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Photosynthetic Enzyme Regulation by the Ferredoxin/Thioredoxin and the Ferralterin Mechanisms

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Genetic Engineering of Symbiotic Nitrogen Fixation and Conservation of Fixed Nitrogen

Abstract

One type of covalent enzyme modification that has been used in studies on the structure and mechanism of action of enzymes is a change in the oxidation state of a “nonprosthetic” part of the protein, such as a sulfhydryl group. Limited attention has been given to the idea that oxidation-reduction changes may be used to regulate the activation of enzymes in a manner analogous to other types of reversible covalent modification, such as phosphorylation-dephosphorylation and adenylation-deadenylation. We summarize in this report evidence that enzyme regulation due to a reversible oxidation-reduction change is a process fundamental to photosyn-thetic and perhaps to other types of living cells. In this article we will first describe work from our own laboratory that led to the finding of a redox-based regulatory mechanism in photosynthesis; we will then relate these findings to other mechanisms of light-dependent enzyme regulation in chloroplasts, including the recently found ferralterin mechanism.

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References

  • Anderson, L. E., 1980, Light modulation of enzyme activity in green plants: the LEM system, Federation Proc., 39:1931.

    Google Scholar 

  • Anderson, L. E., and Avron, M., 1976, Light modulation of enzyme activity in chloroplasts, Plant Physiol., 57:209.

    Article  PubMed  CAS  Google Scholar 

  • Ashton, A. R., and Anderson, L. E., 1979, Reconstitution of the light activation system for pea leaf chloroplast malate dehydrogenase, Plant Physiol., 63,suppl. 24.

    Google Scholar 

  • Ashton, A. R., and Anderson, L. E., 1980, Resolution and reconstitution of the light-dependent modulation system of chloroplast enzymes, Abstracts, 5th Intl. Congr. Photosynthesis, Halkidiki, Greece.

    Google Scholar 

  • Binder, A., Jagendorf, A., and Ngo, E., 1978, Isolation and composition of the subunits of spinach chloroplast coupling factor protein, J. Biol. Chem., 253:3094.

    PubMed  CAS  Google Scholar 

  • Black, S., Harte, E. M., Hudson, B., and Wartofsky, L., 1960, A specific enzymatic reduction of L(-) methionine sulfoxide and a related nonspecific reduction of disulfides, J. Biol. Chem., 235:2910.

    CAS  Google Scholar 

  • Breazeale, V. D., Buchanan, B. B., and Wolosiuk, R. A., 1978, Chloroplast sedoheptulase 1, 7-biphosphatase: Evidence for regulation by the ferredoxin/thioredoxin system, Zeit. Naturforsch. 33c:521.

    CAS  Google Scholar 

  • Brill, W. J., Westphal, J., Stieghorst, M., Davis, L. C., and Shah, V. K., 1974, Detection of nitrogenase components and other non-heme iron proteins in Polyacrylamide gels, Anal. Biochem., 60:237.

    Article  PubMed  CAS  Google Scholar 

  • Buchanan, B. B., Kalberer, P. P., and Arnon, D. E., 1967, Ferredoxin-activated fructose diphosphatase in isolated chloroplasts, Biochem. Biophys. Res. Commun., 29:74.

    Article  PubMed  CAS  Google Scholar 

  • Buchanan, B. B., Schürmann, P., and Kalberer, P. P., 1971, Ferre-doxin-activated fructose diphosphatase of spinach chloroplasts, J. Biol. Chem., 246:5952.

    PubMed  CAS  Google Scholar 

  • Buchanan, B. B., and Wolosiuk, R. A., 1976, Photosynthetic regulatory protein found in animal and bacterial cells, Nature, 264:669.

    Article  PubMed  CAS  Google Scholar 

  • Buchanan, B. B., Wolosiuk, R. A., Crawford, N. A., and Yee, B. C., 1978, Evidence for three thioredoxins in leaves, Plant Physiol., 61:38S.

    Article  Google Scholar 

  • Buchanan, B. B., Crawford, N. A., and Wolosiuk, R. A., 1979, Activation of plant acid phosphatases by oxidized glutathionine and dehydroascorbate, Plant Sci. Lett., 14:245.

    Article  CAS  Google Scholar 

  • Crawford, N. A., Yee, B. C., Nishizawa, A. N., and Buchanan, B. B., 1979, Occurrence of cytoplasmic f and m-type thioredoxins in leaves, FEBS Lett., 104:141.

    Article  CAS  Google Scholar 

  • Frieden, C., 1971, Protein-protein interaction and enzymatic activity, Ann. Rev. Biochem., 40:653.

    Article  PubMed  CAS  Google Scholar 

  • Groden, D., and Beck, E., 1977, Characterization of a membrane bound, ascorbate specific peroxidase from spinach chloroplasts, Abstracts, 4th Int. Cong. Photosynthesis, Reading, U.K.

    Google Scholar 

  • Haddox, M. K., Stephenson, J. H., Moser, M. E., and Goldberg, N. D., 1978, Oxidative-reductive modulation of Guinea pig splenic cell cyclase activity, J. Biol. Chem., 253:3143.

    PubMed  CAS  Google Scholar 

  • Hardy, R. W. F., and Burns, C., 1973, Comparative biochemistry of iron-sulfur proteins and dinitrogen fixation, in: “Iron-Sulfur Proteins,” W. Lovenberg, ed., Vol. 1, Academic Press, NY.

    Google Scholar 

  • Heldt, H. W., Chon, C. J., Lilley, R. McC., and Portis, A., 1978, The role of fructose—and sedoheptulose bisphosphatase in the control of CO2 fixation. Evidence from the effects of Mg++ concentration, pH and H2O2, Proc. 4th Int. Congr. Photosynthesis, The Biochem. Soc., London.

    Google Scholar 

  • Holmgren, A., Buchanan, B. B., and Wolosuik, R. A., 1977, Different receptors for somatostatin and opioids in neuroblastoma x glioma hybrid cells, FEBS Lett., 82:351.

    Article  PubMed  CAS  Google Scholar 

  • Holmgren, A., 1977, Bovine thioredoxin system, J. Biol. Chem., 252:4600.

    PubMed  CAS  Google Scholar 

  • Jacquot, J. P., Vidal, J., and Gadal, P., 1976, Identification of a protein factor involved in dithiothreitol activation of NADP malate dehydrogenase from French bean leaves, FEBS Lett., 71: 223.

    Article  PubMed  CAS  Google Scholar 

  • Jacquot, J. P., Vidal, J., Gadal, P., and Schürmann, P., 1978, Evidence for the existence of several enzyme specific thioredoxins in plants, FEBS Lett., 96:243.

    Article  CAS  Google Scholar 

  • Kagawa, T., and Hatch, M. D., 1977, Regulation of C4 photosynthesis: characterization of a protein factor mediating the activation and inactivation of NADP-malate dehydrogenase, Arch. Biochem. Biophys., 184:290.

    Article  PubMed  CAS  Google Scholar 

  • Lara, C., de la Torre, A., and Buchanan, B. B., 1980, A new protein factor functional in the ferredoxin-independent light activation of chloroplast fructose 1, 6-biphosphatase, Biochem. Biophys. Res. Commun., 93:544.

    Article  PubMed  CAS  Google Scholar 

  • Lara, C., de la Torre, A., and Buchanan, B. B., 1980, Ferraltrin: an iron-sulfur protein functional in enzyme regulation in photosynthesis, Biochem. Biophys. Res. Commun., 94:1337.

    Article  PubMed  CAS  Google Scholar 

  • Laurent, T. C., Moore, E. C., and Reichard, P., 1964, Enzymatic synthesis of deoxyribonucleotides, J. Biol. Chem., 239:3436.

    PubMed  CAS  Google Scholar 

  • Lendzian, K., and Bassham, J. A., 1975, Regulation of glucose-6-phosphate dehydrogenase in spinach chloroplasts by ribulose 1, 5-diphosphate NADPH/NADP+ ratios, Biochem. Biophys. Acta, 396:260.

    Article  PubMed  CAS  Google Scholar 

  • Lorimer, G. H., Badger, M. R., and Andrews, T. J., 1976, The activation of ribulose-1, 5-bisphosphate carboxylase by carbon dioxide and magnesium ions. Equilibria, kinetics, a suggested mechanism and physiological implications, Biochemistry, 15:529.

    Article  PubMed  CAS  Google Scholar 

  • Malkin, R., 1973, The chemical properties of ferredoxins, in: “Iron-Sulfur Proteins,” W. Lovenberg, ed., Vol. 2, Academic Press, New York.

    Google Scholar 

  • Mark, D. F., and Richardson, C. C., 1976, Escherichia coli thio-redoxin: a subunit of bacteriophage T7 DNA polymerase, Proc. Natl. Acad. Sci. USA, 73:780.

    Article  PubMed  CAS  Google Scholar 

  • McKinney, D. W., Buchanan, B. B., and Wolosiuk, R. A., 1978, Activation of chloroplast ATPase by reduced thioredoxin, Phyto-chemistry, 17:794.

    CAS  Google Scholar 

  • McKinney, D. W., Buchanan, B. B., and Wolosiuk, R. A., 1979, Association of a thioredoxin-like protein with chloroplast coupling factor (CF1), Biochem. Biophys. Res. Commun., 86:1178.

    Article  PubMed  CAS  Google Scholar 

  • Mills, J. D., Mitchell, P., and Schürmann, P., 1980, Modulation of coupling factor ATPase activity in intact chloroplasts, FEBS Lett., 112:173.

    Article  CAS  Google Scholar 

  • Moreno, C. G., Aparacio, P. J., Palacian, E., and Losada, M., 1972, Association of a Thioredoxin-like protein with chloroplast coupling factor (CF1), FEBS Lett., 26:11.

    Article  PubMed  CAS  Google Scholar 

  • Müller, B., Ziegler, I., and Ziegler, H., 1969, Lichtinduzierté, reversible aktivitatssteigerung der NADP-abhangigen glycerin-aldehyde−3-phosphat-dehydrogenase in chloroplasta, Eur. J. Biochem., 9:101.

    Article  PubMed  Google Scholar 

  • Nelson, N., Deters, H., Nelson, D. W., and Racker, E., 1973, Partial resolution of the enzymes catalyzing photophosphorylation, J. Biol. Chem., 248:2049.

    PubMed  CAS  Google Scholar 

  • Nelson, N., 1976, Structure and function of chloroplast ATPase, Biochem. Biophys. Acta, 456:314.

    PubMed  Google Scholar 

  • Nishizawa, A. N., Wolosiuk, R. A., and Buchanan, B. B., 1979, Chloroplast phenylalanine ammonia-lyase from spinach leaves, Planta, 145:7.

    Article  CAS  Google Scholar 

  • Petersen, T. A., Kirk, M., and Bassham, J. A., 1966, Light-dark transients in levels of intermediate compounds during photosynthesis in air-adapted Chlorella, Physiol. Plant., 19:219.

    Article  Google Scholar 

  • Pigiet, V., and Conley, R. R., 1978, Isolation and characterization of phosphothioredoxin from Escherichia coli, J. Biol. Chem., 253:1910.

    PubMed  CAS  Google Scholar 

  • Porque, P. G., Baldesten, A., and Reichard, J. P., 1970, Purification of a thioredoxin system from yeast, J. Biol. Chem., 245:2363.

    CAS  Google Scholar 

  • Pupillo, P., and Giuliani-Piccari, G. G., 1975, The reversible de-polymerization of spinach chloroplast glyceraldehyde-phosphate dehydrogenase, Eur. J. Biochem., 51:475.

    Article  PubMed  CAS  Google Scholar 

  • Reichard, P., 1968, The biosynthesis of deoxyribonucleotides, Eur. J. Biochem., 3:259.

    Article  PubMed  CAS  Google Scholar 

  • Scheibe, R., 1980, On the dark modulation of chloroplast enzymes, Federation Proc., 39:1771.

    Google Scholar 

  • Schürmann, P., and Buchanan, B. B., 1975, Role of ferredoxin in the activation of sedoheptulose diphosphatase in isolated chloro-plasts, Biochem. Biophys. Acta, 376:189.

    Article  PubMed  Google Scholar 

  • Schürmann, P., Wolosiuk, R. A., Breazeale, V. D., and Buchanan, B. B., 1976, Two proteins function in the regulation of photosyn-thetic CO2 assimilation in chloroplasts, Nature, 263:257.

    Article  Google Scholar 

  • Suske, G., Wagner, W., and Follmann, H., NADPH-dependent thioredoxin reductase and a new thioredoxin from wheat, Zeit. Naturforsch., 34:214.

    Google Scholar 

  • Wagner, W., and Follmann, H., 1977, A thioredoxin from green algae, Biochem. Biophys. Res. Commun., 77:1044.

    Article  CAS  Google Scholar 

  • Wagner, W., Follmann, H., and Schmidt, A., 1978, Multiple functions of thioredoxins, Zeit. Naturforsch., 33c:517.

    CAS  Google Scholar 

  • Wilson, L. G., Asahi, T., and Bandurski, R. S., 1971, Yeast sulfate-reducing system, J. Biol. Chem., 236:1822.

    Google Scholar 

  • Wildner, G. F., 1975, The regulation of glucose-6-phosphate dehydrogenase in chloroplasts, Zeit. Naturforsch., 30c:756.

    CAS  Google Scholar 

  • Wolosiuk, R. A., Crawford, N. A., Yee, B. C., and Buchanan, B. B., 1979, Isolation of three thioredoxins from spinach leaves, J. Biol. Chem., 254:1627.

    PubMed  CAS  Google Scholar 

  • Wolosiuk, R. A., and Buchanan, B. B., 1977, Thioredoxin and glutathione regulate photosynthesis in chloroplasts, Nature, 266:565.

    Article  CAS  Google Scholar 

  • Wolosiuk, R. A., and Buchanan, B. B., 1978, Regulation of chloroplast phosphoribulokinase by the ferredoxin/thioredoxin system, Arch. Biochem. Biophys., 189:97.

    Article  PubMed  CAS  Google Scholar 

  • Wolosiuk, R. A., Buchanan, B. B., and Crawford, N. A., 1977, Regulation of NADP-malate dehydrogenase by the light-activated ferredoxin/thioredoxin system of chloroplasts, FEBS Lett., 81:253.

    Article  CAS  Google Scholar 

  • Wolosiuk, R. A., and Buchanan, B. B., 1978, Activation of chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by the ferredoxin/thioredoxin system, Plant Physiol., 61:669.

    Article  PubMed  CAS  Google Scholar 

  • Ziegler, H., and Ziegler, I., 1965, Der einfluss der belichtung auf die NADP+-abhängige glycerinaldehyd-3-phosphat-dehydrog-enase, Planta (Berlin), 65:369.

    Article  CAS  Google Scholar 

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Author information

Authors and Affiliations

  1. Section of Cell Physiology, Department of Plant and Soil Biology, University of California, Berkeley, CA, 94720, USA

    Bob B. Buchanan

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  1. Bob B. Buchanan
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Editor information

Editors and Affiliations

  1. University of California, Davis, California, USA

    J. M. Lyons , R. C. Valentine , D. A. Phillips , D. W. Rains  & R. C. Huffaker , , ,  & 

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© 1981 Plenum Press, New York

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Buchanan, B.B. (1981). Photosynthetic Enzyme Regulation by the Ferredoxin/Thioredoxin and the Ferralterin Mechanisms. In: Lyons, J.M., Valentine, R.C., Phillips, D.A., Rains, D.W., Huffaker, R.C. (eds) Genetic Engineering of Symbiotic Nitrogen Fixation and Conservation of Fixed Nitrogen. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3953-3_23

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  • DOI: https://doi.org/10.1007/978-1-4684-3953-3_23

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-3955-7

  • Online ISBN: 978-1-4684-3953-3

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