메뉴 건너뛰기




Volumn 347, Issue 5, 2005, Pages 911-919

An obligatory intermediate controls the folding of the α-subunit of tryptophan synthase, a TIM barrel protein

Author keywords

Hydrogen exchange; Mass spectrometry; Protein folding; TIM barrel; Tryptophan synthase

Indexed keywords

AMIDE; DEUTERIUM; PROTON; TRIOSEPHOSPHATE ISOMERASE; TRYPTOPHAN SYNTHASE; UREA;

EID: 15244354756     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.01.064     Document Type: Article
Times cited : (26)

References (51)
  • 2
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • K.A. Dill, and H.S. Chan From Levinthal to pathways to funnels Nature Struct. Biol. 4 1997 10 19
    • (1997) Nature Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 4
    • 0029249945 scopus 로고
    • The nature of protein folding pathways: The classical versus the new view
    • R.L. Baldwin The nature of protein folding pathways: the classical versus the new view J. Biomol. NMR 5 1995 103 109
    • (1995) J. Biomol. NMR , vol.5 , pp. 103-109
    • Baldwin, R.L.1
  • 5
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • S.E. Jackson How do small single-domain proteins fold? Fold. Des. 3 1998 R81 R91
    • (1998) Fold. Des. , vol.3
    • Jackson, S.E.1
  • 6
    • 0033548553 scopus 로고    scopus 로고
    • Rapid folding with and without populated intermediates in the homologous four helix proteins Im7 and Im9
    • N. Ferguson, A.P. Capaldi, R. James, C. Kleanthous, and S.E. Radford Rapid folding with and without populated intermediates in the homologous four helix proteins Im7 and Im9 J. Mol. Biol. 286 1999 1597 1608
    • (1999) J. Mol. Biol. , vol.286 , pp. 1597-1608
    • Ferguson, N.1    Capaldi, A.P.2    James, R.3    Kleanthous, C.4    Radford, S.E.5
  • 7
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor-2. 1. Evidence for a two-state transition
    • S.E. Jackson, and A.R. Fersht Folding of chymotrypsin inhibitor-2. 1. Evidence for a two-state transition Biochemistry 30 1991 10428 10435
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 9
    • 0034685619 scopus 로고    scopus 로고
    • A breakdown of symmetry in the folding transition state of protein L
    • D.E. Kim, C. Fisher, and D. Baker A breakdown of symmetry in the folding transition state of protein L J. Mol. Biol. 298 2000 971 984
    • (2000) J. Mol. Biol. , vol.298 , pp. 971-984
    • Kim, D.E.1    Fisher, C.2    Baker, D.3
  • 10
    • 0034622508 scopus 로고    scopus 로고
    • Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: Thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles
    • R.M. Ionescu, V.F. Smith, J.C. O'Neill Jr, and C.R. Matthews Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles Biochemistry 39 2000 9540 9550
    • (2000) Biochemistry , vol.39 , pp. 9540-9550
    • Ionescu, R.M.1    Smith, V.F.2    O'Neill Jr., J.C.3    Matthews, C.R.4
  • 11
    • 0029025915 scopus 로고
    • Kinetic traps in lysozyme folding
    • T. Kiefhaber Kinetic traps in lysozyme folding Proc. Natl Acad. Sci. USA 92 1995 9029 9033
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9029-9033
    • Kiefhaber, T.1
  • 12
    • 0030961780 scopus 로고    scopus 로고
    • The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
    • T.M. Raschke, and S. Marqusee The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions Nature Struct. Biol. 4 1997 298 304
    • (1997) Nature Struct. Biol. , vol.4 , pp. 298-304
    • Raschke, T.M.1    Marqusee, S.2
  • 13
    • 0031038918 scopus 로고    scopus 로고
    • Alzheimer's disease: Genotypes, phenotypes, and treatments
    • D.J. Selkoe Alzheimer's disease: genotypes, phenotypes, and treatments Science 275 1997 630 631
    • (1997) Science , vol.275 , pp. 630-631
    • Selkoe, D.J.1
  • 14
    • 34548200331 scopus 로고    scopus 로고
    • Protein folding and misfolding inside and outside the cell
    • C.M. Dobson, and R.J. Ellis Protein folding and misfolding inside and outside the cell EMBO J. 17 1998 5251 5254
    • (1998) EMBO J. , vol.17 , pp. 5251-5254
    • Dobson, C.M.1    Ellis, R.J.2
  • 15
    • 0027770910 scopus 로고
    • Detection of transient protein folding populations by mass spectrometry
    • A. Miranker, C.V. Robinson, S.E. Radford, R.T. Aplin, and C.M. Dobson Detection of transient protein folding populations by mass spectrometry Science 262 1993 896 900
    • (1993) Science , vol.262 , pp. 896-900
    • Miranker, A.1    Robinson, C.V.2    Radford, S.E.3    Aplin, R.T.4    Dobson, C.M.5
  • 16
    • 0242321015 scopus 로고    scopus 로고
    • Role of the B helix in early folding events in apomyoglobin: Evidence from site-directed mutagenesis for native-like long range interactions
    • C. Nishimura, P.E. Wright, and H.J. Dyson Role of the B helix in early folding events in apomyoglobin: evidence from site-directed mutagenesis for native-like long range interactions J. Mol. Biol. 334 2003 293 307
    • (2003) J. Mol. Biol. , vol.334 , pp. 293-307
    • Nishimura, C.1    Wright, P.E.2    Dyson, H.J.3
  • 17
    • 0037614975 scopus 로고    scopus 로고
    • Quaternary structure of aldolase leads to differences in its folding and unfolding intermediates
    • H. Pan, and D.L. Smith Quaternary structure of aldolase leads to differences in its folding and unfolding intermediates Biochemistry 42 2003 5713 5721
    • (2003) Biochemistry , vol.42 , pp. 5713-5721
    • Pan, H.1    Smith, D.L.2
  • 18
    • 0029897362 scopus 로고    scopus 로고
    • Thermal-induced unfolding domains in aldolase identified by amide hydrogen exchange and mass spectrometry
    • Z. Zhang, and D.L. Smith Thermal-induced unfolding domains in aldolase identified by amide hydrogen exchange and mass spectrometry Protein Sci. 5 1996 1282 1289
    • (1996) Protein Sci. , vol.5 , pp. 1282-1289
    • Zhang, Z.1    Smith, D.L.2
  • 19
    • 0033572543 scopus 로고    scopus 로고
    • Rate and equilibrium constants for protein unfolding and refolding determined by hydrogen exchange-mass spectrometry
    • Y. Deng, and D.L. Smith Rate and equilibrium constants for protein unfolding and refolding determined by hydrogen exchange-mass spectrometry Anal. Biochem. 276 1999 150 160
    • (1999) Anal. Biochem. , vol.276 , pp. 150-160
    • Deng, Y.1    Smith, D.L.2
  • 21
    • 0032485916 scopus 로고    scopus 로고
    • Identification of unfolding domains in large proteins by their unfolding rates
    • Y. Deng, and D.L. Smith Identification of unfolding domains in large proteins by their unfolding rates Biochemistry 37 1998 6256 6262
    • (1998) Biochemistry , vol.37 , pp. 6256-6262
    • Deng, Y.1    Smith, D.L.2
  • 22
    • 0033585130 scopus 로고    scopus 로고
    • Hydrogen exchange demonstrates three domains in aldolase unfold sequentially
    • Y. Deng, and D.L. Smith Hydrogen exchange demonstrates three domains in aldolase unfold sequentially J. Mol. Biol. 294 1999 247 258
    • (1999) J. Mol. Biol. , vol.294 , pp. 247-258
    • Deng, Y.1    Smith, D.L.2
  • 23
    • 0033473768 scopus 로고    scopus 로고
    • Comparison of continuous and pulsed labeling amide hydrogen exchange/mass spectrometry for studies of protein dynamics
    • Y. Deng, Z. Zhang, and D.L. Smith Comparison of continuous and pulsed labeling amide hydrogen exchange/mass spectrometry for studies of protein dynamics J. Am. Soc. Mass Spectrom. 10 1999 675 684
    • (1999) J. Am. Soc. Mass Spectrom. , vol.10 , pp. 675-684
    • Deng, Y.1    Zhang, Z.2    Smith, D.L.3
  • 24
    • 0036384350 scopus 로고    scopus 로고
    • One fold with many functions: The evolutionary relationships between TIM barrel families based on their sequences, structures and functions
    • N. Nagano, C.A. Orengo, and J.M. Thornton One fold with many functions: the evolutionary relationships between TIM barrel families based on their sequences, structures and functions J. Mol. Biol. 321 2002 741 765
    • (2002) J. Mol. Biol. , vol.321 , pp. 741-765
    • Nagano, N.1    Orengo, C.A.2    Thornton, J.M.3
  • 25
    • 0026685018 scopus 로고
    • Stable substructures of eightfold β/α-barrel proteins: Fragment complementation of phosphoribosylanthranilate isomerase
    • J. Eder, and K. Kirschner Stable substructures of eightfold β/α-barrel proteins: fragment complementation of phosphoribosylanthranilate isomerase Biochemistry 31 1992 3617 3625
    • (1992) Biochemistry , vol.31 , pp. 3617-3625
    • Eder, J.1    Kirschner, K.2
  • 26
    • 0028287276 scopus 로고
    • Detection of an intermediate in the folding of the (βα)8- barrel N-(5′-phosphoribosyl) anthranilate isomerase from E. coli
    • A. Jasanoff, B. Davis, and A.R. Fersht Detection of an intermediate in the folding of the (βα)8-barrel N-(5′-phosphoribosyl) anthranilate isomerase from E. coli Biochemistry 33 1994 6350 6355
    • (1994) Biochemistry , vol.33 , pp. 6350-6355
    • Jasanoff, A.1    Davis, B.2    Fersht, A.R.3
  • 27
    • 0037540410 scopus 로고    scopus 로고
    • Nonsequential unfolding of the alpha/beta barrel protein indole-3-glycerol-phosphate synthase
    • M.M. Sanchez del Pino, and A.R. Fersht Nonsequential unfolding of the alpha/beta barrel protein indole-3-glycerol-phosphate synthase Biochemistry 36 1997 5560 5565
    • (1997) Biochemistry , vol.36 , pp. 5560-5565
    • Sanchez Del Pino, M.M.1    Fersht, A.R.2
  • 28
    • 0030906459 scopus 로고    scopus 로고
    • Stability of a thermophilic TIM barrel enzyme: Indole-3-glycerol phosphate synthase from the thermophilic archaeon Sulfolobus solfataricus
    • G. Andreotti, M.V. Cubellis, M.D. Palo, D. Fessas, G. Sannia, and G. Marino Stability of a thermophilic TIM barrel enzyme: indole-3-glycerol phosphate synthase from the thermophilic archaeon Sulfolobus solfataricus Biochem. J. 323 1997 259 264
    • (1997) Biochem. J. , vol.323 , pp. 259-264
    • Andreotti, G.1    Cubellis, M.V.2    Palo, M.D.3    Fessas, D.4    Sannia, G.5    Marino, G.6
  • 29
    • 0032813944 scopus 로고    scopus 로고
    • The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli
    • P.J. Gualfetti, O. Bilsel, and C.R. Matthews The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli Protein Sci. 8 1999 1623 1635
    • (1999) Protein Sci. , vol.8 , pp. 1623-1635
    • Gualfetti, P.J.1    Bilsel, O.2    Matthews, C.R.3
  • 31
    • 0036071577 scopus 로고    scopus 로고
    • Folding mechanism of indole-3-glycerol phosphate synthase from Sulfolobus solfataricus: A test of the conservation of folding mechanisms hypothesis in (beta(alpha))(8) barrels
    • W.R. Forsyth, and C.R. Matthews Folding mechanism of indole-3-glycerol phosphate synthase from Sulfolobus solfataricus: a test of the conservation of folding mechanisms hypothesis in (beta(alpha))(8) barrels J. Mol. Biol. 320 2002 1119 1133
    • (2002) J. Mol. Biol. , vol.320 , pp. 1119-1133
    • Forsyth, W.R.1    Matthews, C.R.2
  • 33
    • 0033579862 scopus 로고    scopus 로고
    • Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: Global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels
    • O. Bilsel, J.A. Zitzewitz, K.E. Bowers, and C.R. Matthews Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels Biochemistry 38 1999 1018 1029
    • (1999) Biochemistry , vol.38 , pp. 1018-1029
    • Bilsel, O.1    Zitzewitz, J.A.2    Bowers, K.E.3    Matthews, C.R.4
  • 34
    • 0033520098 scopus 로고    scopus 로고
    • Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: An amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein
    • J.A. Zitzewitz, and C.R. Matthews Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein Biochemistry 38 1999 10205 10214
    • (1999) Biochemistry , vol.38 , pp. 10205-10214
    • Zitzewitz, J.A.1    Matthews, C.R.2
  • 35
    • 0019883139 scopus 로고
    • Urea-induced unfolding of the alpha subunit of tryptophan synthase: Evidence for a multistate process
    • C.R. Matthews, and M.M. Crisanti Urea-induced unfolding of the alpha subunit of tryptophan synthase: evidence for a multistate process Biochemistry 20 1981 784 792
    • (1981) Biochemistry , vol.20 , pp. 784-792
    • Matthews, C.R.1    Crisanti, M.M.2
  • 36
    • 0033060003 scopus 로고    scopus 로고
    • Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein
    • J.A. Zitzewitz, P.J. Gualfetti, I.A. Perkons, S.A. Wasta, and C.R. Matthews Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein Protein Sci. 8 1999 1200 1209
    • (1999) Protein Sci. , vol.8 , pp. 1200-1209
    • Zitzewitz, J.A.1    Gualfetti, P.J.2    Perkons, I.A.3    Wasta, S.A.4    Matthews, C.R.5
  • 37
    • 0036965922 scopus 로고    scopus 로고
    • A cis-prolyl peptide bond isomerization dominates the folding of the alpha subunit of Trp synthase, a TIM barrel protein
    • Y. Wu, and C.R. Matthews A cis-prolyl peptide bond isomerization dominates the folding of the alpha subunit of Trp synthase, a TIM barrel protein J. Mol. Biol. 322 2002 7 13
    • (2002) J. Mol. Biol. , vol.322 , pp. 7-13
    • Wu, Y.1    Matthews, C.R.2
  • 38
    • 0036404928 scopus 로고    scopus 로고
    • Parallel channels and rate-limiting steps in complex protein folding reactions: Prolyl isomerization and the alpha subunit of trp synthase, a TIM barrel protein
    • Y. Wu, and C.R. Matthews Parallel channels and rate-limiting steps in complex protein folding reactions: prolyl isomerization and the alpha subunit of trp synthase, a TIM barrel protein J. Mol. Biol. 323 2002 309 325
    • (2002) J. Mol. Biol. , vol.323 , pp. 309-325
    • Wu, Y.1    Matthews, C.R.2
  • 39
    • 0038690118 scopus 로고    scopus 로고
    • Proline replacements and the simplification of the complex, parallel channel folding mechanism for the alpha subunit of Trp synthase, a TIM barrel protein
    • Y. Wu, and C.R. Matthews Proline replacements and the simplification of the complex, parallel channel folding mechanism for the alpha subunit of Trp synthase, a TIM barrel protein J. Mol. Biol. 330 2003 1131 1144
    • (2003) J. Mol. Biol. , vol.330 , pp. 1131-1144
    • Wu, Y.1    Matthews, C.R.2
  • 40
    • 4143057003 scopus 로고    scopus 로고
    • Multi-state unfolding of the alpha subunit of tryptophan synthase, a TIM barrel protein: Insights into the secondary structure of the stable equilibrium intermediates by hydrogen exchange mass spectrometry
    • T. Rojsajjakul, P. Wintrode, R. Vadrevu, C.R. Matthews, and D.L. Smith Multi-state unfolding of the alpha subunit of tryptophan synthase, a TIM barrel protein: insights into the secondary structure of the stable equilibrium intermediates by hydrogen exchange mass spectrometry J. Mol. Biol. 341 2004 241 253
    • (2004) J. Mol. Biol. , vol.341 , pp. 241-253
    • Rojsajjakul, T.1    Wintrode, P.2    Vadrevu, R.3    Matthews, C.R.4    Smith, D.L.5
  • 42
    • 0019883139 scopus 로고
    • Urea-induced unfolding of α-subunit of tryptophan synthase: Evidence for a multistate process
    • C.R. Matthews, and M.M. Crisanti Urea-induced unfolding of α-subunit of tryptophan synthase: evidence for a multistate process Biochemistry 20 1981 784 792
    • (1981) Biochemistry , vol.20 , pp. 784-792
    • Matthews, C.R.1    Crisanti, M.M.2
  • 43
    • 15244351786 scopus 로고    scopus 로고
    • Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time
    • O. Bilsel, L. Yang, J.A. Zitzewitz, J.M. Beechem, and C.R. Matthews Time-resolved fluorescence anisotropy study of the refolding reaction of the alpha-subunit of tryptophan synthase reveals nonmonotonic behavior of the rotational correlation time Biochemistry 384 1999 177 187
    • (1999) Biochemistry , vol.384 , pp. 177-187
    • Bilsel, O.1    Yang, L.2    Zitzewitz, J.A.3    Beechem, J.M.4    Matthews, C.R.5
  • 44
    • 0028873081 scopus 로고
    • Elucidating the folding problem of α-helical peptides using empirical parameters, II. Helix macrodipole effects and rational modification of the helical content of natural peptides
    • V. Muñoz, and L. Serrano Elucidating the folding problem of α-helical peptides using empirical parameters, II. Helix macrodipole effects and rational modification of the helical content of natural peptides J. Mol. Biol. 245 1994 275 296
    • (1994) J. Mol. Biol. , vol.245 , pp. 275-296
    • Muñoz, V.1    Serrano, L.2
  • 45
    • 0028834210 scopus 로고
    • Elucidating the folding problem of α-helical peptides using empirical parameters III: Temperature and pH dependence
    • V. Muñoz, and L. Serrano Elucidating the folding problem of α-helical peptides using empirical parameters III: temperature and pH dependence J. Mol. Biol. 245 1994 297 308
    • (1994) J. Mol. Biol. , vol.245 , pp. 297-308
    • Muñoz, V.1    Serrano, L.2
  • 46
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation within the agadir model of α-helix formation. Comparison with Zimm-Bragg and Lifson-Roig formalisms
    • V. Muñoz, and L. Serrano Development of the multiple sequence approximation within the agadir model of α-helix formation. Comparison with Zimm-Bragg and Lifson-Roig formalisms Biopolymers 41 1997 495 509
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Muñoz, V.1    Serrano, L.2
  • 47
    • 0032553332 scopus 로고    scopus 로고
    • Elucidating the folding problem of α-helices: Local motifs, long-range electrostatics, ionic strength dependence and prediction of NMR parameters
    • E. Lacroix, A.R. Viguera, and L. Serrano Elucidating the folding problem of α-helices: local motifs, long-range electrostatics, ionic strength dependence and prediction of NMR parameters J. Mol. Biol. 284 1998 173 191
    • (1998) J. Mol. Biol. , vol.284 , pp. 173-191
    • Lacroix, E.1    Viguera, A.R.2    Serrano, L.3
  • 48
    • 0034705115 scopus 로고    scopus 로고
    • How native-state topology affects the folding of dihydrofolate reductase and interleukin-1beta
    • C. Clementi, P.A. Jennings, and J.N. Onuchic How native-state topology affects the folding of dihydrofolate reductase and interleukin-1beta Proc. Natl Acad. Sci. USA 97 2000 5871 5876
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5871-5876
    • Clementi, C.1    Jennings, P.A.2    Onuchic, J.N.3
  • 49
    • 0036394906 scopus 로고    scopus 로고
    • Native-like mean structure in the unfolded ensemble of small proteins
    • B. Zagrovic, C.D. Snow, S. Khaliq, M.R. Shirts, and V.S. Pande Native-like mean structure in the unfolded ensemble of small proteins J. Mol. Biol. 323 2002 153 164
    • (2002) J. Mol. Biol. , vol.323 , pp. 153-164
    • Zagrovic, B.1    Snow, C.D.2    Khaliq, S.3    Shirts, M.R.4    Pande, V.S.5
  • 50
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures J. Appl. Crystallog. 24 1991 946 950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 51
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsch, and C. Sander Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22 1983 2577 2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.