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Volumn 300, Issue 1, 2003, Pages 29-35

Fluorescence and folding properties of Tyr mutant tryptophan synthase α-subunits from Escherichia coli

Author keywords

Folding intermediate; Protein folding; Tryptophan synthase subunit; Tyrosine fluorescence; Tyrosine mutant

Indexed keywords

PHENYLALANINE; PROTEIN SUBUNIT; TRYPTOPHAN SYNTHASE; TYROSINE; UREA;

EID: 0037224037     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)02769-9     Document Type: Article
Times cited : (6)

References (31)
  • 1
    • 0033616632 scopus 로고    scopus 로고
    • Time-resolved fluorescence anisotropy study of the refolding reaction of the α-subunit of tryptophan synthase reveals non-monotonic behavior of the rotational correlation time
    • O. Bilsel, L. Yang, J.A. Zitzewitz, J.M. Beechem, C.R. Matthews, Time-resolved fluorescence anisotropy study of the refolding reaction of the α-subunit of tryptophan synthase reveals non-monotonic behavior of the rotational correlation time, Biochemistry 38 (1999) 4177-4187.
    • (1999) Biochemistry , vol.38 , pp. 4177-4187
    • Bilsel, O.1    Yang, L.2    Zitzewitz, J.A.3    Beechem, J.M.4    Matthews, C.R.5
  • 2
    • 0033579862 scopus 로고    scopus 로고
    • Folding mechanism of the α-subunit of tryptophan synthase, an α/β 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, C.R. Matthews, Folding mechanism of the α-subunit of tryptophan synthase, an α/β 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
  • 3
    • 0026035205 scopus 로고
    • Relative activities and stabilities of mutant Escherichia coli tryptophan synthase α subunits
    • W.K. Lim, H.J. Shin, D.L. Milton, J.K. Hardman, Relative activities and stabilities of mutant Escherichia coli tryptophan synthase α subunits, J. Bacteriol. 173 (1991) 1886-1893.
    • (1991) J. Bacteriol. , vol.173 , pp. 1886-1893
    • Lim, W.K.1    Shin, H.J.2    Milton, D.L.3    Hardman, J.K.4
  • 4
    • 0023053396 scopus 로고
    • Effects of the phenylalanine-22→leucine, glutamic acid-49→methionine, glycine-234→aspartic acid, and glycine-234→lysine mutations on the folding and stability of the α subunit of tryptophan synthase from Escherichia coli
    • A.M. Beasty, M.R. Hurle, J.T. Manz, T. Stackhouse, J.J. Onuffer, C.R. Matthews, Effects of the phenylalanine-22→leucine, glutamic acid-49→methionine, glycine-234→aspartic acid, and glycine-234→lysine mutations on the folding and stability of the α subunit of tryptophan synthase from Escherichia coli, Biochemistry 25 (1986) 2965-2974.
    • (1986) Biochemistry , vol.25 , pp. 2965-2974
    • Beasty, A.M.1    Hurle, M.R.2    Manz, J.T.3    Stackhouse, T.4    Onuffer, J.J.5    Matthews, C.R.6
  • 5
    • 0031039381 scopus 로고    scopus 로고
    • Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase subunit
    • K. Ogasahara, K. Yutani, Equilibrium and kinetic analyses of unfolding and refolding for the conserved proline mutants of tryptophan synthase subunit, Biochemistry 36 (1997) 932-940.
    • (1997) Biochemistry , vol.36 , pp. 932-940
    • Ogasahara, K.1    Yutani, K.2
  • 6
    • 0032813944 scopus 로고    scopus 로고
    • The progressive development of structure and stability during the equilibrium folding of the α subunit of tryptophan synthase from Escherichia coli
    • P.J. Gualfetti, O. Bilsel, C.R. Matthews, The progressive development of structure and stability during the equilibrium folding of the α 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
  • 7
    • 0022884556 scopus 로고
    • In vitro mutagenesis and overexpression of the Escherichia coli trpA gene and the partial characterization of the resultant tryptophan synthase mutant α-subunits
    • D.L. Milton, M.L. Napier, R.M. Myers, J.K. Hardman, In vitro mutagenesis and overexpression of the Escherichia coli trpA gene and the partial characterization of the resultant tryptophan synthase mutant α-subunits, J. Biol. Chem. 261 (1986) 16604-16615.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16604-16615
    • Milton, D.L.1    Napier, M.L.2    Myers, R.M.3    Hardman, J.K.4
  • 9
    • 70449159833 scopus 로고
    • Ultraviolet fluorescence of the aromatic amino acids
    • F.J.W. Teale, G. Weber, Ultraviolet fluorescence of the aromatic amino acids, Biochem. J. 65 (1957) 476-482.
    • (1957) Biochem. J. , vol.65 , pp. 476-482
    • Teale, F.J.W.1    Weber, G.2
  • 10
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • T.A. Kunkel, J.D. Roberts, R.A. Zakour, Rapid and efficient site-specific mutagenesis without phenotypic selection, Methods Enzymol. 154 (1987) 367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 11
    • 0028883248 scopus 로고
    • Affinities of phosphorylated substrates for the E. coli tryptophan synthase α-subunit: Roles of Ser-235 and helix-8′ dipole
    • K.D. Sarker, J.K. Hardman, Affinities of phosphorylated substrates for the E. coli tryptophan synthase α-subunit: Roles of Ser-235 and helix-8′ dipole, Proteins 21 (1995) 130-139.
    • (1995) Proteins , vol.21 , pp. 130-139
    • Sarker, K.D.1    Hardman, J.K.2
  • 13
    • 0016163586 scopus 로고
    • 2 complexes of tryptophan synthetase of Escherichia coli. A comparison between the native complex and the reconstituted complex
    • 2 complexes of tryptophan synthetase of Escherichia coli. A comparison between the native complex and the reconstituted complex, J. Biol. Chem. 249 (1974) 7756-7763.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7756-7763
    • Adachi, O.1    Kohn, L.D.2    Miles, E.W.3
  • 14
    • 0028978238 scopus 로고
    • Tryptophan-containing α-subunits of the Escherichia coli tryptophan synthase. Enzymatic and urea stability properties
    • S.G. Choi, S.E. O'Donnell, K.D. Sarken, J.K. Hardman, Tryptophan-containing α-subunits of the Escherichia coli tryptophan synthase. Enzymatic and urea stability properties, J. Biol. Chem. 270 (1995) 17712-17715.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17712-17715
    • Choi, S.G.1    O'Donnell, S.E.2    Sarken, K.D.3    Hardman, J.K.4
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0016768876 scopus 로고
    • The tryptophan synthase from Escherichia coli. An improved purification procedure for the α-subunit and binding studies with substrate analogues
    • K. Kirschner, R.L. Wiskocil, M. Foehn, L. Rezeau, The tryptophan synthase from Escherichia coli. An improved purification procedure for the α-subunit and binding studies with substrate analogues, Eur. J. Biochem. 60 (1975) 513-523.
    • (1975) Eur. J. Biochem. , vol.60 , pp. 513-523
    • Kirschner, K.1    Wiskocil, R.L.2    Foehn, M.3    Rezeau, L.4
  • 17
    • 0002343673 scopus 로고
    • Measuring the conformational stability of a protein
    • T.E. Creighton (Ed.), IRL Press, Oxford
    • C.N. Pace, B.A. Shirley, J.A. Thomson, Measuring the conformational stability of a protein, in: T.E. Creighton (Ed.), Protein Structure: A Practical Approach, IRL Press, Oxford, 1989, pp. 311-330.
    • (1989) Protein Structure: A Practical Approach , pp. 311-330
    • Pace, C.N.1    Shirley, B.A.2    Thomson, J.A.3
  • 19
    • 0000722070 scopus 로고
    • Spectral methods of characterizing protein conformation and conformational changes
    • T.E. Creighton (Ed.), IRL Press, Oxford
    • F.X. Schmid, Spectral methods of characterizing protein conformation and conformational changes, in: T.E. Creighton (Ed.), Protein Structure: A Practical Approach, IRL Press, Oxford, 1989, pp. 251-285.
    • (1989) Protein Structure: A Practical Approach , pp. 251-285
    • Schmid, F.X.1
  • 20
    • 0028784310 scopus 로고
    • Unfolding properties of tryptophan-containing α-subunits of the Escherichia coli tryptophan synthase
    • S.G. Choi, J.K. Hardman, Unfolding properties of tryptophan-containing α-subunits of the Escherichia coli tryptophan synthase, J. Biol. Chem. 270 (1995) 28177-28182.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28177-28182
    • Choi, S.G.1    Hardman, J.K.2
  • 21
    • 0018805386 scopus 로고
    • An active proteolytic derivative of the α subunit of tryptophan synthase. Identification of the site of cleavage and characterization of the fragments
    • W. Higgins, T. Fairwell, E.W. Miles, An active proteolytic derivative of the α subunit of tryptophan synthase. Identification of the site of cleavage and characterization of the fragments, Biochemistry 18 (1979) 4827-4835.
    • (1979) Biochemistry , vol.18 , pp. 4827-4835
    • Higgins, W.1    Fairwell, T.2    Miles, E.W.3
  • 22
    • 0022417649 scopus 로고
    • Characterization of an early intermediate in the folding of the α subunit of tryptophan synthase by hydrogen exchange measurement
    • A.M. Beasty, C.R. Matthews, Characterization of an early intermediate in the folding of the α subunit of tryptophan synthase by hydrogen exchange measurement, Biochemistry 24 (1985) 3547-3553.
    • (1985) Biochemistry , vol.24 , pp. 3547-3553
    • Beasty, A.M.1    Matthews, C.R.2
  • 23
    • 0028966987 scopus 로고
    • Contribution of individual tryptophan residues to the fluorescence spectrum of native and denatured forms of human carbonic anhydrase II
    • L.G. Martensson, P. Jonasson, P.O. Freskgard, M. Svensson, U. Carlsson, B.H. Jonsson, Contribution of individual tryptophan residues to the fluorescence spectrum of native and denatured forms of human carbonic anhydrase II, Biochemistry 34 (1995) 1011-1021.
    • (1995) Biochemistry , vol.34 , pp. 1011-1021
    • Martensson, L.G.1    Jonasson, P.2    Freskgard, P.O.3    Svensson, M.4    Carlsson, U.5    Jonsson, B.H.6
  • 24
    • 0025741701 scopus 로고
    • Fluorescence spectrum of barnase: Contributions of three tryptophan residues and a histidine-related pH dependence
    • R. Loewenthal, J. Sancho, A.R. Fersht, Fluorescence spectrum of barnase: Contributions of three tryptophan residues and a histidine-related pH dependence, Biochemistry 30 (1991) 6775-6779.
    • (1991) Biochemistry , vol.30 , pp. 6775-6779
    • Loewenthal, R.1    Sancho, J.2    Fersht, A.R.3
  • 25
    • 0033593272 scopus 로고    scopus 로고
    • Exploring the folding funnel of a polypeptide chain by biophysical studies on protein fragments
    • J.L. Neira, A.R. Fersht, Exploring the folding funnel of a polypeptide chain by biophysical studies on protein fragments, J. Mol. Biol. 285 (1999) 1309-1333.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1309-1333
    • Neira, J.L.1    Fersht, A.R.2
  • 26
    • 0020490638 scopus 로고
    • Guanidine hydrochloride induced unfolding of the α subunit of tryptophan synthase and of the two α proteolytic fragments: Evidence for stepwise unfolding of the two α domains
    • E.W. Miles, K. Yutani, K. Ogasahara, Guanidine hydrochloride induced unfolding of the α subunit of tryptophan synthase and of the two α proteolytic fragments: Evidence for stepwise unfolding of the two α domains, Biochemistry 21 (1982) 2586-2592.
    • (1982) Biochemistry , vol.21 , pp. 2586-2592
    • Miles, E.W.1    Yutani, K.2    Ogasahara, K.3
  • 27
    • 0021103614 scopus 로고
    • Effect of a single amino acid substitution on the folding of the α subunit of tryptophan synthase
    • C.R. Matthews, M.M. Crisanti, J.T. Manz, G.L. Gepner, Effect of a single amino acid substitution on the folding of the α subunit of tryptophan synthase, Biochemistry 22 (1983) 1445-1452.
    • (1983) Biochemistry , vol.22 , pp. 1445-1452
    • Matthews, C.R.1    Crisanti, M.M.2    Manz, J.T.3    Gepner, G.L.4
  • 28
    • 0023203755 scopus 로고
    • Proline isomerization and the slow folding reactions of the α subunit of tryptophan synthase from Escherichia coli
    • M.R. Hurle, C.R. Matthews, Proline isomerization and the slow folding reactions of the α subunit of tryptophan synthase from Escherichia coli, Biochim. Biophys. Acta 913 (1987) 179-184.
    • (1987) Biochim. Biophys. Acta , vol.913 , pp. 179-184
    • Hurle, M.R.1    Matthews, C.R.2
  • 29
    • 0028258789 scopus 로고
    • Unfolding-refolding kinetics of the tryptophan synthase subunit by CD and fluorescence measurements
    • K. Ogasahara, K. Yutani, Unfolding-refolding kinetics of the tryptophan synthase subunit by CD and fluorescence measurements, J. Mol. Biol. 236 (1994) 1227-1240.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1227-1240
    • Ogasahara, K.1    Yutani, K.2
  • 30
    • 0036965922 scopus 로고    scopus 로고
    • A cis-prolyl peptide bond isomerization dominates the folding of the α subunit of Trp synthase, a TIM barrel protein
    • Y. Wu, C.R. Matthews, A cis-prolyl peptide bond isomerization dominates the folding of the α 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
  • 31
    • 0031028212 scopus 로고    scopus 로고
    • Protein architecture, dynamics and allostery in tryptophan synthase channeling
    • P. Pan, E. Woehl, M.F. Dunn, Protein architecture, dynamics and allostery in tryptophan synthase channeling, Trends Biochem. Sci. 22 (1997) 22-27.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 22-27
    • Pan, P.1    Woehl, E.2    Dunn, M.F.3


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