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Volumn 75, Issue 2, 2009, Pages 509-517

The osmolyte betaine promotes protein misfolding and disruption of protein aggregates

Author keywords

Aggregation; Circular dichroism; Disaggregation; Dynamic light scattering; Fourier transform infrared spectroscopy; Oligomers; Osmolytes; Protein destabilization; Protein stability

Indexed keywords

BETAINE; GLUTATHIONE TRANSFERASE; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; THIOFLAVINE; PEPTIDE HYDROLASE;

EID: 66149143156     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22266     Document Type: Article
Times cited : (58)

References (48)
  • 1
    • 43149110398 scopus 로고    scopus 로고
    • Intracellular organic osmolytes: Function and regulation
    • Burg MB, Ferraris JD. Intracellular organic osmolytes: function and regulation. J Biol Chem 2008;283:7309-7313.
    • (2008) J Biol Chem , vol.283 , pp. 7309-7313
    • Burg, M.B.1    Ferraris, J.D.2
  • 2
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross CA, Poirier MA. Protein aggregation and neurodegenerative disease. Nat Med 2004;10:S10-S17.
    • (2004) Nat Med , vol.10
    • Ross, C.A.1    Poirier, M.A.2
  • 3
    • 23044456332 scopus 로고    scopus 로고
    • Characterization of the aggregates formed during recombinant protein expression in bacteria
    • Schrodel A, de Marco A. Characterization of the aggregates formed during recombinant protein expression in bacteria. BMC Biochem 2005;6:10.
    • (2005) BMC Biochem , vol.6 , pp. 10
    • Schrodel, A.1    de Marco, A.2
  • 6
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson CM. Protein folding and misfolding. Nature 2003;426:884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 7
    • 0035839035 scopus 로고    scopus 로고
    • Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain
    • Zurdo J, Guijarro JL, Jimenez JL, Saibil HR, Dobson CM. Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain. J Mol Biol 2001;311:325-340.
    • (2001) J Mol Biol , vol.311 , pp. 325-340
    • Zurdo, J.1    Guijarro, J.L.2    Jimenez, J.L.3    Saibil, H.R.4    Dobson, C.M.5
  • 8
    • 12544259221 scopus 로고    scopus 로고
    • Re versal of protein aggregation provides evidence for multiple aggregated states
    • Calamai M, Canale C, Relini A, Stefani M, Chiti F, Dobson CM. Re versal of protein aggregation provides evidence for multiple aggregated states. J Mol Biol 2005;346:603-616.
    • (2005) J Mol Biol , vol.346 , pp. 603-616
    • Calamai, M.1    Canale, C.2    Relini, A.3    Stefani, M.4    Chiti, F.5    Dobson, C.M.6
  • 9
    • 16344385440 scopus 로고    scopus 로고
    • Oxidative metabolites accelerate Alzheimer's amyloidogenesis by a two-step mechanism, eliminating the requirement for nucleation
    • Bieschke J, Zhang Q, Powers ET, Lerner RA, Kelly JW. Oxidative metabolites accelerate Alzheimer's amyloidogenesis by a two-step mechanism, eliminating the requirement for nucleation. Biochemistry 2005;44:4977-983.
    • (2005) Biochemistry , vol.44 , pp. 4977-4983
    • Bieschke, J.1    Zhang, Q.2    Powers, E.T.3    Lerner, R.A.4    Kelly, J.W.5
  • 10
    • 39649101910 scopus 로고    scopus 로고
    • Physical and chemical perturbations induce the formation of protein aggregates with different structural features
    • Natalello A, Santarella R, Doglia SM, de Marco A. Physical and chemical perturbations induce the formation of protein aggregates with different structural features. Prot Expr Purif 2008;58: 356-361.
    • (2008) Prot Expr Purif , vol.58 , pp. 356-361
    • Natalello, A.1    Santarella, R.2    Doglia, S.M.3    de Marco, A.4
  • 11
    • 33748588165 scopus 로고    scopus 로고
    • Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant
    • Ignatova Z, Gierasch LM. Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant. Proc Natl Acad Sci USA 2006;103:13357- 13361.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13357-13361
    • Ignatova, Z.1    Gierasch, L.M.2
  • 12
    • 1842850631 scopus 로고    scopus 로고
    • Inhibition of insulin amyloid formation by small stress molecules
    • Arora A, Ha C, Park CB. Inhibition of insulin amyloid formation by small stress molecules. FEBS Lett 2004;564:121-125.
    • (2004) FEBS Lett , vol.564 , pp. 121-125
    • Arora, A.1    Ha, C.2    Park, C.B.3
  • 14
    • 0035976814 scopus 로고    scopus 로고
    • Trimethylamine-N-oxide-induced folding of alpha-synuclein
    • Uversky VN, Li J, Fink AL. Trimethylamine-N-oxide-induced folding of alpha-synuclein. FEBS Lett 2001;509:31-35.
    • (2001) FEBS Lett , vol.509 , pp. 31-35
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 15
    • 0032755251 scopus 로고    scopus 로고
    • Manipulating the amyloid-beta aggregation pathway with chemical chaper-ones
    • Yang DS, Yip CM, Huang TH, Chakrabartty A, Fraser PE. Manipulating the amyloid-beta aggregation pathway with chemical chaper-ones. J Biol Chem 1999;274:32970-32974.
    • (1999) J Biol Chem , vol.274 , pp. 32970-32974
    • Yang, D.S.1    Yip, C.M.2    Huang, T.H.3    Chakrabartty, A.4    Fraser, P.E.5
  • 16
    • 33645241089 scopus 로고    scopus 로고
    • TMAO promotes fibrillization and microtubule assembly activity in the C-terminal repeat region of tau
    • Scaramozzino F, Peterson DW, Farmer P, Gerig JT, Graves DJ, Lew J. TMAO promotes fibrillization and microtubule assembly activity in the C-terminal repeat region of tau. Biochemistry 2006;45:3684-3691.
    • (2006) Biochemistry , vol.45 , pp. 3684-3691
    • Scaramozzino, F.1    Peterson, D.W.2    Farmer, P.3    Gerig, J.T.4    Graves, D.J.5    Lew, J.6
  • 17
    • 33646498780 scopus 로고    scopus 로고
    • Organic compatible solutes of halotolerant and halo-philic microorganisms
    • Roberts MF. Organic compatible solutes of halotolerant and halo-philic microorganisms. Saline Systems 2005;1:5.
    • (2005) Saline Systems , vol.1 , pp. 5
    • Roberts, M.F.1
  • 18
    • 29144469368 scopus 로고    scopus 로고
    • Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid-or benzyl alcohol-overexpressed molecular chaperones
    • de Marco A, Vigh L, Diamant S, Goloubinoff P. Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid-or benzyl alcohol-overexpressed molecular chaperones. Cell Stress Chaperones 2005;10:329-339.
    • (2005) Cell Stress Chaperones , vol.10 , pp. 329-339
    • de Marco, A.1    Vigh, L.2    Diamant, S.3    Goloubinoff, P.4
  • 19
    • 34247558033 scopus 로고    scopus 로고
    • Accumulation of proteins bearing atypical isoaspartyl residues in livers of alcohol-fed rats is prevented by betaine administration: Effects on protein-L-isoaspartyl methyltransferase activity
    • Kharbanda KK, Mailliard ME, Baldwin CR, Sorrell MF, Tuma DJ. Accumulation of proteins bearing atypical isoaspartyl residues in livers of alcohol-fed rats is prevented by betaine administration: effects on protein-L-isoaspartyl methyltransferase activity. J Hepatol 2007;46:1119-1125.
    • (2007) J Hepatol , vol.46 , pp. 1119-1125
    • Kharbanda, K.K.1    Mailliard, M.E.2    Baldwin, C.R.3    Sorrell, M.F.4    Tuma, D.J.5
  • 20
    • 0036335009 scopus 로고    scopus 로고
    • Metabolic engineering of osmo-protectant accumulation in plants
    • Rontein D, Basset G, Hanson AD. Metabolic engineering of osmo-protectant accumulation in plants. Metab Eng 2002;4:49-56.
    • (2002) Metab Eng , vol.4 , pp. 49-56
    • Rontein, D.1    Basset, G.2    Hanson, A.D.3
  • 21
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • Goloubinoff P, Mogk A, Ben Zvi AP, Tomoyasu T, Bukau B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc Natl Acad Sci USA 1999;96:13732-13737.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Ben Zvi, A.P.3    Tomoyasu, T.4    Bukau, B.5
  • 22
    • 0142125283 scopus 로고    scopus 로고
    • Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation
    • Mogk A, Deuerling E, Vorderwulbecke S, Vierling E, Bukau B. Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation. Mol Microbiol 2003;50:585-595.
    • (2003) Mol Microbiol , vol.50 , pp. 585-595
    • Mogk, A.1    Deuerling, E.2    Vorderwulbecke, S.3    Vierling, E.4    Bukau, B.5
  • 23
    • 0037468510 scopus 로고    scopus 로고
    • Maltodextrin-bind-ing proteins from diverse bacteria and archaea are potent solubility enhancers
    • Fox JD, Routzahn KM, Bucher MH, Waugh DS. Maltodextrin-bind-ing proteins from diverse bacteria and archaea are potent solubility enhancers. FEBS Lett 2003;537:53-57.
    • (2003) FEBS Lett , vol.537 , pp. 53-57
    • Fox, J.D.1    Routzahn, K.M.2    Bucher, M.H.3    Waugh, D.S.4
  • 24
    • 0034956228 scopus 로고    scopus 로고
    • A strategy for optimizing the monodispersity of fusion proteins: Application to purification of recombinant HPV E6 oncoprotein
    • Nominee Y, Ristriani T, Laurent C, Lefevre J-F, Weiss E, Travee G. A strategy for optimizing the monodispersity of fusion proteins: application to purification of recombinant HPV E6 oncoprotein. Protein Eng 2001;14:297-305.
    • (2001) Protein Eng , vol.14 , pp. 297-305
    • Nominee, Y.1    Ristriani, T.2    Laurent, C.3    Lefevre, J.-F.4    Weiss, E.5    Travee, G.6
  • 25
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of (3-sheet amyloid fibril structures with thioflavin T
    • LeVine H. Quantification of (3-sheet amyloid fibril structures with thioflavin T. Methods Enzymol 1999;309:274-284.
    • (1999) Methods Enzymol , vol.309 , pp. 274-284
    • LeVine, H.1
  • 26
    • 20044395316 scopus 로고    scopus 로고
    • Comparative analysis of protein aggregates by blue native electrophoresis and subsequent SDS-PAGE in a three-dimensional geometry gel
    • Stegemann J, Ventzki R, Schrodel A, de Marco A. Comparative analysis of protein aggregates by blue native electrophoresis and subsequent SDS-PAGE in a three-dimensional geometry gel. Proteo-mics 2005;5:2002-2009.
    • (2005) Proteo-mics , vol.5 , pp. 2002-2009
    • Stegemann, J.1    Ventzki, R.2    Schrodel, A.3    de Marco, A.4
  • 28
    • 0032831759 scopus 로고    scopus 로고
    • Fourier transform infrared spec-troscopy in analysis of protein deposits
    • Seshadri S, Khurana R, Fink AL. Fourier transform infrared spec-troscopy in analysis of protein deposits. Methods Enzymol 1999; 309:559-576.
    • (1999) Methods Enzymol , vol.309 , pp. 559-576
    • Seshadri, S.1    Khurana, R.2    Fink, A.L.3
  • 29
    • 0036880493 scopus 로고    scopus 로고
    • What vibrations tell us about proteins
    • Barth A, Zscherp C. What vibrations tell us about proteins. Q Rev Biophys 2002;35:369-430.
    • (2002) Q Rev Biophys , vol.35 , pp. 369-430
    • Barth, A.1    Zscherp, C.2
  • 32
    • 0022463740 scopus 로고
    • Resolution-enhanced Fourier transform infrared spectroscopy of enzymes
    • Susi H, Byler DM. Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Methods Enzymol 1986;130:291-311.
    • (1986) Methods Enzymol , vol.130 , pp. 291-311
    • Susi, H.1    Byler, D.M.2
  • 33
    • 0344672542 scopus 로고    scopus 로고
    • Structure and dynamics of membrane proteins as studied by infrared spectroscopy
    • Arrondo JLR, Goni FM. Structure and dynamics of membrane proteins as studied by infrared spectroscopy. Prog Biophys Mol Biol 1999;72:367-405.
    • (1999) Prog Biophys Mol Biol , vol.72 , pp. 367-405
    • Arrondo, J.L.R.1    Goni, F.M.2
  • 34
    • 0028593398 scopus 로고
    • Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV
    • Lim K, Ho JX, Keeling K, Gilliland GL, Ji X, Ruker F, Carter DC. Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV. Protein Sci 1994;3:2233-2244.
    • (1994) Protein Sci , vol.3 , pp. 2233-2244
    • Lim, K.1    Ho, J.X.2    Keeling, K.3    Gilliland, G.L.4    Ji, X.5    Ruker, F.6    Carter, D.C.7
  • 36
    • 12844274977 scopus 로고    scopus 로고
    • Secondary structure, conformational stability and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopy
    • Natalello A, Ami D, Brocca S, Lotti M, Doglia SM. Secondary structure, conformational stability and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopy. Biochem J 2005;385:511-517.
    • (2005) Biochem J , vol.385 , pp. 511-517
    • Natalello, A.1    Ami, D.2    Brocca, S.3    Lotti, M.4    Doglia, S.M.5
  • 37
    • 33846243823 scopus 로고    scopus 로고
    • Role of flavin mono-nucleotide in the thermostability and oligomerization of Escherichia coli stress-defense protein WrbA
    • Natalello A, Doglia SM, Carey J, Grandori R. Role of flavin mono-nucleotide in the thermostability and oligomerization of Escherichia coli stress-defense protein WrbA. Biochemistry 2007;46:543-553.
    • (2007) Biochemistry , vol.46 , pp. 543-553
    • Natalello, A.1    Doglia, S.M.2    Carey, J.3    Grandori, R.4
  • 38
    • 0035958656 scopus 로고    scopus 로고
    • The osmophobic effect: Natural selection of a thermodynamic force in protein folding
    • Bolen DW, Baskakov IV. The osmophobic effect: natural selection of a thermodynamic force in protein folding. J Mol Biol 2001;310: 955-963.
    • (2001) J Mol Biol , vol.310 , pp. 955-963
    • Bolen, D.W.1    Baskakov, I.V.2
  • 39
    • 4344614677 scopus 로고    scopus 로고
    • Effects of naturally occurring osmolytes on protein stability and solubility: Issues important in protein crystallization
    • Bolen DW. Effects of naturally occurring osmolytes on protein stability and solubility: issues important in protein crystallization. Methods 2004;34:312-322.
    • (2004) Methods , vol.34 , pp. 312-322
    • Bolen, D.W.1
  • 40
    • 35748959041 scopus 로고    scopus 로고
    • Effects of osmolytes on protein folding and aggregation in cells
    • Ignatova Z, Gierasch LM. Effects of osmolytes on protein folding and aggregation in cells. Methods Enzymol 2007;428:355-372.
    • (2007) Methods Enzymol , vol.428 , pp. 355-372
    • Ignatova, Z.1    Gierasch, L.M.2
  • 41
    • 27244437952 scopus 로고    scopus 로고
    • Predicting the energetics of osmolyte-induced protein folding/unfolding
    • Auton M, Bolen DW. Predicting the energetics of osmolyte-induced protein folding/unfolding. Proc Natl Acad Sci USA 2005;102:15065-15068.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15065-15068
    • Auton, M.1    Bolen, D.W.2
  • 43
    • 34447618598 scopus 로고    scopus 로고
    • DNA induces folding in alpha-synuclein: Understanding the mechanism using chaperone property of osmo-lytes
    • Hegde ML, Rao KS. DNA induces folding in alpha-synuclein: understanding the mechanism using chaperone property of osmo-lytes. Arch Biochem Biophys 2007;464:57-69.
    • (2007) Arch Biochem Biophys , vol.464 , pp. 57-69
    • Hegde, M.L.1    Rao, K.S.2
  • 44
    • 44749084768 scopus 로고    scopus 로고
    • Parvalbumin characterization from the euryhaline stingray Dasyatis sabina
    • Heffron JK, Moerland TS. Parvalbumin characterization from the euryhaline stingray Dasyatis sabina. Comp Biochem Physiol A Mol Integr Physiol 2008;150:339-346.
    • (2008) Comp Biochem Physiol A Mol Integr Physiol , vol.150 , pp. 339-346
    • Heffron, J.K.1    Moerland, T.S.2
  • 45
    • 15744404427 scopus 로고    scopus 로고
    • Counteracting osmolyte trimethyl-amine N-oxide destabilizes proteins at pH below its pKa. Measurements of thermodynamic parameters of proteins in the presence and absence of trimethylamine N-oxide
    • Singh R, Haque I, Ahmad F. Counteracting osmolyte trimethyl-amine N-oxide destabilizes proteins at pH below its pKa. Measurements of thermodynamic parameters of proteins in the presence and absence of trimethylamine N-oxide. J Biol Chem 2005;280: 11035-11042.
    • (2005) J Biol Chem , vol.280 , pp. 11035-11042
    • Singh, R.1    Haque, I.2    Ahmad, F.3
  • 46
    • 33947197428 scopus 로고    scopus 로고
    • Thermal destabilization of stem bromelain by trehalose
    • Habib S, Khan MA, Younus H. Thermal destabilization of stem bromelain by trehalose. Protein J 2007;26:117-124.
    • (2007) Protein J , vol.26 , pp. 117-124
    • Habib, S.1    Khan, M.A.2    Younus, H.3
  • 47
    • 35448999589 scopus 로고    scopus 로고
    • A practical guide on how osmolytes modulate macromolecular properties
    • Harries D, Rosgen J. A practical guide on how osmolytes modulate macromolecular properties. Methods Cell Biol 2008;84:679-735.
    • (2008) Methods Cell Biol , vol.84 , pp. 679-735
    • Harries, D.1    Rosgen, J.2
  • 48
    • 0026559541 scopus 로고
    • Origins of the osmoprotective properties of betaine and proline in Escherichia coli K-12
    • Cayley S, Lewis BA, Record MT, Jr. Origins of the osmoprotective properties of betaine and proline in Escherichia coli K-12. J Bacter-iol 1992;174:1586-1595.
    • (1992) J Bacter-iol , vol.174 , pp. 1586-1595
    • Cayley, S.1    Lewis, B.A.2    Record Jr., M.T.3


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