. (2002) Metal imbalance and compromised antioxidant function are early changes in prion disease, Biochem. J. 362, 253-258.
    • (2002) Biochem. J , vol.362 , pp. 253-258
    • Thackray, A.M.1    Knight, R.2    Haswell, S.J.3    Bujdoso, R.4    Brown, D.R.5
  • 15
    • 0034654304 scopus 로고    scopus 로고
    • Consequences of manganese replacement of copper for prion protein function and proteinase resistance
    • Brown, D. R., Hafiz, F., Glasssmith, L. L., Wong, B.-S., Jones, I. M., Clive, C., and Haswell, S. J. (2000) Consequences of manganese replacement of copper for prion protein function and proteinase resistance, EMBO J. 19, 1180-1186.
    • (2000) EMBO J , vol.19 , pp. 1180-1186
    • Brown, D.R.1    Hafiz, F.2    Glasssmith, L.L.3    Wong, B.-S.4    Jones, I.M.5    Clive, C.6    Haswell, S.J.7
  • 16
    • 33744766845 scopus 로고    scopus 로고
    • Effect of copper and manganese on the de novo generation of protease-resistant prion protein in yeast cells
    • Treiber, C., Simons, A., and Multhaup, G. (2006) Effect of copper and manganese on the de novo generation of protease-resistant prion protein in yeast cells, Biochemistry 45, 6674-6680.
    • (2006) Biochemistry , vol.45 , pp. 6674-6680
    • Treiber, C.1    Simons, A.2    Multhaup, G.3
  • 17
    • 0033515029 scopus 로고    scopus 로고
    • Copper binding to the prion protein: Structural implications of four identical cooperative binding sites
    • Viles, J. H., Cohen, F. E., Prusiner, S. B., Goodin, D. B., Wright, P. E., and Dyson, H. J. (1999) Copper binding to the prion protein: Structural implications of four identical cooperative binding sites, Proc. Natl. Acad. Sci. U.S.A. 96, 2042-2047.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 2042-2047
    • Viles, J.H.1    Cohen, F.E.2    Prusiner, S.B.3    Goodin, D.B.4    Wright, P.E.5    Dyson, H.J.6
  • 18
    • 3542999252 scopus 로고    scopus 로고
    • 111 induces β-sheet formation in the unstructured amyloidogenic region of the prion protein
    • 111 induces β-sheet formation in the unstructured amyloidogenic region of the prion protein, J. Biol. Chem. 279, 32018-32027.
    • (2004) J. Biol. Chem , vol.279 , pp. 32018-32027
    • Jones, C.E.1    Abdelraheim, S.R.2    Brown, D.R.3    Viles, J.H.4
  • 21
    • 30044443305 scopus 로고    scopus 로고
    • High affinity binding between copper and full-length prion protein identified by two different techniques
    • Thompsett, A. R., Abdelraheim, S. R., Daniels, M., and Brown, D. R. (2005) High affinity binding between copper and full-length prion protein identified by two different techniques, J. Biol. Chem. 280, 42750-42758.
    • (2005) J. Biol. Chem , vol.280 , pp. 42750-42758
    • Thompsett, A.R.1    Abdelraheim, S.R.2    Daniels, M.3    Brown, D.R.4
  • 22
    • 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. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 26444497106 scopus 로고    scopus 로고
    • Raman optical activity: A tool for protein structure analysis
    • Zhu, F., Isaacs, N. W., Hecht, L., and Barron, L. D. (2005) Raman optical activity: a tool for protein structure analysis, Structure 13, 1409-1419.
    • (2005) Structure , vol.13 , pp. 1409-1419
    • Zhu, F.1    Isaacs, N.W.2    Hecht, L.3    Barron, L.D.4
  • 25
    • 23444456924 scopus 로고    scopus 로고
    • How to study proteins by circular dichroism
    • Kelly, S. M., Jess, T. J., and Price, N. C. (2005) How to study proteins by circular dichroism, Biochim. Biophys. Acta 1751, 119-139.
    • (2005) Biochim. Biophys. Acta , vol.1751 , pp. 119-139
    • Kelly, S.M.1    Jess, T.J.2    Price, N.C.3
  • 26
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from CD spectra: Comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set
    • Sreerama, N., and Woody, R. W. (2000) Estimation of protein secondary structure from CD spectra: Comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set, Anal. Biochem. 287 (2), 252-260.
    • (2000) Anal. Biochem , vol.287 , Issue.2 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 27
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB: An online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore, L., and Wallace, B. A. (2004) DICHROWEB: an online server for protein secondary structure analyses from circular dichroism spectroscopic data, Nucleic Acids Res. 32, W668-673.
    • (2004) Nucleic Acids Res , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 29
    • 33749057923 scopus 로고    scopus 로고
    • Structure and behaviour of biomolecules from Raman optical activity
    • Barron, L. D. (2006) Structure and behaviour of biomolecules from Raman optical activity, Curr. Opin. Struct. Biol. 16, 638-643.
    • (2006) Curr. Opin. Struct. Biol , vol.16 , pp. 638-643
    • Barron, L.D.1
  • 30
    • 0041519431 scopus 로고    scopus 로고
    • A new perspective on β-sheet structures using vibrational Raman optical activity: From poly(L-lysine) to the prion protein
    • McColl, I. H., Blanch, E. W., Gill, A. C., Rhie, A. G. O., Ritchie, M, A., Hecht, L., Nielsen, K., and Barron, L. D. (2003) A new perspective on β-sheet structures using vibrational Raman optical activity: from poly(L-lysine) to the prion protein, J. Am. Chem. Soc. 125, 10019-10026.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 10019-10026
    • McColl, I.H.1    Blanch, E.W.2    Gill, A.C.3    Rhie, A.G.O.4    Ritchie, M.A.5    Hecht, L.6    Nielsen, K.7    Barron, L.D.8
  • 31
    • 3042850001 scopus 로고    scopus 로고
    • A study of α-helix hydration in polypeptides, proteins and viruses using vibrational Raman optical activity
    • McColl, I. H., Blanch, E. W., Hecht, L., and Barron, L. D. (2004) A study of α-helix hydration in polypeptides, proteins and viruses using vibrational Raman optical activity, J. Am. Chem. Soc. 126, 8181-8188.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 8181-8188
    • McColl, I.H.1    Blanch, E.W.2    Hecht, L.3    Barron, L.D.4
  • 32
    • 4644372554 scopus 로고    scopus 로고
    • Raman optical activity demonstrates poly(L-proline) II helix in the N-terminal region of the ovine prion protein: Implications for function and misfunction
    • Blanch, E. W., Gill, A. C., Rhie, A. G. O., Hope, J., Hecht, L., Nielsen, K., and Barron, L. D. (2004) Raman optical activity demonstrates poly(L-proline) II helix in the N-terminal region of the ovine prion protein: implications for function and misfunction, J. Mol. Biol. 343, 467-476.
    • (2004) J. Mol. Biol , vol.343 , pp. 467-476
    • Blanch, E.W.1    Gill, A.C.2    Rhie, A.G.O.3    Hope, J.4    Hecht, L.5    Nielsen, K.6    Barron, L.D.7
  • 33
    • 1942489291 scopus 로고    scopus 로고
    • Vibrational Raman optical activity characterization of poly(L-proline) II helix in alanine oligopeptides
    • McColl, I. H., Blanch, E. W., Hecht, L., Kallenbach, N. R., and Barron, L. D. (2004) Vibrational Raman optical activity characterization of poly(L-proline) II helix in alanine oligopeptides, J. Am. Chem. Soc. 126, 5076-5077.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 5076-5077
    • McColl, I.H.1    Blanch, E.W.2    Hecht, L.3    Kallenbach, N.R.4    Barron, L.D.5
  • 34
    • 33748770091 scopus 로고    scopus 로고
    • Delineation of protein structure classes from multivariate analysis of protein Raman optical activity data
    • Zhu, F., Tranter, G. E., Isaacs, N. W., Hecht, L., and Barron, L. D. (2006) Delineation of protein structure classes from multivariate analysis of protein Raman optical activity data, J. Mol. Biol. 363, 19-26.
    • (2006) J. Mol. Biol , vol.363 , pp. 19-26
    • Zhu, F.1    Tranter, G.E.2    Isaacs, N.W.3    Hecht, L.4    Barron, L.D.5
  • 35
    • 38549110665 scopus 로고    scopus 로고
    • Residual structure in disordered peptides and unfolded proteins from multivariate analysis and ab initio simulation of Raman optical activity data
    • Zhu, F., Kapitan, J., Tranter, G. E., Pudney, P. D. A., Isaacs, N. W., Hecht, L., and Barron, L. D. (2008) Residual structure in disordered peptides and unfolded proteins from multivariate analysis and ab initio simulation of Raman optical activity data, Proteins, 70, 823-833.
    • (2008) Proteins , vol.70 , pp. 823-833
    • Zhu, F.1    Kapitan, J.2    Tranter, G.E.3    Pudney, P.D.A.4    Isaacs, N.W.5    Hecht, L.6    Barron, L.D.7
  • 36
    • 0035478472 scopus 로고    scopus 로고
    • Synchrotron radiation circular dichroism spectroscopy of proteins: Secondary structure, fold recognition and structural genomics
    • Wallace, B. A., and Janes, R. W. (2001) Synchrotron radiation circular dichroism spectroscopy of proteins: secondary structure, fold recognition and structural genomics, Curr. Opin. Chem. Biol. 5, 567-571.
    • (2001) Curr. Opin. Chem. Biol , vol.5 , pp. 567-571
    • Wallace, B.A.1    Janes, R.W.2
  • 38
    • 34250802050 scopus 로고    scopus 로고
    • Dual polarisation interferometry analysis of copper binding to the prion protein: Evidence for two folding states
    • Thompsett, A. R., and Brown, D. R. (2007) Dual polarisation interferometry analysis of copper binding to the prion protein: evidence for two folding states, Biochim. Biophys. Acta 1774, 920-927.
    • (2007) Biochim. Biophys. Acta , vol.1774 , pp. 920-927
    • Thompsett, A.R.1    Brown, D.R.2
  • 42
    • 0041315527 scopus 로고    scopus 로고
    • Influence of pH on NMR structure and stability of the human prion protein globular domain
    • Calzolai, L., and Zahn, R. (2003) Influence of pH on NMR structure and stability of the human prion protein globular domain, J. Biol. Chem. 278, 35592-35596.
    • (2003) J. Biol. Chem , vol.278 , pp. 35592-35596
    • Calzolai, L.1    Zahn, R.2
  • 45
    • 0036646546 scopus 로고    scopus 로고
    • Metal ions bound at the active site of the junction-resolving enzyme T7 endonuclease I
    • Hadden, J. M., Déclais, A.-C., Phillips, S. E. V., and Lilley, D. M. J. (2002) Metal ions bound at the active site of the junction-resolving enzyme T7 endonuclease I, EMBO J. 21, 3505-3515.
    • (2002) EMBO J , vol.21 , pp. 3505-3515
    • Hadden, J.M.1    Déclais, A.-C.2    Phillips, S.E.V.3    Lilley, D.M.J.4
  • 51
    • 2942616602 scopus 로고    scopus 로고
    • Evidence for assembly of prions with left-handed β-helices into trimers
    • Govaerts, C., Wille, H., Prusiner, S. B., and Cohen, F. E. (2004) Evidence for assembly of prions with left-handed β-helices into trimers, Proc. Natl. Acad. Sci. U.S.A. 101, 8342-8347.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 8342-8347
    • Govaerts, C.1    Wille, H.2    Prusiner, S.B.3    Cohen, F.E.4
  • 52
    • 12144271772 scopus 로고    scopus 로고
    • NMR structure of the bovine prion protein isolated from healthy calf brains,
    • 5
    • Hornemann, S., Schorn, C., and Wüthrich, K. (2004) NMR structure of the bovine prion protein isolated from healthy calf brains, EMBO Rep. 5, 1159-1164.
    • (2004) EMBO Rep , pp. 1159-1164
    • Hornemann, S.1    Schorn, C.2    Wüthrich, K.3
  • 53
    • 0033807078 scopus 로고    scopus 로고
    • Carbohydrates as ligands: Coordination equilibria and structure of the metal complexes
    • Gyurcsik, B., and Nagy, L. (2000) Carbohydrates as ligands: coordination equilibria and structure of the metal complexes, Coord. Chem. Rev. 203, 81-149.
    • (2000) Coord. Chem. Rev , vol.203 , pp. 81-149
    • Gyurcsik, B.1    Nagy, L.2
  • 54
    • 0022000573 scopus 로고
    • Scrapie PrP 27-30 is a sialoglycoprotein
    • Bolton, D. C., Meyer, R. K., and Prusiner, S. B. (1985) Scrapie PrP 27-30 is a sialoglycoprotein, J. Virol. 53, 596-606.
    • (1985) J. Virol , vol.53 , pp. 596-606
    • Bolton, D.C.1    Meyer, R.K.2    Prusiner, S.B.3
  • 55
    • 16244403611 scopus 로고    scopus 로고
    • Coordination modes between copper (II) and N-acetylneuraminic (sialic) acid from a 2D simulation analysis of EPR spectra. Implications for copper mediation of sialoglyco-conjugate chemistry relevant to human biology
    • Fainerman-Melnikova, M., Szabó-Plánka, T., Rockenbauer, A., and Codd, R. (2005) Coordination modes between copper (II) and N-acetylneuraminic (sialic) acid from a 2D simulation analysis of EPR spectra. Implications for copper mediation of sialoglyco-conjugate chemistry relevant to human biology, Inorg. Chem. 44, 2531-2543.
    • (2005) Inorg. Chem , vol.44 , pp. 2531-2543
    • Fainerman-Melnikova, M.1    Szabó-Plánka, T.2    Rockenbauer, A.3    Codd, R.4


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