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Volumn 120, Issue 5, 1996, Pages 946-953

Acid and thermal unfolding of Escherichia coli dihyrdrofolate reductase

Author keywords

Acid unfolding; Dihydrofolate reductase; Intermediate; Molten globule; Thermal unfolding

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ACID; BACTERIAL ENZYME; DIHYDROFOLATE REDUCTASE; POTASSIUM CHLORIDE; TRYPTOPHAN;

EID: 0029847060     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021511     Document Type: Article
Times cited : (25)

References (36)
  • 1
    • 0020441466 scopus 로고
    • Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution
    • Bolin, J.T., Filman, D.J., Matthews, D.A., Hamlin, R.C., and Kraut, J. (1982) Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. J. Biol. Chem. 257, 13650-13662
    • (1982) J. Biol. Chem. , vol.257 , pp. 13650-13662
    • Bolin, J.T.1    Filman, D.J.2    Matthews, D.A.3    Hamlin, R.C.4    Kraut, J.5
  • 2
    • 0026065644 scopus 로고
    • Crystal structure of unliganded Escherichia coli dihydrofolate reductase: Ligand-induced conformational changes and cooperativity in binding
    • Bystroff, C. and Kraut, J. (1991) Crystal structure of unliganded Escherichia coli dihydrofolate reductase: Ligand-induced conformational changes and cooperativity in binding. Biochemistry 30, 2227-2239
    • (1991) Biochemistry , vol.30 , pp. 2227-2239
    • Bystroff, C.1    Kraut, J.2
  • 3
    • 0024963670 scopus 로고
    • Effects of multiple replacements at a single position on the folding and stability of dihydrofolate reductase from Escherichia coli
    • Garvey, E.P. and Matthews, C.R. (1989) Effects of multiple replacements at a single position on the folding and stability of dihydrofolate reductase from Escherichia coli. Biochemistry 28, 2083-2093
    • (1989) Biochemistry , vol.28 , pp. 2083-2093
    • Garvey, E.P.1    Matthews, C.R.2
  • 4
    • 0024457568 scopus 로고
    • Long-range electrostatic interactions can influence the folding, stability, and cooperativity of dihydrofolate reductase
    • Perry, K.M., Onuffer, J.J., Gittelman, M.S., Barmat, L., and Matthews, C.R. (1989) Long-range electrostatic interactions can influence the folding, stability, and cooperativity of dihydrofolate reductase. Biochemistry 28, 7961-7968
    • (1989) Biochemistry , vol.28 , pp. 7961-7968
    • Perry, K.M.1    Onuffer, J.J.2    Gittelman, M.S.3    Barmat, L.4    Matthews, C.R.5
  • 5
    • 0026005997 scopus 로고
    • Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy
    • Kuwajima, K., Garvey, E.P., Finn, B.E., Matthews, C.R., and Sugai, S. (1991) Transient intermediates in the folding of dihydrofolate reductase as detected by far-ultraviolet circular dichroism spectroscopy. Biochemistry 30, 7693-7703
    • (1991) Biochemistry , vol.30 , pp. 7693-7703
    • Kuwajima, K.1    Garvey, E.P.2    Finn, B.E.3    Matthews, C.R.4    Sugai, S.5
  • 6
    • 0024498518 scopus 로고
    • Dihydrofolate reductase: Multiple conformations and alternative modes of substrate binding
    • Birdsall, B., Feeney, S.J.B., Tendler, S.J., Hammond, D.J., and Roberts, G.C.K. (1989) Dihydrofolate reductase: Multiple conformations and alternative modes of substrate binding. Biochemistry 28, 2297-2305
    • (1989) Biochemistry , vol.28 , pp. 2297-2305
    • Birdsall, B.1    Feeney, S.J.B.2    Tendler, S.J.3    Hammond, D.J.4    Roberts, G.C.K.5
  • 7
    • 0026028965 scopus 로고
    • Evidence for two interconverting protein isomers in the methotrexate complex of dihydrofolate reductase from Escherichia coli
    • Falzone, C.J., Wright, P.E., and Benkovic, S.J. (1991) Evidence for two interconverting protein isomers in the methotrexate complex of dihydrofolate reductase from Escherichia coli. Biochemistry 30, 2184-2191
    • (1991) Biochemistry , vol.30 , pp. 2184-2191
    • Falzone, C.J.1    Wright, P.E.2    Benkovic, S.J.3
  • 8
    • 0023668190 scopus 로고
    • Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli
    • Fierke, C.A., Johnson, K.A., and Benkovic, S.J. (1987) Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli. Biochemistry 26, 4085-4092
    • (1987) Biochemistry , vol.26 , pp. 4085-4092
    • Fierke, C.A.1    Johnson, K.A.2    Benkovic, S.J.3
  • 9
    • 0025184401 scopus 로고
    • A second-site mutation at phenylalanine-137 that increases catalytic efficiency in the mutant aspartate-27→serine Escherichia coli dihydrofolate reductase
    • Howell, E.E., Booth, C., Farnum, M., Kraut, J., and Warren, M.S. (1990) A second-site mutation at phenylalanine-137 that increases catalytic efficiency in the mutant aspartate-27→serine Escherichia coli dihydrofolate reductase. Biochemistry 29, 8561-8569
    • (1990) Biochemistry , vol.29 , pp. 8561-8569
    • Howell, E.E.1    Booth, C.2    Farnum, M.3    Kraut, J.4    Warren, M.S.5
  • 10
    • 0025756093 scopus 로고
    • Impact on catalysis of secondary structure manipulation of the αC-helix of Escherichia coli dihydrofolate reductase
    • Li, L. and Benkovic, S.J. (1991) Impact on catalysis of secondary structure manipulation of the αC-helix of Escherichia coli dihydrofolate reductase. Biochemistry 30, 1470-1478
    • (1991) Biochemistry , vol.30 , pp. 1470-1478
    • Li, L.1    Benkovic, S.J.2
  • 11
    • 0027315969 scopus 로고
    • Reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: Verification and refinement of a four-channel model
    • Jennings, P.A., Finn, B.E., Jones, B.E., and Matthews, C.R. (1993) Reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: Verification and refinement of a four-channel model. Biochemistry 32, 3783-3789
    • (1993) Biochemistry , vol.32 , pp. 3783-3789
    • Jennings, P.A.1    Finn, B.E.2    Jones, B.E.3    Matthews, C.R.4
  • 12
    • 0028561835 scopus 로고
    • Development of nonpolar surfaces in the folding of Escherichia coli dihydrofolate reductase detected by 1-anilinonaphthalene-8-sulfonate binding
    • Jones, B.E., Jennings, P.A., Pierre, R.A., and Matthews, C.R. (1994) Development of nonpolar surfaces in the folding of Escherichia coli dihydrofolate reductase detected by 1-anilinonaphthalene-8-sulfonate binding. Biochemistry 33, 15250-15258
    • (1994) Biochemistry , vol.33 , pp. 15250-15258
    • Jones, B.E.1    Jennings, P.A.2    Pierre, R.A.3    Matthews, C.R.4
  • 13
    • 0029971560 scopus 로고    scopus 로고
    • A large compressibility change of protein induced by a single amino acid substitution
    • Gekko, K., Tamura, Y., Ohmae, E., Hayashi, H., Kagamiyama, H., and Ueno, H. (1996) A large compressibility change of protein induced by a single amino acid substitution. Protein Sci. 5, 542-545
    • (1996) Protein Sci. , vol.5 , pp. 542-545
    • Gekko, K.1    Tamura, Y.2    Ohmae, E.3    Hayashi, H.4    Kagamiyama, H.5    Ueno, H.6
  • 14
    • 0023055739 scopus 로고
    • Folding of dihydrofolate reductase from Escherichia coli
    • Touchette, N.A., Perry, K.M., and Matthews, C.R. (1986) Folding of dihydrofolate reductase from Escherichia coli. Biochemistry 25, 5445-5452
    • (1986) Biochemistry , vol.25 , pp. 5445-5452
    • Touchette, N.A.1    Perry, K.M.2    Matthews, C.R.3
  • 16
    • 0025989451 scopus 로고
    • Effects of point mutations in a hinge region on the stability, folding, and enzymatic activity of Escherichia coli dihydrofolate reductase
    • Ahrweiler, P.M. and Frieden, C. (1991) Effects of point mutations in a hinge region on the stability, folding, and enzymatic activity of Escherichia coli dihydrofolate reductase. Biochemistry 30, 7801-7809
    • (1991) Biochemistry , vol.30 , pp. 7801-7809
    • Ahrweiler, P.M.1    Frieden, C.2
  • 17
    • 0026648195 scopus 로고
    • Intramolecular catalysis of a proline isomerization reaction in the folding of dihydrofolate reductase
    • Texter, F.L., Spencer, D.B., Rosenstein, R., and Matthews, C.R. (1992) Intramolecular catalysis of a proline isomerization reaction in the folding of dihydrofolate reductase. Biochemistry 31, 5687-5691
    • (1992) Biochemistry , vol.31 , pp. 5687-5691
    • Texter, F.L.1    Spencer, D.B.2    Rosenstein, R.3    Matthews, C.R.4
  • 18
    • 0027411746 scopus 로고
    • Effects of point mutations in a flexible loop on the stability and enzymatic function of Escherichia coli dihydrofolate reductase
    • Gekko, K., Yamagami, K., Kunori, Y., Ichihara, S., Kodama, M., and Iwakura, M. (1993) Effects of point mutations in a flexible loop on the stability and enzymatic function of Escherichia coli dihydrofolate reductase. J. Biochem. 113, 74-80
    • (1993) J. Biochem. , vol.113 , pp. 74-80
    • Gekko, K.1    Yamagami, K.2    Kunori, Y.3    Ichihara, S.4    Kodama, M.5    Iwakura, M.6
  • 19
    • 0027998347 scopus 로고
    • Point mutations at glycine-121 of Escherichia coli dihydrofolate reductase: Important roles of a flexible loop in the stability and function
    • Gekko, K., Kunori, Y., Takeuchi, H., Ichihara, S., and Kodama, M. (1994) Point mutations at glycine-121 of Escherichia coli dihydrofolate reductase: Important roles of a flexible loop in the stability and function. J. Biochem. 116, 34-41
    • (1994) J. Biochem. , vol.116 , pp. 34-41
    • Gekko, K.1    Kunori, Y.2    Takeuchi, H.3    Ichihara, S.4    Kodama, M.5
  • 20
    • 0029939820 scopus 로고    scopus 로고
    • Effects of point mutations at the flexible loop glycine-67 of Escherichia coli dihydrofolate reductase on its stability and function
    • Ohmae, E., Iriyama, K., Ichihara, S., and Gekko, K. (1996) Effects of point mutations at the flexible loop glycine-67 of Escherichia coli dihydrofolate reductase on its stability and function. J. Biochem. 119, 703-710
    • (1996) J. Biochem. , vol.119 , pp. 703-710
    • Ohmae, E.1    Iriyama, K.2    Ichihara, S.3    Gekko, K.4
  • 22
    • 0028174361 scopus 로고
    • Energetics of the α-lactalbumin states: A calorimetric and statistical thermodynamic study
    • Griko, Y.V., Friere, E., and Privalov, P.L. (1994) Energetics of the α-lactalbumin states: A calorimetric and statistical thermodynamic study. Biochemistry 33, 1889-1899
    • (1994) Biochemistry , vol.33 , pp. 1889-1899
    • Griko, Y.V.1    Friere, E.2    Privalov, P.L.3
  • 24
    • 0027407097 scopus 로고
    • Dynamics of a monomeric insulin analogue: Testing the molten-globule hypothesis
    • Hua, Q.X., Ladbury, J.E., and Weiss, M.A. (1993) Dynamics of a monomeric insulin analogue: Testing the molten-globule hypothesis. Biochemistry 32, 1433-1442
    • (1993) Biochemistry , vol.32 , pp. 1433-1442
    • Hua, Q.X.1    Ladbury, J.E.2    Weiss, M.A.3
  • 25
    • 0024963570 scopus 로고
    • Conformational states of beta-lactamase: Molten-globule states at acidic and alkaline pH with high salt
    • Goto, Y. and Fink, A.L. (1989) Conformational states of beta-lactamase: Molten-globule states at acidic and alkaline pH with high salt. Biochemistry 28, 945-952
    • (1989) Biochemistry , vol.28 , pp. 945-952
    • Goto, Y.1    Fink, A.L.2
  • 26
    • 0027995384 scopus 로고
    • Classification of acid denaturation of proteins: Intermediates and unfolded states
    • Fink, A.L., Calciano, L.J., Goto, Y., Kurotsu, T., and Palleros, D.R. (1994) Classification of acid denaturation of proteins: Intermediates and unfolded states. Biochemistry 33, 12504-12511
    • (1994) Biochemistry , vol.33 , pp. 12504-12511
    • Fink, A.L.1    Calciano, L.J.2    Goto, Y.3    Kurotsu, T.4    Palleros, D.R.5
  • 27
    • 0026537527 scopus 로고
    • Dihydrofolate reductase gene as a versatile expression marker
    • Iwakura, M. and Tanaka, T. (1992) Dihydrofolate reductase gene as a versatile expression marker. J. Biochem. 111, 31-36
    • (1992) J. Biochem. , vol.111 , pp. 31-36
    • Iwakura, M.1    Tanaka, T.2
  • 29
    • 0001109155 scopus 로고
    • Unavoidable time-dependent ellipticity changes of proteins in the current CD measurements
    • Takeda, K. and Moriyama, Y. (1991) Unavoidable time-dependent ellipticity changes of proteins in the current CD measurements. J. Am. Chem. Soc. 113, 6700-6701
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 6700-6701
    • Takeda, K.1    Moriyama, Y.2
  • 30
    • 0001755735 scopus 로고
    • The effect of temperature on the fluorescence of some aromatic amino acids and proteins
    • Gally, J.A. and Edelman, G.M. (1962) The effect of temperature on the fluorescence of some aromatic amino acids and proteins. Biochim. Biophys. Acta 60, 499-509
    • (1962) Biochim. Biophys. Acta , vol.60 , pp. 499-509
    • Gally, J.A.1    Edelman, G.M.2
  • 31
    • 0002465965 scopus 로고
    • Program system SALS for nonlinear least-squares fitting in experimental sciences
    • (Matsushita, K., ed.) North Holland Publishing, Amsterdam
    • Nakagawa, T. and Oyanagi, Y. (1980) Program system SALS for nonlinear least-squares fitting in experimental sciences in Recent Developments in Statistical Inference and Data Analysis (Matsushita, K., ed.) pp. 221-225, North Holland Publishing, Amsterdam
    • (1980) Recent Developments in Statistical Inference and Data Analysis , pp. 221-225
    • Nakagawa, T.1    Oyanagi, Y.2
  • 32
    • 0027787520 scopus 로고
    • Further examination of the intermediate state in the denaturation of the tryptophan synthase alpha subunit. Evidence that the equilibrium denaturation intermediate is a molten globule
    • Ogasahara, K., Matsushita, E., and Yutani, K. (1993) Further examination of the intermediate state in the denaturation of the tryptophan synthase alpha subunit. Evidence that the equilibrium denaturation intermediate is a molten globule. J. Mol. Biol. 234, 1197-1206
    • (1993) J. Mol. Biol. , vol.234 , pp. 1197-1206
    • Ogasahara, K.1    Matsushita, E.2    Yutani, K.3
  • 33
    • 0028941934 scopus 로고
    • A calorimetric study of the thermal stability of barstar and its interaction with barnase
    • Martinez, J.C., Filimonov, V.V., Mateo, P.L., Schreiber, G., and Fersht, A.R. (1995) A calorimetric study of the thermal stability of barstar and its interaction with barnase. Biochemistry 34, 5224-5233
    • (1995) Biochemistry , vol.34 , pp. 5224-5233
    • Martinez, J.C.1    Filimonov, V.V.2    Mateo, P.L.3    Schreiber, G.4    Fersht, A.R.5
  • 34
    • 10544253281 scopus 로고
    • Effect of amino acid-replacement on the thermal transition and stability of E. coli dihydrofolate reductase
    • Kodama, M., Takebayashi, S., and Gekko, K. (1993) Effect of amino acid-replacement on the thermal transition and stability of E. coli dihydrofolate reductase (in Japanese). Nippon Kagaku Kaishi 22-27
    • (1993) Nippon Kagaku Kaishi , pp. 22-27
    • Kodama, M.1    Takebayashi, S.2    Gekko, K.3
  • 35
    • 0023041667 scopus 로고
    • Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: A comparative study of the folding reactions of α-lactalbumin and lysozyme
    • Ikeguchi, M., Kuwajima, K., Mitani, M., and Sugai, S. (1986) Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: A comparative study of the folding reactions of α-lactalbumin and lysozyme. Biochemistry 25, 6965-6972
    • (1986) Biochemistry , vol.25 , pp. 6965-6972
    • Ikeguchi, M.1    Kuwajima, K.2    Mitani, M.3    Sugai, S.4
  • 36
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings, P.A. and Wright, P.E. (1993) Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science 262, 892-896
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2


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