메뉴 건너뛰기




Volumn 106, Issue 43, 2009, Pages 18273-18278

Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization

Author keywords

Amyotrophic lateral sclerosis; Nuclear magnetic resonance relaxation; Protein misfolding

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; DIMER; DISULFIDE; METAL; OLIGOMER;

EID: 70849113863     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0907387106     Document Type: Article
Times cited : (71)

References (52)
  • 1
    • 33747605320 scopus 로고    scopus 로고
    • Molecular biology of amyotrophic lateral sclerosis: Insights from genetics
    • DOI 10.1038/nrn1971, PII NRN1971
    • Pasinelli P, Brown RH (2006) Molecular biology of amyotrophic lateral sclerosis: Insights from genetics. Nat Rev Neurosci 7:710-723. (Pubitemid 44267495)
    • (2006) Nature Reviews Neuroscience , vol.7 , Issue.9 , pp. 710-723
    • Pasinelli, P.1    Brown, R.H.2
  • 2
    • 22244479388 scopus 로고    scopus 로고
    • Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis
    • DOI 10.1146/annurev.biochem.72.121801.161647
    • Valentine JS, Doucette PA, Potter SZ (2005) Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis. Annu Rev Biochem 74:563-593. (Pubitemid 40995518)
    • (2005) Annual Review of Biochemistry , vol.74 , pp. 563-593
    • Valentine, J.S.1    Doucette, P.A.2    Potter, S.Z.3
  • 4
    • 0032544674 scopus 로고    scopus 로고
    • Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1
    • Bruijn LI, et al. (1998) Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science 281:1851-1854.
    • (1998) Science , vol.281 , pp. 1851-1854
    • Bruijn, L.I.1
  • 5
    • 0033749379 scopus 로고    scopus 로고
    • Formation of high molecular weight complexes of mutant Cu,Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis
    • Johnston JA, Dalton MJ, Gurney ME, Kopito RR (2000) Formation of high molecular weight complexes of mutant Cu,Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proc Natl Acad Sci USA 97:12571-12576.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12571-12576
    • Johnston, J.A.1    Dalton, M.J.2    Gurney, M.E.3    Kopito, R.R.4
  • 6
    • 0347358915 scopus 로고    scopus 로고
    • Minute quantities of misfolded mutant superoxide dismutase-1 cause amyotrophic lateral sclerosis
    • Jonsson PA, et al. (2004) Minute quantities of misfolded mutant superoxide dismutase-1 cause amyotrophic lateral sclerosis. Brain 127:73-88.
    • (2004) Brain , vol.127 , pp. 73-88
    • Jonsson, P.A.1
  • 8
    • 66049156169 scopus 로고    scopus 로고
    • Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS
    • Karch CM, Prudencio M, Winkler DD, Hart PJ, Borchelt DR (2009) Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALS. Proc Natl Acad Sci USA 106:7774-7779.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 7774-7779
    • Karch, C.M.1    Prudencio, M.2    Winkler, D.D.3    Hart, P.J.4    Borchelt, D.R.5
  • 9
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti F, Dobson CM (2009) Amyloid formation by globular proteins under native conditions. Nat Chem Biol 5:15-22.
    • (2009) Nat Chem Biol , vol.5 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2
  • 10
    • 33751212177 scopus 로고    scopus 로고
    • Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis
    • DOI 10.1016/j.bbadis.2006.05.004, PII S0925443906000846
    • Rakhit R, Chakrabartty A (2006) Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis. Biochim Biophys Acta 1762:1025-1037. (Pubitemid 44781177)
    • (2006) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1762 , Issue.11-12 , pp. 1025-1037
    • Rakhit, R.1    Chakrabartty, A.2
  • 11
    • 53049109088 scopus 로고    scopus 로고
    • Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis
    • Furukawa Y, Kaneko K, Yamanaka K, O'Halloran TV, Nukina N (2008) Complete loss of post-translational modifications triggers fibrillar aggregation of SOD1 in the familial form of amyotrophic lateral sclerosis. J Biol Chem 283:24167-24176.
    • (2008) J Biol Chem , vol.283 , pp. 24167-24176
    • Furukawa, Y.1    Kaneko, K.2    Yamanaka, K.3    O'Halloran, T.V.4    Nukina, N.5
  • 12
    • 2442624720 scopus 로고    scopus 로고
    • Monomeric Cu,Zn-superoxide Dismutase Is a Common Misfolding Intermediate in the Oxidation Models of Sporadic and Familial Amyotrophic Lateral Sclerosis
    • DOI 10.1074/jbc.M313295200
    • Rakhit R, et al. (2004) Monomeric Cu,Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis. J Biol Chem 279:15499-15504. (Pubitemid 38618950)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.15 , pp. 15499-15504
    • Rakhit, R.1    Crow, J.P.2    Lepock, J.R.3    Kondejewski, L.H.4    Cashman, N.R.5    Chakrabartty, A.6
  • 13
    • 6344277909 scopus 로고    scopus 로고
    • The rate and equilibrium constants for a multistep reaction sequence for the aggregation of superoxide dismutase in amyotrophic lateral sclerosis
    • DOI 10.1073/pnas.0406650101
    • Khare SD, Caplow M, Dokholyan NV (2004) The rate and equilibrium constants for a multistep reaction sequence for the aggregation of superoxide dismutase in amyotrophic lateral sclerosis. Proc Natl Acad Sci USA 101:15094-15099. (Pubitemid 39391724)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.42 , pp. 15094-15099
    • Khare, S.D.1    Caplow, M.2    Dokholyan, N.V.3
  • 16
    • 57749100302 scopus 로고    scopus 로고
    • Initiation and elongation in fibrillation of ALS-linked superoxide dismutase
    • Chattopadhyay M, et al. (2008) Initiation and elongation in fibrillation of ALS-linked superoxide dismutase. Proc Natl Acad Sci USA 105:18663-18668.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 18663-18668
    • Chattopadhyay, M.1
  • 17
    • 58149402390 scopus 로고    scopus 로고
    • Dynamical roles of metal ions and the disulfide bond in Cu,Zn superoxide dismutase folding and aggregation
    • Ding F, Dokholyan NV (2008) Dynamical roles of metal ions and the disulfide bond in Cu,Zn superoxide dismutase folding and aggregation. Proc Natl Acad Sci USA 105:19696-19701.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 19696-19701
    • Ding, F.1    Dokholyan, N.V.2
  • 18
    • 66349087949 scopus 로고    scopus 로고
    • Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutants
    • Banci L, et al. (2009) Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutants. Proc Natl Acad Sci USA 106:6980-6985.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 6980-6985
    • Banci, L.1
  • 19
    • 67649852607 scopus 로고    scopus 로고
    • Functional features cause misfolding of the ALS-provoking enzyme SOD1
    • Nordlund A, et al. (2009) Functional features cause misfolding of the ALS-provoking enzyme SOD1. Proc Natl Acad Sci USA 106:9667-9672.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9667-9672
    • Nordlund, A.1
  • 21
    • 33846978054 scopus 로고    scopus 로고
    • Impaired post-translational folding of familial ALS-linked Cu,Zn superoxide dismutase mutants
    • Bruns CK, Kopito RR (2007) Impaired post-translational folding of familial ALS-linked Cu,Zn superoxide dismutase mutants. EMBO J 26:855-866.
    • (2007) EMBO J , vol.26 , pp. 855-866
    • Bruns, C.K.1    Kopito, R.R.2
  • 22
    • 9144261759 scopus 로고    scopus 로고
    • The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status
    • DOI 10.1074/jbc.M406021200
    • Arnesano F, et al. (2004) The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status. J Biol Chem 279:47998-48003. (Pubitemid 39540952)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.46 , pp. 47998-48003
    • Arnesano, F.1    Banci, L.2    Bertini, I.3    Martinelli, M.4    Furukawa, Y.5    O'Halloran, T.V.6
  • 23
    • 38149115471 scopus 로고    scopus 로고
    • Cysteine 111 affects aggregation and cytotoxicity of mutant Cu,Zn-superoxide dismutase associated with familial amyotrophic lateral sclerosis
    • Cozzolino M, et al. (2007) Cysteine 111 affects aggregation and cytotoxicity of mutant Cu,Zn-superoxide dismutase associated with familial amyotrophic lateral sclerosis. J Biol Chem 283:866-874.
    • (2007) J Biol Chem , vol.283 , pp. 866-874
    • Cozzolino, M.1
  • 25
    • 0038247520 scopus 로고    scopus 로고
    • Solution structure of apo Cu,Zn superoxide dismutase: Role of metal ions in protein folding
    • DOI 10.1021/bi034324m
    • Banci L, Bertini I, Cramaro F, Del CR, Viezzoli MS (2003) Solution structure of Apo Cu,Zn superoxide dismutase: Role of metal ions in protein folding. Biochemistry 42:9543-9553. (Pubitemid 37006303)
    • (2003) Biochemistry , vol.42 , Issue.32 , pp. 9543-9553
    • Banci, L.1    Bertini, I.2    Cramaro, F.3    Del Conte, R.4    Viezzoli, M.S.5
  • 26
    • 0034919305 scopus 로고    scopus 로고
    • Nuclear magnetic resonance methods for quantifying microsecond-to- millisecond motions in biological macromolecules
    • Palmer AG, Kroenke CD, Loria JP (2001) Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol 339:204-238.
    • (2001) Methods Enzymol , vol.339 , pp. 204-238
    • Palmer, A.G.1    Kroenke, C.D.2    Loria, J.P.3
  • 27
    • 33645834303 scopus 로고    scopus 로고
    • New tools provide new insights in NMR studies of protein dynamics
    • Mittermaier A, Kay LE (2006) New tools provide new insights in NMR studies of protein dynamics. Science 312:224-228.
    • (2006) Science , vol.312 , pp. 224-228
    • Mittermaier, A.1    Kay, L.E.2
  • 28
    • 34547120448 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-associated copper/zinc superoxide dismutase mutations preferentially reduce the repulsive charge of the proteins
    • DOI 10.1074/jbc.M700765200
    • Sandelin E, Nordlund A, Andersen PM, Marklund SL, Oliveberg M (2007) Amyotrophic lateral sclerosis-associated copper/zinc superoxide dismutase mutations preferentially reduce the repulsive charge of the proteins. J Biol Chem 282:21230-21236. (Pubitemid 47099916)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.29 , pp. 21230-21236
    • Sandelin, E.1    Nordlund, A.2    Andersen, P.M.3    Marklund, S.S.L.4    Oliveberg, M.5
  • 29
    • 0036814981 scopus 로고    scopus 로고
    • 13C chemical shift statistics
    • DOI 10.1023/A:1020997118364
    • Schubert M, Labudde D, Oschkinat H, Schmieder P (2002) A software tool for the prediction of Xaa-Pro peptide bond conformations in proteins based on C-13 chemical shift statistics. J Biomol NMR 24:149-154. (Pubitemid 35414678)
    • (2002) Journal of Biomolecular NMR , vol.24 , Issue.2 , pp. 149-154
    • Schubert, M.1    Labudde, D.2    Oschkinat, H.3    Schmieder, P.4
  • 30
    • 0037184476 scopus 로고    scopus 로고
    • Investigation of the neighboring residue effects on protein chemical shifts
    • DOI 10.1021/ja026811f
    • Wang Y, Jardetzky O (2002) Investigation of the neighboring residue effects on protein chemical shifts. J Am Chem Soc 124:14075-14084. (Pubitemid 35386860)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.47 , pp. 14075-14084
    • Wang, Y.1    Jardetzky, O.2
  • 31
    • 33846561471 scopus 로고    scopus 로고
    • 1H transverse paramagnetic relaxation enhancement measurements on macromolecules
    • DOI 10.1016/j.jmr.2006.10.003, PII S109078070600334X
    • Iwahara J, Tang C, Clore GM (2007) Practical aspects of H-1 transverse paramagnetic relaxation enhancement measurements on macromolecules. J Magn Reson 184:185-195. (Pubitemid 46177665)
    • (2007) Journal of Magnetic Resonance , vol.184 , Issue.2 , pp. 185-195
    • Iwahara, J.1    Tang, C.2    Marius Clore, G.3
  • 33
    • 23044431627 scopus 로고    scopus 로고
    • Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis
    • Rodriguez JA, et al. (2005) Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis. Proc Natl Acad Sci USA 102:10516-10521.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 10516-10521
    • Rodriguez, J.A.1
  • 34
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar RS, Record MT (1994) Coupling of local folding to site-specific binding of proteins to DNA. Science 263:777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record, M.T.2
  • 35
    • 0037427449 scopus 로고    scopus 로고
    • The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis
    • Strange RW, et al. (2003) The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis. J Mol Biol 328:877-891.
    • (2003) J Mol Biol , vol.328 , pp. 877-891
    • Strange, R.W.1
  • 36
    • 0038442784 scopus 로고    scopus 로고
    • Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS
    • Elam JS, et al. (2003) Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS. Nat Struct Biol 10:461-467.
    • (2003) Nat Struct Biol , vol.10 , pp. 461-467
    • Elam, J.S.1
  • 38
    • 0037022563 scopus 로고    scopus 로고
    • Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation
    • Richardson JS, Richardson DC (2002) Natural β-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci USA 99:2754-2759.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2754-2759
    • Richardson, J.S.1    Richardson, D.C.2
  • 39
    • 33144467755 scopus 로고    scopus 로고
    • Amyloid formation under physiological conditions proceeds via a native-like folding intermediate
    • Jahn TR, Parker MJ, Homans SW, Radford SE (2006) Amyloid formation under physiological conditions proceeds via a native-like folding intermediate. Nat Struct Mol Biol 13:195-201.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 195-201
    • Jahn, T.R.1    Parker, M.J.2    Homans, S.W.3    Radford, S.E.4
  • 40
    • 37249017468 scopus 로고    scopus 로고
    • Systematic in vivo analysis of the intrinsic determinants of amyloid b pathogeneicity
    • Luheshi LM, et al. (2007) Systematic in vivo analysis of the intrinsic determinants of amyloid b pathogeneicity. PLOS Biol 5:2493-2500.
    • (2007) PLOS Biol , vol.5 , pp. 2493-2500
    • Luheshi, L.M.1
  • 42
    • 33745889333 scopus 로고    scopus 로고
    • Folding of Cu/Zn superoxide dismutase suggests structural hotspots for gain of neurotoxic function in ALS: Parallels to precursors in amyloid disease
    • DOI 10.1073/pnas.0601696103
    • Nordlund A, Oliveberg M (2006) Folding of Cu/Zn superoxide dismutase suggests structural hotspots for gain of neurotoxic function in ALS: Parallels to precursors in amyloid disease. Proc Natl Acad Sci USA 103:10218-10223. (Pubitemid 44051147)
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , Issue.27 , pp. 10218-10223
    • Nordlund, A.1    Oliveberg, M.2
  • 43
    • 3242880292 scopus 로고    scopus 로고
    • Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR
    • Korzhnev DM, et al. (2004) Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR. Nature 430:586-590.
    • (2004) Nature , vol.430 , pp. 586-590
    • Korzhnev, D.M.1
  • 44
    • 33646466296 scopus 로고    scopus 로고
    • Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria
    • Deng H-X, et al. (2006) Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria. Proc Natl Acad Sci USA 103:7142-7147.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 7142-7147
    • Deng, H.-X.1
  • 46
    • 0033577288 scopus 로고    scopus 로고
    • A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy [13]
    • DOI 10.1021/ja983961a
    • Loria JP, Rance M, Palmer AG (1999) A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy. J Am Chem Soc 121:2331-2332. (Pubitemid 29152458)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.10 , pp. 2331-2332
    • Loria, J.P.1    Rance, M.2    Palmer III, A.G.3
  • 47
    • 0035819455 scopus 로고    scopus 로고
    • 15N relaxation dispersion NMR spectroscopy: Application to Asn and Gln residues in a cavity mutant of T4 lysozyme
    • DOI 10.1021/ja003447g
    • Mulder FAA, Skrynnikov NR, Hon B, Dahlquist FW, Kay LE (2001) Measurement of slow (microseconds-milliseconds) time scale dynamics in protein side chains by 15N relaxation dispersion NMR spectroscopy: Application to Asn and Gln residues in a cavity mutant of T4 lysozyme. J Am Chem Soc 123:967-975. (Pubitemid 32151376)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.5 , pp. 967-975
    • Mulder, F.A.A.1    Skrynnikov, N.R.2    Hon, B.3    Dahlquist, F.W.4    Kay, L.E.5
  • 48
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio F, et al. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277-293.
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1
  • 51
    • 0028941877 scopus 로고
    • Backbone dynamics of Eschericia coli ribonuclease HI: Correlations with structure and function in an active enzyme
    • Mandel AM, Akke M, Palmer AG (1995) Backbone dynamics of Eschericia coli ribonuclease HI: Correlations with structure and function in an active enzyme. J Mol Biol 246:144-163.
    • (1995) J Mol Biol , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.