메뉴 건너뛰기




Volumn 369, Issue 4, 2007, Pages 1113-1125

Hydrogen/Deuterium Exchange Mass Spectrometric Analysis of Conformational Changes Accompanying the Assembly of the Yeast Prion Ure2p into Protein Fibrils

Author keywords

conformational changes; hydrogen deuterium exchange; mass spectrometry; prions; Ure2p fibrils

Indexed keywords

DEUTERIUM; HYDROGEN; PROTEIN DERIVATIVE; UNCLASSIFIED DRUG; URE2 PROTEIN;

EID: 34248586540     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.04.018     Document Type: Article
Times cited : (19)

References (44)
  • 1
    • 0028308104 scopus 로고
    • [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae
    • Wickner R.B. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264 (1994) 566-569
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 2
    • 0029584303 scopus 로고
    • [PSI] and [URE3] as yeast prions
    • Wickner R.B., Masison D.C., and Edskes H.K. [PSI] and [URE3] as yeast prions. Yeast 11 (1995) 1671-1685
    • (1995) Yeast , vol.11 , pp. 1671-1685
    • Wickner, R.B.1    Masison, D.C.2    Edskes, H.K.3
  • 3
    • 0033969457 scopus 로고    scopus 로고
    • Rnq1: an epigenetic modifier of protein function in yeast
    • Sondheimer N., and Lindquist S. Rnq1: an epigenetic modifier of protein function in yeast. Mol. Cell. 5 (2000) 163-172
    • (2000) Mol. Cell. , vol.5 , pp. 163-172
    • Sondheimer, N.1    Lindquist, S.2
  • 4
    • 0015056102 scopus 로고
    • Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast
    • Lacroute F. Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast. J. Bacteriol. 106 (1971) 519-522
    • (1971) J. Bacteriol. , vol.106 , pp. 519-522
    • Lacroute, F.1
  • 6
    • 0028859540 scopus 로고
    • Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells
    • Masison D.C., and Wickner R.B. Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells. Science 270 (1995) 93-95
    • (1995) Science , vol.270 , pp. 93-95
    • Masison, D.C.1    Wickner, R.B.2
  • 7
    • 0030780097 scopus 로고    scopus 로고
    • The prion model for [URE3] of yeast: spontaneous generation and requirements for propagation
    • Masison D.C., Maddelein M.L., and Wickner R.B. The prion model for [URE3] of yeast: spontaneous generation and requirements for propagation. Proc. Natl Acad. Sci. USA 94 (1997) 12503-12508
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 12503-12508
    • Masison, D.C.1    Maddelein, M.L.2    Wickner, R.B.3
  • 8
    • 2142762962 scopus 로고    scopus 로고
    • Structural characterization of the fibrillar form of the yeast Saccharomyces cerevisiae prion Ure2p
    • Bousset L., Redeker V., Decottignies P., Dubois S., Le Maréchal P., and Melki R. Structural characterization of the fibrillar form of the yeast Saccharomyces cerevisiae prion Ure2p. Biochemistry 43 (2004) 5022-5032
    • (2004) Biochemistry , vol.43 , pp. 5022-5032
    • Bousset, L.1    Redeker, V.2    Decottignies, P.3    Dubois, S.4    Le Maréchal, P.5    Melki, R.6
  • 9
    • 0035156642 scopus 로고    scopus 로고
    • Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae
    • Bousset L., Belrhali H., Janin J., Melki R., and Morera S. Structure of the globular region of the prion protein Ure2 from the yeast Saccharomyces cerevisiae. Structure 9 (2001) 39-46
    • (2001) Structure , vol.9 , pp. 39-46
    • Bousset, L.1    Belrhali, H.2    Janin, J.3    Melki, R.4    Morera, S.5
  • 10
    • 0035852745 scopus 로고    scopus 로고
    • The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p
    • Umland T.C., Taylor K.L., Rhee S., Wickner R.B., and Davies D.R. The crystal structure of the nitrogen regulation fragment of the yeast prion protein Ure2p. Proc. Natl Acad. Sci. USA 98 (2001) 1459-1464
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 1459-1464
    • Umland, T.C.1    Taylor, K.L.2    Rhee, S.3    Wickner, R.B.4    Davies, D.R.5
  • 11
    • 0035856522 scopus 로고    scopus 로고
    • Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds
    • Bousset L., Belrhali H., Melki R., and Morera S. Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds. Biochemistry 40 (2001) 13564-13573
    • (2001) Biochemistry , vol.40 , pp. 13564-13573
    • Bousset, L.1    Belrhali, H.2    Melki, R.3    Morera, S.4
  • 12
    • 9644287905 scopus 로고    scopus 로고
    • The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms
    • Bai M., Zhou J.M., and Perrett S. The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms. J. Biol. Chem. 279 (2004) 50025-50030
    • (2004) J. Biol. Chem. , vol.279 , pp. 50025-50030
    • Bai, M.1    Zhou, J.M.2    Perrett, S.3
  • 13
    • 0037124337 scopus 로고    scopus 로고
    • The yeast prion Ure2p retains its native alphahelical conformation upon assembly into protein fibrils in vitro
    • Bousset L., Thomson N.H., Radford S.E., and Melki R. The yeast prion Ure2p retains its native alphahelical conformation upon assembly into protein fibrils in vitro. EMBO J. 21 (2002) 2903-2911
    • (2002) EMBO J. , vol.21 , pp. 2903-2911
    • Bousset, L.1    Thomson, N.H.2    Radford, S.E.3    Melki, R.4
  • 14
    • 0042530513 scopus 로고    scopus 로고
    • Assembly ofthe yeast prion Ure2p into protein fibrils, thermodynamic and kinetic characterization
    • Fay N., Inoue Y., Bousset L., Taguchi H., and Melki R. Assembly ofthe yeast prion Ure2p into protein fibrils, thermodynamic and kinetic characterization. J. Biol. Chem. 278 (2003) 30199-30205
    • (2003) J. Biol. Chem. , vol.278 , pp. 30199-30205
    • Fay, N.1    Inoue, Y.2    Bousset, L.3    Taguchi, H.4    Melki, R.5
  • 15
    • 0033605278 scopus 로고    scopus 로고
    • Prion domain initiation of amyloid formation in vitro from native Ure2p
    • Taylor K.L., Cheng N., Williams R.W., Steven A.C., and Wickner R.B. Prion domain initiation of amyloid formation in vitro from native Ure2p. Science 283 (1999) 1339-1343
    • (1999) Science , vol.283 , pp. 1339-1343
    • Taylor, K.L.1    Cheng, N.2    Williams, R.W.3    Steven, A.C.4    Wickner, R.B.5
  • 16
    • 2542542833 scopus 로고    scopus 로고
    • A model for Ure2p prion filaments and other amyloids: the parallel superpleated beta-structure
    • Kajava A.V., Baxa U., Wickner R.B., and Steven A.C. A model for Ure2p prion filaments and other amyloids: the parallel superpleated beta-structure. Proc. Natl Acad. Sci. USA 101 (2004) 7885-7890
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 7885-7890
    • Kajava, A.V.1    Baxa, U.2    Wickner, R.B.3    Steven, A.C.4
  • 17
  • 19
    • 0037291995 scopus 로고    scopus 로고
    • The native-like conformation of Ure2p in fibrils assembled under physiologically relevant conditions switches to an amyloid-like conformation upon heat-treatment of the fibrils
    • Bousset L., Briki F., Doucet J., and Melki R. The native-like conformation of Ure2p in fibrils assembled under physiologically relevant conditions switches to an amyloid-like conformation upon heat-treatment of the fibrils. J. Struct. Biol. 141 (2003) 132-142
    • (2003) J. Struct. Biol. , vol.141 , pp. 132-142
    • Bousset, L.1    Briki, F.2    Doucet, J.3    Melki, R.4
  • 23
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation
    • Zhang Z., and Smith D.L. Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation. Protein Sci. 2 (1993) 522-531
    • (1993) Protein Sci. , vol.2 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 24
    • 0031018084 scopus 로고    scopus 로고
    • Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry
    • Smith D.L., Deng Y., and Zhang Z. Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry. J. Mass. Spectrom. 32 (1997) 135-146
    • (1997) J. Mass. Spectrom. , vol.32 , pp. 135-146
    • Smith, D.L.1    Deng, Y.2    Zhang, Z.3
  • 25
    • 0032428378 scopus 로고    scopus 로고
    • Identification of protein-protein interfaces by decreased amide proton solvent accessibility
    • Mandell J.G., Falick A.M., and Komives E.A. Identification of protein-protein interfaces by decreased amide proton solvent accessibility. Proc. Natl Acad. Sci. USA 95 (1998) 14705-14710
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 14705-14710
    • Mandell, J.G.1    Falick, A.M.2    Komives, E.A.3
  • 26
    • 0032555738 scopus 로고    scopus 로고
    • Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry
    • Nettleton E.J., Sunde M., Lai Z., Kelly J.W., Dobson C.M., and Robinson C.V. Protein subunit interactions and structural integrity of amyloidogenic transthyretins: evidence from electrospray mass spectrometry. J. Mol. Biol. 281 (1998) 553-564
    • (1998) J. Mol. Biol. , vol.281 , pp. 553-564
    • Nettleton, E.J.1    Sunde, M.2    Lai, Z.3    Kelly, J.W.4    Dobson, C.M.5    Robinson, C.V.6
  • 27
    • 0030451744 scopus 로고    scopus 로고
    • Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling
    • Gross M., Robinson C.V., Mayhew M., Hartl F.U., and Radford S.E. Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling. Protein Sci. 5 (1996) 2506-2513
    • (1996) Protein Sci. , vol.5 , pp. 2506-2513
    • Gross, M.1    Robinson, C.V.2    Mayhew, M.3    Hartl, F.U.4    Radford, S.E.5
  • 28
    • 0033545907 scopus 로고    scopus 로고
    • Characterization of the conformational changes of acetohydroxy acid isomeroreductase induced by the binding of Mg2+ ions, NADPH, and a competitive inhibitor
    • Halgand F., Dumas R., Biou V., Andrieu J.P., Thomazeau K., Gagnon J., et al. Characterization of the conformational changes of acetohydroxy acid isomeroreductase induced by the binding of Mg2+ ions, NADPH, and a competitive inhibitor. Biochemistry 38 (1999) 6025-6034
    • (1999) Biochemistry , vol.38 , pp. 6025-6034
    • Halgand, F.1    Dumas, R.2    Biou, V.3    Andrieu, J.P.4    Thomazeau, K.5    Gagnon, J.6
  • 29
    • 24344480244 scopus 로고    scopus 로고
    • Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme
    • Johnson R.J., Christodoulou J., Dumoulin M., Caddy G.L., Alcocer M.J., Murtagh G.J., et al. Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme. J. Mol. Biol. 352 (2005) 823-836
    • (2005) J. Mol. Biol. , vol.352 , pp. 823-836
    • Johnson, R.J.1    Christodoulou, J.2    Dumoulin, M.3    Caddy, G.L.4    Alcocer, M.J.5    Murtagh, G.J.6
  • 30
    • 33746781304 scopus 로고    scopus 로고
    • Structural differences in Abeta amyloid protofibrils and fibrils mapped by hydrogen exchange-mass spectrometry with on-line proteolytic fragmentation
    • Kheterpal I., Chen M., Cook K.D., and Wetzel R. Structural differences in Abeta amyloid protofibrils and fibrils mapped by hydrogen exchange-mass spectrometry with on-line proteolytic fragmentation. J. Mol. Biol. 361 (2006) 785-795
    • (2006) J. Mol. Biol. , vol.361 , pp. 785-795
    • Kheterpal, I.1    Chen, M.2    Cook, K.D.3    Wetzel, R.4
  • 32
    • 0042572518 scopus 로고    scopus 로고
    • Hydrogen exchange-mass spectrometry analysis of beta-amyloid peptide structure
    • Wang S.S., Tobler S.A., Good T.A., and Fernandez E.J. Hydrogen exchange-mass spectrometry analysis of beta-amyloid peptide structure. Biochemistry 42 (2003) 9507-9514
    • (2003) Biochemistry , vol.42 , pp. 9507-9514
    • Wang, S.S.1    Tobler, S.A.2    Good, T.A.3    Fernandez, E.J.4
  • 33
    • 27344436619 scopus 로고    scopus 로고
    • Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level
    • Del Mar C., Greenbaum E.A., Mayne L., Englander S.W., and Woods Jr. V.L. Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level. Proc. Natl Acad. Sci. USA 102 (2005) 15477-15482
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 15477-15482
    • Del Mar, C.1    Greenbaum, E.A.2    Mayne, L.3    Englander, S.W.4    Woods Jr., V.L.5
  • 34
    • 0041345995 scopus 로고    scopus 로고
    • Conformational transition occurring upon amyloid aggregation of the HET-s prion protein of Podospora anserina analyzed by hydrogen/deuterium exchange and mass spectrometry
    • Nazabal A., Dos Reis S., Bonneu M., Saupe S.J., and Schmitter J.M. Conformational transition occurring upon amyloid aggregation of the HET-s prion protein of Podospora anserina analyzed by hydrogen/deuterium exchange and mass spectrometry. Biochemistry 42 (2003) 8852-8861
    • (2003) Biochemistry , vol.42 , pp. 8852-8861
    • Nazabal, A.1    Dos Reis, S.2    Bonneu, M.3    Saupe, S.J.4    Schmitter, J.M.5
  • 35
    • 33846811599 scopus 로고    scopus 로고
    • β-1Sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange
    • Lu X., Wintrode P.L., and Surewicz W.K. β-1Sheet core of human prion protein amyloid fibrils as determined by hydrogen/deuterium exchange. Proc. Natl Acad. Sci. USA 104 (2007) 1510-1515
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 1510-1515
    • Lu, X.1    Wintrode, P.L.2    Surewicz, W.K.3
  • 36
    • 0242579199 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange mass spectrometry of actin in various biochemical contexts
    • Chik J.K., and Schriemer D.C. Hydrogen/deuterium exchange mass spectrometry of actin in various biochemical contexts. J. Mol. Biol. 334 (2003) 373-385
    • (2003) J. Mol. Biol. , vol.334 , pp. 373-385
    • Chik, J.K.1    Schriemer, D.C.2
  • 37
    • 33646911952 scopus 로고    scopus 로고
    • Investigating the structural properties of amyloid-like fibrils formed in vitro from beta2-microglobulin using limited proteolysis and electrospray ionisation mass spectrometry
    • Myers S.L., Thomson N.H., Radford S.E., and Ashcroft A.E. Investigating the structural properties of amyloid-like fibrils formed in vitro from beta2-microglobulin using limited proteolysis and electrospray ionisation mass spectrometry. Rapid Commun. Mass. Spectrom. 20 (2006) 1628-1636
    • (2006) Rapid Commun. Mass. Spectrom. , vol.20 , pp. 1628-1636
    • Myers, S.L.1    Thomson, N.H.2    Radford, S.E.3    Ashcroft, A.E.4
  • 38
    • 0942298128 scopus 로고    scopus 로고
    • Amyloid nucleation and hierarchical assembly of Ure2p fibrils: role of asparagine/glutamine repeat and nonrepeat regions of the prion domain
    • Jiang Y., Li H., Zhu L., Zhou J.M., and Perrett S. Amyloid nucleation and hierarchical assembly of Ure2p fibrils: role of asparagine/glutamine repeat and nonrepeat regions of the prion domain. J. Biol. Chem. 279 (2004) 3361-3369
    • (2004) J. Biol. Chem. , vol.279 , pp. 3361-3369
    • Jiang, Y.1    Li, H.2    Zhu, L.3    Zhou, J.M.4    Perrett, S.5
  • 39
  • 42
    • 0032186122 scopus 로고    scopus 로고
    • Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry
    • Mandell J.G., Falick A.M., and Komives E.A. Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry. Anal. Chem. 70 (1998) 3987-3995
    • (1998) Anal. Chem. , vol.70 , pp. 3987-3995
    • Mandell, J.G.1    Falick, A.M.2    Komives, E.A.3
  • 43
    • 0033473760 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption ionization hydrogen/deuterium exchange studies to probe peptide conformational changes
    • Figueroa I.D., and Russell D.H. Matrix-assisted laser desorption ionization hydrogen/deuterium exchange studies to probe peptide conformational changes. J. Am. Soc. Mass. Spectrom. 10 (1999) 719-731
    • (1999) J. Am. Soc. Mass. Spectrom. , vol.10 , pp. 719-731
    • Figueroa, I.D.1    Russell, D.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.