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Abstract:

To characterize the mechanism of chloroplast fructose‐1,6‐bisphosphatase activation, we have examined kinetic and structural changes elicited by protein perturbants and reductants. At variance with its well‐known capacity for enzyme inactivation, 150 mM sodium trichloroacetate yielded an activatable chloroplast fructose‐1,6‐bisphosphatase in the presence of 1.0 mM fructose 1,6‐bisphosphate and 0.1 mM Ca2+. Other sugar bisphosphates did not replace fructose 1,6‐bisphosphate whereas Mg2+ and Mn2+ were functional in place of Ca2+. Variations of the emission fluorescence of intrinsic fluorophores and a noncovalently bound extrinsic probe [2‐(P‐toluidinyl)naphthalene‐6‐sulfonate] indicated the presence of conformations different from the native form. A similar conclusion was drawn from the analysis of absorption spectra by means of fourth‐derivative spectrophotometry. The effect of these conformational changes on the reductive process was studied by subsequently incubating the enzyme with dithiothreitol. The reaction of chloroplast fructose‐1,6‐bisphosphatase with dithiothreitol was accelerated 13‐fold by the chaotropic anion: second‐order rate constants were 48.1 M−1· min−1 and 3.7 M−1· min−1 in the presence and in the absence of trichloroacetate, respectively. Thus, the enhancement of the reductive activation by compounds devoid of redox activity illustrated that the modification of intramolecular noncovalent interactions of chloroplast fructose‐1,6‐bisphosphatase plays an essential role in the conversion of enzyme disulfide bonds to sulfhydryl groups. In consequence, a conformational change would operate concertedly with the reduction of disulfide bridges in the light‐dependent activation mediated by the ferredoxin–thioredoxin system. Copyright © 1994, Wiley Blackwell. All rights reserved

Registro:

Documento: Artículo
Título:Enhancement of the reductive activation of chloroplast fructose‐1,6‐bisphosphatase by modulators and protein perturbants
Autor:Ballicora, M.A.; Wolosiuk, R.A.
Filiación:Instituto de Investigaciones Bioquímicas, Fundación Campomar, IIBBA‐CONICET, FCEN‐UBA, Buenos Aires, Argentina
Palabras clave:fructose 2,6 bisphosphatase; article; chloroplast; conformational transition; disulfide bond; enzyme inactivation; enzyme mechanism; priority journal; spinach; Cations, Divalent; Chloroplasts; Fructose-Bisphosphatase; Fructosediphosphates; Kinetics; Oxidation-Reduction; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Support, Non-U.S. Gov't; Trichloroacetic Acid; Vegetables
Año:1994
Volumen:222
Número:2
Página de inicio:467
Página de fin:474
DOI: http://dx.doi.org/10.1111/j.1432-1033.1994.tb18887.x
Handle:http://hdl.handle.net/20.500.12110/paper_00142956_v222_n2_p467_Ballicora
Título revista:European Journal of Biochemistry
Título revista abreviado:Eur. J. Biochem.
ISSN:00142956
CAS:Cations, Divalent; fructose-1,6-diphosphate, 488-69-7; Fructose-Bisphosphatase, EC 3.1.3.11; Fructosediphosphates; Trichloroacetic Acid, 76-03-9
PDF:https://bibliotecadigital.exactas.uba.ar/download/paper/paper_00142956_v222_n2_p467_Ballicora.pdf
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00142956_v222_n2_p467_Ballicora

Referencias:

  • Buchanan, B.B., Wolosiuk, R.A., Schurmann, P., (1979) Trends Biochem. Sci., 4, pp. 93-96
  • Wolosiuk, R.A., Ballicora, M.A., Hagelin, K., (1993) FASEB J., 7, pp. 622-633
  • Eklund, H., Gleason, F.K., Holmgren, A., (1991) Proteins, 11, pp. 13-28
  • Wolosiuk, R.A., Crawford, N.A., Yee, B.C., Buchanan, B.B., (1979) J. Biol. Chem., 254, pp. 1627-1632
  • Lamotte‐Guery, F., Miginiac‐Maslow, M., Decottignies, P., Stein, M., Minard, P., Jacquot, J.P., (1991) Eur. J. Biochem., 196, pp. 287-294
  • Haberlein, I., Wurfel, M., Follmann, H., (1992) Biochim. Biophys. Acta, 1121, pp. 293-296
  • Wolosiuk, R.A., (1986) Thioredoxin and glutaredoxin systems. Structure and Function, pp. 253-266. , Holmgren, A. et al., eds, pp., Raven Press, New York
  • Stein, M., Wolosiuk, R.A., The effect of chaotropic anions on the activation and the activity of spinach chloroplast fructose-1,6-bisphosphatase. (1987) J Biol Chem, 262, pp. 16171-16179
  • Prat‐Gay, G., Paladini, A., Jr., Stein, M., Wolosiuk, R.A., (1991) J. Biol. Chem., 266, pp. 20913-20921
  • Wolosiuk, R.A., Stein, M., (1990) Arch. Biochem. Biophys., 279, pp. 70-77
  • Chen, P.S., Toribara, T.I., Warner, H., (1956) Anal. Chem., 28, pp. 1756-1758
  • Yvon, M., Chabanet, C., Pelissier, J‐P., (1989) Int. J. Peptide Protein Res., 34, pp. 166-176
  • Ballicora, M.A., Wolosiuk, R.A., (1990) Plant Sci., 70, pp. 35-41
  • Marcus, F., Harrsch, P.B., (1990) Arch. Biochem. Biophys., 279, pp. 151-157
  • Teale, F.W.J., (1960) Biochem. J., 76, pp. 381-388
  • Lakowicz, J.R., (1986) Principles of fluorescence spectroscopy, pp. 257-295. , 3rd. edn, Raven Press, New York
  • Chardot, T., Queiroz‐Claret, C., Meunier, J.‐C., (1991) Biochimie, 73, pp. 1205-1209
  • Turner, D.C., Brand, L., (1968) Biochemistry, 7, pp. 3381-3390
  • Frankewich, R.P., Thimmaiah, K.N., Hinze, W.L., (1991) Anal. Chem., 63, pp. 2924-2933
  • Padros, E., Morros, A., Mañosa, J., Duñach, M., The State of Tyrosine and Phenylalanine Residues in Proteins Analyzed by Fourth-Derivative Spectrophotometry. Histone H1 and Ribonuclease A (1982) European Journal of Biochemistry, 127, pp. 117-122
  • Corley, E., Wolosiuk, R.A., (1985) J. Biol. Chem., 260, pp. 3978-3983
  • Soulie, J‐M., Buc, J., Meunier, J‐C., Pradel, J., Ricard, J., Molecular Properties of Chloroplastic Thioredoxin f and the Photoregulation of the Activity of Fructose 1,6-Bisphosphatase (1981) European Journal of Biochemistry, 119, pp. 497-502
  • Fraser, R.D.B., Suzuki, E., (1973) Physical principles and techniques in protein chemistry, pp. 301-355. , Leach, S. J., ed., part C, pp., Academic Press, New York
  • Chardot, T., Meunier, J.‐C., (1991) Biochem. J., 278, pp. 787-791
  • Stein, M., Lazaro, J.J., Wolosiuk, R.A., (1989) Eur. J. Biochem., 185, pp. 425-431
  • Russel, M., Model, P., (1986) J. Biol. Chem., 261, pp. 14997-15005
  • Huber, H.E., Russel, M., Model, P., Richardson, C.C., (1986) J. Biol. Chem., 261, pp. 15006-15012

Citas:

---------- APA ----------
Ballicora, M.A. & Wolosiuk, R.A. (1994) . Enhancement of the reductive activation of chloroplast fructose‐1,6‐bisphosphatase by modulators and protein perturbants. European Journal of Biochemistry, 222(2), 467-474.
http://dx.doi.org/10.1111/j.1432-1033.1994.tb18887.x
---------- CHICAGO ----------
Ballicora, M.A., Wolosiuk, R.A. "Enhancement of the reductive activation of chloroplast fructose‐1,6‐bisphosphatase by modulators and protein perturbants" . European Journal of Biochemistry 222, no. 2 (1994) : 467-474.
http://dx.doi.org/10.1111/j.1432-1033.1994.tb18887.x
---------- MLA ----------
Ballicora, M.A., Wolosiuk, R.A. "Enhancement of the reductive activation of chloroplast fructose‐1,6‐bisphosphatase by modulators and protein perturbants" . European Journal of Biochemistry, vol. 222, no. 2, 1994, pp. 467-474.
http://dx.doi.org/10.1111/j.1432-1033.1994.tb18887.x
---------- VANCOUVER ----------
Ballicora, M.A., Wolosiuk, R.A. Enhancement of the reductive activation of chloroplast fructose‐1,6‐bisphosphatase by modulators and protein perturbants. Eur. J. Biochem. 1994;222(2):467-474.
http://dx.doi.org/10.1111/j.1432-1033.1994.tb18887.x