Redox Regulation of Enzymes in Chloroplasts

Our group worked on the ferredoxin/thioredoxin system, a light-dependent redox system regulating the activitiy of key enzymes in chloroplasts. We have purified, cloned and overexpressed the proteins involved in the regulatory cascade, i.e. ferredoxin:thioredoxin reductase (FTR), a novel Fe-S protein, the thioredoxins f and m and one of the target enzymes, the fructose 1,6-bisphosphatase. These proteins are used to study their structure and the mechanism of redox regulation.

The three-dimensional structures of FTR and the two chloroplast thioredoxins have been solved in collaboration with Shaodong Dai in Uppsala (http://alpha2.bmc.uu.se/~dai/) and Guido Capitani (now at the University of Zürich, Biochemisches Institut, capitani@biocfebs.unizh.ch) at the Biozentrum in Basel, respectively. The FTR structure was published in Science in January 2000.

We have also made significant progress in the understanding of the reaction mechanism of the FTR which is studied in collaboration with Michael K. Johnson (http://www.uga.edu/cms/FacMKJ.html) at the Center for Metalloenzyme Studies, University of Georgia in Athens, USA.
 

Recent publications on the subject:

The local collaborators are indicated in bold

• Schwarz, O., P. Schürmann and H. Strotmann (1997). Kinetics and thioredoxin specificity of thiol modulation of the chloroplast H+-ATPase. J.Biol.Chem. 272: 16924-16927.
• Staples, C.R., E. Gaymard, A.L. Stritt-Etter, J. Telser, B.M. Hoffman, P. Schürmann, D.B. Knaff and M.K. Johnson (1998). Role of the [Fe4S4] cluster in mediating disulfide reduction in spinach ferredoxin: thioredoxin reductase. Biochemistry 37: 4612-4620.
• Raeber, L., E. Gaymard and P. Schürmann (1998). Cloning and sequencing of a full-length cDNA coding for the precursor of the catalytic subunit of ferredoxin:thioredoxin reductase (Accession No. Y15076) from soybean. Plant Physiol. 116: 446-446. (http://www.tarweed.com/pgr/PGR98-010.html )
• Iwadate, H., K. Kizuki, A.-L. Stritt-Etter, J. Li, P. Schürmann and A. Tsugita (1998). Primary structure of maize ferredoxin:thioredoxin reductase catalytic subunit. Research Communication in Biochemistry and Cell & Molecular Biology 2: 105-112.
• Balmer, Y. and Schürmann, P. (1998). Construction of mutants for the study of reduction of spinach fructose 1,6-bisphosphatase by thioredoxin f. In: Photosynthesis: Mechanisms and Effects (Proceedings of the XIth International Photosynthesis Congress, Budapest, Hungary), Garab, G. (Ed.), Vol.3, pp.1935-1938, Kluwer Academic Publishers, Dordrecht, The Netherlands.
• Capitani, G., Markovic-Housley, Z., Jansonius, J. N., del Val, G., Morris, M., and Schürmann, P. (1998). Crystal structures of thioredoxins f and m from spinach chloroplasts. Ibidem pp.1939-1942
• Dai, S., Schwendtmayer, C., Ramaswamy, S., Eklund, H., and Schürmann, P. (1998). Crystallization and crystallographic investigations of ferredoxin:thioredoxin reductase from Synachocystis sp.PCC6803. Ibidem pp.1931-1934
• Schwendtmayer, C., Manieri, W., Hirasawa, M., Knaff, D. B., and Schürmann, P. (1998). Cloning, expression and characterization of ferredoxin:thioredoxin reductase from Synechocystis sp.PCC6803. Ibidem pp.1927-1930
• Iwadate, H., Kizuki, K., Tsugita, A., Stritt-Etter, A.-L., Li, J. and Schürmann, P. (1998). Binding sites between variable and catalytic subunits of ferredoxin:thioredoxin reductase from maize. Research Communications in Biochemistry, Cell and Molecular Biology 2: 209-222.
• Hirasawa, M., Schürmann, P., Jacquot, J.-P., Manieri, W., Jacquot, P., Keryer, E., Hartman, F.C. and Knaff, D.B. (1999). Oxidation-reduction properties of chloroplast thioredoxins, ferredoxin:thioredoxin reductase and thioredoxin f-regulated enzymes. Biochemistry 38: 5200-5205.
• del Val, G., Maurer, F., Stutz, E. and Schürmann, P. (1999). Modification of the reactivity of spinach chloroplast thioredoxin f by site-directed mutagenesis. Plant Sci. 149: 183-190.
• Ballicora, M.A., Frueauf, J.B., Fu, Y., Schürmann, P. and Preiss, J. (2000). Activation of the potato tuber ADP-glucose pyrophosphorylase by thioredoxin. J.Biol.Chem. 275: 1315-1320.
• Capitani, G., Markovic-Housley, Z., del Val, G., Morris, M., Jansonius, J.N. and Schürmann, P. (2000). Crystal structures of two functionally different thioredoxins in spinach chloroplasts. J.Mol.Biol. 302: 135-154.
• Dai, S., Schwendtmayer, C., Schürmann, P., Ramaswamy, S. and Eklund, H. (2000). Redox signaling in chloroplasts: Cleavage of disulfides by an iron-sulfur cluster. Science 287: 655-658.
• Dai, S., Schwendtmayer, C., Johansson, K., Ramaswamy, S., Schürmann, P. and Eklund, H. (2000). How does light regulate chloroplast enzymes? Structure - function studies of the ferredoxin/thioredoxin system. Quart.Rev.Biophys. 33: 67-108.
• Gaymard, E., Franchini, L., Manieri, W., Stutz, E. and Schürmann, P. (2000). A dicistronic construct for the expression of functional spinach chloroplast ferredoxin:thioredoxin reductase in E.coli. Plant Sci. 158: 107-113.
• Jarret, C., Stauffer, F., Henz, M.E., Marty, M., Lüönd, R.M., Bobálová, J., Schürmann, P. and Neier, R. (2000). Inhibition of Escherichia coli porphobilinogen synthase using analogs of postulated intermediates. Chem.Biol. 7: 185-196.
• Kopriva, S., Suter, M., Weber, M., Schürmann, P. and Brunold, C. (2000) Characterization of APS reductase enzyme purified from Arabidopsis thaliana. In: Sulfur nutrition and sulfur assimilation in higher plants: molecular, biochemical and physiological aspects (Brunold, C., Rennenberg, H., De Kok, L.J., Stulen, I., and Davidian, J.-C., Eds.) pp. 223-224. Paul Haupt, Bern, Switzerland.
• Schürmann, P., Schwendtmayer, C., Dai, S., Ramaswamy, S. and Eklund, H. (2000) Structure and Function of Ferredoxin:Thioredoxin Reductase. Ibidem pp. 231-232.
• Suter, M., Weber, M., Kopriva, S., Kuhlemeier, C., Schürmann, P. and Brunold, C. (2000) Adenosine 5'-phosphosulfate sulfotransferase and adenosine 5'-phosphosulfate reductase are identical enzymes. Ibidem pp. 225-227.
• Schürmann, P. and Jacquot, J.-P. (2000). Plant thioredoxin systems revisited. (Jones, R.L., Bohnert, H.J., and Delmer, D.P., eds.), Annu.Rev.Plant Physiol.Plant Mol.Biol., Vol. 51, pp. 371-400. Annu.Reviews, Inc., Palo Alto, USA.
• Suter, M., von Ballmoos, P., Kopriva, S., Op den Camp, R., Schaller, J., Kuhlemeier, C., Schürmann, P. and Brunold, C. (2000). Adenosine 5'-Phosphosulfate Sulfotransferase and Adenosine 5'- Phosphosulfate Reductase Are Identical Enzymes. J.Biol.Chem. 275: 930-936.
• Balmer, Y., Stritt-Etter, A.-L., Hirasawa, M., Jacquot, J.-P., Keryer, E., Knaff, D.B. and Schürmann, P. (2001). Oxidation-reduction and activation properties of chloroplast fructose 1,6-bisphosphatase with mutated regulatory site. Biochemistry 40: 15444-15450.
• Balmer, Y. and Schürmann, P. (2001). Heterodimer formation between thioredoxin f and fructose 1,6-bisphosphatase from spinach chloroplasts. FEBS Letters 492: 58-61.
• Kopriva, S., Büchert, T., Fritz, G., Suter, M., Weber, M., Benda, R., Schaller, J., Feller, U., Schürmann, P., Schünemann, V., Trautwein, A.X., Kroneck, P.M.H. and Brunold, C. (2001). Plant adenosine 5'-phosphosulfate reductase is a novel iron-sulfur protein. J.Biol.Chem. 276: 42881-42886.
• Meyer, Y., Miginiac-Maslow, M., Schürmann, P. and Jacquot, J.-P. (2001). Protein-protein interactions in the plant thioredoxin dependent systems. In: Protein - Protein Interactions in Plant Biology (McManus, M.T., Laing, W., and Allan, A., eds.), The Annual Plant Reviews, Vol. 7, pp. 1-29. Sheffield Academic Press, Sheffield, England.
• Schürmann, P. and Buchanan, B.B. (2001). The structure and function of the ferredoxin/thioredoxin system in photosynthesis. In: Regulation of Photosynthesis (Aro, E.-M. and Andersson, B., eds.), Advances in Photosynthesis and Respiration, Vol. 11, pp. 331-361. Kluwer Academic Publishers, Dordrecht, The Netherlands.
• Zhang, N., Schürmann, P. and Portis Jr, A.R. (2001). Characterization of the regulatory function of the 46-kDa isoform of Rubisco activase from Arabidopsis. Photosynth.Res. 68: 29-37.
• Buchanan, B.B., Schürmann, P., Wolosiuk, R.A. and Jacquot, J.-P. (2002). The ferredoxin/thioredoxin system: from discovery to molecular structures and beyond. Photosynth.Res. 273: 215-222.
• Kopriva, S., Büchert, T., Fritz, G., Suter, M., Benda, R., Schünemann, V., Koprivova, A., Schürmann, P., Trautwein, A.X., Kroneck, P.M. and Brunold, C. (2002). The presence of an iron-sulfur cluster in adenosine 5'-phosphosulfate reductase separates organisms utilizing adenosine 5'-phosphosulfate and phosphoadenosine 5'-phosphosulfate for sulfate assimilation. J.Biol.Chem. 277: 21786-21791.
• König, J., Baier, M., Horling, F., Kahmann, U., Harris, G., Schürmann, P. and Dietz, K.J. (2002). The plant-specific function of 2-Cys peroxiredoxin-mediated detoxification of peroxides in the redox hierarchy of photosynthetic electron flux. Proc.Natl.Acad.Sci.USA 99: 5738-5743.
• Schürmann, P. (2002). Ferredoxin-dependent thioredoxin reductase: a unique Fe-S protein. In: Protein sensors of reactive oxygen species (Packer, L. and Sies, H., eds.), Methods in Enzymology, Vol. 347, pp. 403-411. Academic Press, San Diego, USA.
• Balmer, Y., Koller, A., del Val, G., Manieri, W., Schürmann, P. and Buchanan, B.B. (2003). Proteomics gives insight into the regulatory function of chloroplast thioredoxins. Proc.Natl.Acad.Sci.U.S.A 100: 370-375.
• Jameson, G.N.L., Walters, E.M., Manieri, W., Schürmann, P., Johnson, M.K. and Huynh, B.H. (2003). Spectroscopic Evidence for Site Specific Chemistry at a Unique Iron Site of the [4Fe-4S] Cluster in Ferredoxin:Thioredoxin Reductase. J.Am.Chem.Soc. 125: 1146-1147.
• Manieri, W., Franchini, L., Raeber, L., Dai, S., Stritt-Etter, A.-L. and Schürmann, P. (2003). N-terminal truncation of the variable subunit stabilizes spinach ferredoxin:thioredoxin reductase . FEBS Letters 549: 167-170.
• Schürmann, P. (2003). The ferredoxin/thioredoxin system. A light-dependent redox regulatory system in oxygenic photosynthetic cells. In: Cellular Implications of Redox Signalling (Gitler, C. and Danon, A., eds.), pp. 73-98. World Scientific Publishing Co Pte Ltd, Singapore.
• Schürmann, P. (2003). Redox Signaling in the Chloroplast — the Ferredoxin/Thioredoxin System. Antioxid.Redox Signal. 5: 69-78.
• Balmer, Y., Vensel, W.H., Tanaka, C.K., Hurkman, W.J., Gelhaye, E., Rouhier, N., Jacquot, J.P., Manieri, W., Schürmann, P., Droux, M. and Buchanan, B.B. (2004). Thioredoxin links redox to the regulation of fundamental processes of plant mitochondria. Proc.Natl.Acad.Sci.U.S.A 101: 2642-2647.
• Balmer, Y., Koller, A., del Val, G., Schürmann, P. and Buchanan, B.B. (2004). Proteomics uncovers proteins interacting electrostatically with thioredoxin in chloroplasts. Photosynth.Res. 79: 275-280.
• Capitani, G. and Schürmann, P. (2004). On the quaternary assembly of spinach chloroplast thioredoxin m. Photosynth.Res. 79: 281-285.
• Dai, S., Johansson, K., Miginiac-Maslow, M., Schürmann, P. and Eklund, H. (2004). Structural basis of redox signaling in photosynthesis: Structure and function of ferredoxin:thioredoxin reductase and target enzymes. Photosynth.Res. 79: 233-248.
• Glauser, D.A., Bourquin, F., Manieri, W. and Schürmann, P. (2004). Characterization of ferredoxin:thioredoxin reductase (FTR) modified by site-directed mutagenesis. J.Biol.Chem. 279: 16662-16669.
• Miller, M., Schürmann, P., Hodges, M. and Jacquot, J.-P. (2004). Isolation of the pea thioredoxin f precursor protein and characterization of its biochemical properties. Photosynth.Res. 79: 287-294.
• Mikkelsen, R., Mutenda, K.E., Mant, A., Schürmann, P. and Blennow, A. (2005). a-Glucan, water dikinase (GWD): A plastidic enzyme with redox-regulated and coordinated catalytic activity and binding affinity. Proc.Natl.Acad.Sci.U.S.A 102: 1785-1790.
  

Back to the main page of the University of Neuchâtel in French or in English

Back to the main page of biology in Neuchâtel in French or in English

Back to the main page of Biochemistry

Last modifications : 22nd February 2005

(editor: Jean-Marc Neuhaus)