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Volumn 262, Issue 3, 1999, Pages 858-865

Biochemical and structural characterization of recombinant copper- metallothionein from Saccharomyces cerevisiae

Author keywords

Cu metallothionein; Purification; Structure; X ray scattering

Indexed keywords

COPPER METALLOTHIONEIN; METALLOTHIONEIN; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 0033564015     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00451.x     Document Type: Article
Times cited : (10)

References (48)
  • 1
    • 0013616809 scopus 로고
    • Metallothionein and related molecules
    • Academic Press Inc, San Diego
    • 1. Riordan, J.F. & Vallee, B.L., eds (1991) Metallothionein and Related Molecules. Methods in Enzymology, Vol. 205. Academic Press Inc, San Diego.
    • (1991) Methods in Enzymology , vol.205
    • Riordan, J.F.1    Vallee, B.L.2
  • 2
    • 0023781524 scopus 로고
    • Biochemistry of metallothionein
    • 2. Kägi, J.H. & Schäffer, A. (1988) Biochemistry of metallothionein. Biochemistry 27, 8509-8515.
    • (1988) Biochemistry , vol.27 , pp. 8509-8515
    • Kägi, J.H.1    Schäffer, A.2
  • 3
    • 0027169905 scopus 로고
    • Yeast and mammalian metallothioneins functionally substitute for yeast copper-zinc superoxide dismutase
    • 3. Tamai, K.T., Gralla, E.B., Ellerby, L.M., Valentine, J. & Thiele, D.J. (1993) Yeast and mammalian metallothioneins functionally substitute for yeast copper-zinc superoxide dismutase. Proc. Natl Acad. Sci. USA 90, 8013-8017.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 8013-8017
    • Tamai, K.T.1    Gralla, E.B.2    Ellerby, L.M.3    Valentine, J.4    Thiele, D.J.5
  • 4
    • 0023072509 scopus 로고
    • Nutritional and physiological significance of metallothionein
    • 4. Bremner, I. (1987) Nutritional and physiological significance of metallothionein. Experientia 52 (Suppl.), 81-107.
    • (1987) Experientia , vol.52 , Issue.SUPPL. , pp. 81-107
    • Bremner, I.1
  • 5
    • 0021839915 scopus 로고
    • Function and autoregulation of yeast copperthionein
    • 5. Hamer, D.H., Thiele, D.J. & Lemontt, J.E. (1985) Function and autoregulation of yeast copperthionein. Science 228, 685-690.
    • (1985) Science , vol.228 , pp. 685-690
    • Hamer, D.H.1    Thiele, D.J.2    Lemontt, J.E.3
  • 6
    • 0343299702 scopus 로고
    • Tandem gene amplification mediates copper resistance in yeast
    • 6. Fogel, S. & Welch, J. (1982) Tandem gene amplification mediates copper resistance in yeast. Proc. Natl Acad. Sci. USA 79, 5342-5346.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 5342-5346
    • Fogel, S.1    Welch, J.2
  • 8
    • 0026691697 scopus 로고
    • Characterization of the copper- and silver-thiolate clusters in N-terminal fragments of the yeast ACE1 transcription factor capable of binding to its specific DNA recognition sequence
    • 8. Casas-Fine, J.R., Hu, S., Hamer, D. & Karpel, R.L. (1992) Characterization of the copper- and silver-thiolate clusters in N-terminal fragments of the yeast ACE1 transcription factor capable of binding to its specific DNA recognition sequence. Biochemistry 31, 6617-6626.
    • (1992) Biochemistry , vol.31 , pp. 6617-6626
    • Casas-Fine, J.R.1    Hu, S.2    Hamer, D.3    Karpel, R.L.4
  • 9
    • 0024291353 scopus 로고
    • Copper activates metallothionein gene transcription by altering conformation of a specific DNA binding protein
    • 9. Furst, P., Hu, S., Hackett, R. & Hamer, D. (1988) Copper activates metallothionein gene transcription by altering conformation of a specific DNA binding protein. Cell 55, 705-717.
    • (1988) Cell , vol.55 , pp. 705-717
    • Furst, P.1    Hu, S.2    Hackett, R.3    Hamer, D.4
  • 10
    • 0024044018 scopus 로고
    • ACE1 regulates expression of Saccharomyces cerevisiae metallothionein gene
    • 10. Thiele, D. (1987) ACE1 regulates expression of Saccharomyces cerevisiae metallothionein gene. Mol. Cell. Biol. 8, 2745-2752.
    • (1987) Mol. Cell. Biol. , vol.8 , pp. 2745-2752
    • Thiele, D.1
  • 11
    • 0024968557 scopus 로고
    • Cadmium-binding protein in a cadmium-resistant strain of Saccharomyces cerevisiae
    • 11. Inouhe, M., Hiyama, M., Tohoyama, H., Joho, M. & Murayama, T. (1989) Cadmium-binding protein in a cadmium-resistant strain of Saccharomyces cerevisiae. Biochim. Biophys. Acta 993, 51-55.
    • (1989) Biochim. Biophys. Acta , vol.993 , pp. 51-55
    • Inouhe, M.1    Hiyama, M.2    Tohoyama, H.3    Joho, M.4    Murayama, T.5
  • 12
    • 0023664953 scopus 로고
    • Structural and functional studies of the amino terminus of yeast metallothionein
    • 12. Wright, C.F., McKenney, K., Hamer, D.H., Byrd, J. & Winge, D.R. (1987) Structural and functional studies of the amino terminus of yeast metallothionein. J. Biol. Chem. 262, 12912-12919.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12912-12919
    • Wright, C.F.1    McKenney, K.2    Hamer, D.H.3    Byrd, J.4    Winge, D.R.5
  • 13
    • 0022432526 scopus 로고
    • Yeast metallothionein, sequence and metal binding properties
    • 13. Winge, D.R., Nielson, K.B., Gray, W.R. & Hamer, D.H. (1985) Yeast metallothionein, sequence and metal binding properties. J. Biol. Chem. 260, 14464-14470.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14464-14470
    • Winge, D.R.1    Nielson, K.B.2    Gray, W.R.3    Hamer, D.H.4
  • 15
    • 0027467849 scopus 로고
    • Cloning and expression of Saccharomyces cerevisiae copper-metallothionein gene in Escherichia coli and characterization of the recombinant protein
    • 15. Sayers, Z., Brouillon, P., Vorgias, C.E., Nolting, H.F., Hermes, C. & Koch, M.H.J. (1993) Cloning and expression of Saccharomyces cerevisiae copper-metallothionein gene in Escherichia coli and characterization of the recombinant protein. Eur. J. Biochem. 212, 521-528.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 521-528
    • Sayers, Z.1    Brouillon, P.2    Vorgias, C.E.3    Nolting, H.F.4    Hermes, C.5    Koch, M.H.J.6
  • 16
    • 0024287598 scopus 로고
    • Characterization of the copper-thiolate cluster in yeast metallothionein and two truncated mutants
    • 16. Byrd, J., Berger, R.M., McMillin, R.M., Wright, C.F., Hamer, D.H. & Winge, D.R. (1988) Characterization of the copper-thiolate cluster in yeast metallothionein and two truncated mutants. J. Biol. Chem. 263, 6688-6694.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6688-6694
    • Byrd, J.1    Berger, R.M.2    McMillin, R.M.3    Wright, C.F.4    Hamer, D.H.5    Winge, D.R.6
  • 18
    • 0001964202 scopus 로고
    • Cuprous-thiolate polymetallic clusters in biology
    • Karlin, K.D. & Tyeklar, Z., eds. Chapman & Hall, New York
    • 18. Winge, D.R., Dameron, C.T., George, G.N., Pickering, I.J. & Dance, I.G. (1993) Cuprous-thiolate polymetallic clusters in biology. In Bioinorganic Chemistry of Copper (Karlin, K.D. & Tyeklar, Z., eds), pp. 110-123. Chapman & Hall, New York.
    • (1993) Bioinorganic Chemistry of Copper , pp. 110-123
    • Winge, D.R.1    Dameron, C.T.2    George, G.N.3    Pickering, I.J.4    Dance, I.G.5
  • 19
    • 0026341261 scopus 로고
    • Copper coordination in metallothionein
    • 19. Winge, D.R. (1991) Copper coordination in metallothionein. Methods Enzymol. 205, 458-469.
    • (1991) Methods Enzymol. , vol.205 , pp. 458-469
    • Winge, D.R.1
  • 20
    • 0023917462 scopus 로고
    • X-ray absorption studies of yeast copper metallothionein
    • 20. George, G.N., Byrd, J. & Winge, D.R. (1988) X-ray absorption studies of yeast copper metallothionein. J. Biol. Chem. 263, 8199-8203.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8199-8203
    • George, G.N.1    Byrd, J.2    Winge, D.R.3
  • 21
    • 0000204980 scopus 로고
    • Establishment of the metal-to-cysteine connectivities in silver-substituted yeast metallothionein
    • 21. Narula, S.S., Mehra, R.K., Winge, D.R. & Armitage, I.M. (1991) Establishment of the metal-to-cysteine connectivities in silver-substituted yeast metallothionein. J. Am. Chem. Soc. 113, 9354-9358.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 9354-9358
    • Narula, S.S.1    Mehra, R.K.2    Winge, D.R.3    Armitage, I.M.4
  • 22
    • 0027321313 scopus 로고
    • 1H NMR assignments reflecting conformational heterogeneity at the C terminus
    • 1H NMR assignments reflecting conformational heterogeneity at the C terminus. Biochemistry 32, 6773-6787.
    • (1993) Biochemistry , vol.32 , pp. 6773-6787
    • Narula, S.S.1    Winge, D.R.2    Armitage, I.3
  • 23
    • 0030052073 scopus 로고    scopus 로고
    • 3D solution structure of copper and silver-substituted yeast metallothioneins
    • 23. Peterson, C.W., Narula, S.S. & Armitage, I.A. (1996) 3D solution structure of copper and silver-substituted yeast metallothioneins. FEBS Lett. 379, 85-93.
    • (1996) FEBS Lett. , vol.379 , pp. 85-93
    • Peterson, C.W.1    Narula, S.S.2    Armitage, I.A.3
  • 24
    • 0026328575 scopus 로고
    • Large-scale preparation of metallothionein: Biological sources
    • 24. Vasak, M. (1991) Large-scale preparation of metallothionein: biological sources. Methods Enzymol. 205, 39-41.
    • (1991) Methods Enzymol. , vol.205 , pp. 39-41
    • Vasak, M.1
  • 25
    • 0026335647 scopus 로고
    • Purification and quantification of metallothioneins by reversed-phase-high-performance liquid chromatography
    • 25. Richards, M.P. (1991) Purification and quantification of metallothioneins by reversed-phase-high-performance liquid chromatography. Methods Enzymol. 205, 217-238.
    • (1991) Methods Enzymol. , vol.205 , pp. 217-238
    • Richards, M.P.1
  • 26
    • 0026344710 scopus 로고
    • Quantification and identification of metallothioneins by gel electrophoresis and silver staining
    • 26. McCormick, C.C. & Lin, L.-Y. (1991) Quantification and identification of metallothioneins by gel electrophoresis and silver staining. Methods Enzymol. 205, 71-78.
    • (1991) Methods Enzymol. , vol.205 , pp. 71-78
    • McCormick, C.C.1    Lin, L.-Y.2
  • 27
    • 0026317899 scopus 로고
    • Purification of yeast copper-metallothionein
    • 27. Weser, U. & Hanmann, H.-J. (1991) Purification of yeast copper-metallothionein. Methods Enzymol. 205, 274-278.
    • (1991) Methods Enzymol. , vol.205 , pp. 274-278
    • Weser, U.1    Hanmann, H.-J.2
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 30. Laemmli, U. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 31
    • 0020114103 scopus 로고
    • X-ray scattering and diffraction on disordered systems using synchrotron radiation
    • 31. Koch, M.H.J. & Bordas, J. (1983) X-ray scattering and diffraction on disordered systems using synchrotron radiation. Nucl. Instrum. Methods 208, 461-469.
    • (1983) Nucl. Instrum. Methods , vol.208 , pp. 461-469
    • Koch, M.H.J.1    Bordas, J.2
  • 32
    • 0019067193 scopus 로고
    • The localization method used at EMBL
    • 32. Gabriel, A. & Dauvergne (1982) The localization method used at EMBL. Nucl. Instrum. Methods 201, 223-224.
    • (1982) Nucl. Instrum. Methods , vol.201 , pp. 223-224
    • Gabriel, A.1    Dauvergne2
  • 33
    • 0024033744 scopus 로고
    • Data acquisition systems for linear and area X-ray detectors using delay-line readout
    • 33. Boulin, C.J., Kempf, R., Gabriel, A. & Koch, M.H.J. (1988) Data acquisition systems for linear and area X-ray detectors using delay-line readout. Nucl. Instrum. Methods 269, 312-320.
    • (1988) Nucl. Instrum. Methods , vol.269 , pp. 312-320
    • Boulin, C.J.1    Kempf, R.2    Gabriel, A.3    Koch, M.H.J.4
  • 34
    • 0022787110 scopus 로고
    • Data appraisal, evaluation and display for synchrotron radiation experiments: Hardware and software
    • 34. Boulin, C.J., Kempf, R., Koch, M.H.J. & McLaughlin, S.M. (1986) Data appraisal, evaluation and display for synchrotron radiation experiments: hardware and software. Nucl. Instrum. Methods 249, 399-407.
    • (1986) Nucl. Instrum. Methods , vol.249 , pp. 399-407
    • Boulin, C.J.1    Kempf, R.2    Koch, M.H.J.3    McLaughlin, S.M.4
  • 35
    • 0001132350 scopus 로고
    • Scattering from noncrystalline systems
    • Ebashi, S., Koch, M. & Rubenstein, E., eds. Elsevier, Amsterdam
    • 35. Koch, M.H.J. (1991) Scattering from noncrystalline systems. In Handbook on Synchrotron Radiation (Ebashi, S., Koch, M. & Rubenstein, E., eds) Vol. 4, pp. 241-268. Elsevier, Amsterdam.
    • (1991) Handbook on Synchrotron Radiation , vol.4 , pp. 241-268
    • Koch, M.H.J.1
  • 36
    • 0027578071 scopus 로고
    • A direct indirect method of small-angle scattering data treatment
    • 36. Svergun, D.I. (1993) A direct indirect method of small-angle scattering data treatment. J. Appl. Crystallogr. 26, 258-267.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 258-267
    • Svergun, D.I.1
  • 37
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect transform methods using perceptual criteria
    • 37. Svergun, D.I. (1992) Determination of the regularization parameter in indirect transform methods using perceptual criteria. J. Appl. Crystallogr. 25, 495-503.
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 38
    • 84944815124 scopus 로고
    • Small-angle scattering data treatment by the regularization method
    • 38. Svergun, D.I., Semenyuk, A.V. & Feigin, L.A. (1988) Small-angle scattering data treatment by the regularization method. Acta Crystallogr. 44, 244-250.
    • (1988) Acta Crystallogr. , vol.44 , pp. 244-250
    • Svergun, D.I.1    Semenyuk, A.V.2    Feigin, L.A.3
  • 39
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macro-molecules from atomic coordinates
    • 39. Svergun, D.I., Barberato, C. & Koch, M.H.J. (1995) CRYSOL - a program to evaluate X-ray solution scattering of biological macro-molecules from atomic coordinates. J. Appl. Crystallogr. 28, 768-773.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 40
    • 0027050011 scopus 로고
    • Sequence-structure matching in globular proteins: Application to supersecondary and tertiary structure determination
    • 40. Godzik, A. & Skolnick, J. (1992) Sequence-structure matching in globular proteins: application to supersecondary and tertiary structure determination. Proc. Natl Acad. Sci. USA 89, 12098-12102.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 12098-12102
    • Godzik, A.1    Skolnick, J.2
  • 42
    • 0026350008 scopus 로고
    • Purification of canine hepatic lysosomal copper-metallothionein
    • 42. Stockert, R.J., Morell, A.G. & Sternlieb, I. (1991) Purification of canine hepatic lysosomal copper-metallothionein. Methods Enzymol. 205, 287-291.
    • (1991) Methods Enzymol. , vol.205 , pp. 287-291
    • Stockert, R.J.1    Morell, A.G.2    Sternlieb, I.3
  • 43
    • 0026345449 scopus 로고
    • Purification of Neurospora crassa copper-metallothionein
    • 43. Lerch, K. (1991) Purification of Neurospora crassa copper-metallothionein. Methods Enzymol. 205, 278-283.
    • (1991) Methods Enzymol. , vol.205 , pp. 278-283
    • Lerch, K.1
  • 44
    • 0020475366 scopus 로고
    • Tetrahedral copper-sulphur coordination in yeast Cu-thionein an EXAFS study
    • 44. Bordas, J., Koch, M.H.J., Hartmann, H.-J. & Weser, U. (1982) Tetrahedral copper-sulphur coordination in yeast Cu-thionein an EXAFS study. FEBS Lett. 140, 19-21.
    • (1982) FEBS Lett. , vol.140 , pp. 19-21
    • Bordas, J.1    Koch, M.H.J.2    Hartmann, H.-J.3    Weser, U.4
  • 46
    • 0026353520 scopus 로고
    • Determination of three dimensional structure of metallothioneins by nuclear magnetic resonance spectroscopy in solution
    • 46. Wüthrich, K. (1991) Determination of three dimensional structure of metallothioneins by nuclear magnetic resonance spectroscopy in solution. Methods Enzymol. 205, 502-519.
    • (1991) Methods Enzymol. , vol.205 , pp. 502-519
    • Wüthrich, K.1


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