Modification of the reactivity of spinach chloroplast thioredoxin f by site-directed mutagenesis

Plant Science

Volumn 149, Issue 2, 1999, Pages 183-190

  Del Val, Gregorio ^a   Maurer, Fabienne ^a   Stutz, Erhard ^a   Schürmann, Peter ^a  

^a UNIVERSITY OF NEUCHÂTEL   (Switzerland)

Author keywords

Dimer; Fructose 1,6 bisphosphatase; Protein protein interaction; Reactivity; Site directed mutagenesis; Spinach; Thioredoxin f

Indexed keywords

THIOREDOXIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; CHLOROPLAST; NONHUMAN; PHYTOCHEMISTRY; SITE DIRECTED MUTAGENESIS; SPINACH;

EID: 0033521164     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9452(99)00168-5     Document Type: Article

References (33)

1. Holmgren A. Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide. Structure. 3:1995;239-243.
2. Jacquot J.-P., Lancelin J.-M., Meyer Y. Thioredoxins: structure and function in plant cells. New. Phytol. 136:1997;543-570.
3. Nishizawa A.N., Buchanan B.B. Enzyme regulation in C4 photosynthesis. Purification and properties of thioredoxin-linked fructose bisphosphatase and sedoheptulose bisphosphatase from corn leaves. J. Biol. Chem. 256:1981;6119-6126.
4. +-ATPase. J. Biol. Chem. 272:1997;16924-16927.
5. Jacquot J.-P., Vidal J., Gadal P., Schürmann P. Evidence for the existence of several enzyme-specific thioredoxins in plants. FEBS Lett. 96:1978;243-246.
6. Wenderoth I., Scheibe R., von Schaewen A. Identification of the cysteine residues involved in redox modification of plant plastidic glucose-6-phosphate dehydrogenase. J. Biol. Chem. 272:1997;26985-26990.
7. Wolosiuk R.A., Crawford N.A., Yee B.C., Buchanan B.B. Isolation of three thioredoxins from spinach leaves. J. Biol. Chem. 254:1979;1627-1632.
8. Schürmann P., Maeda K., Tsugita A. Isomers in thioredoxins of spinach chloroplasts. Eur. J. Biochem. 116:1981;37-45.
9. Soulié 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. Eur. J. Biochem. 119:1981;497-502.
10. Prado F.E., Lázaro J.J., Hermoso R., Chueca A., Gorgé J.L. Purification and properties of pea (Pisum sativum L.) thioredoxin f, a plant thioredoxin with unique features in the activation of chloroplast fructose-1,6-bisphosphatase. Planta. 188:1992;345-353.
11. Kamo M., Tsugita A., Wiessner Ch., Wedel N., Bartling D., Herrmann R.G., Aguilar F., Gardet-Salvi L., Schürmann P. Primary structure of spinach-chloroplast thioredoxin f. Protein sequencing and analysis of complete cDNA clones for spinach-chloroplast thioredoxin f. Eur. J. Biochem. 182:1989;315-322.
12. Lepiniec L., Hodges M., Gadal P., Crétin C. Isolation, characterization and nucleotide sequence of a full-length pea cDNA encoding thioredoxin-f. Plant Mol. Biol. 18:1992;1023-1025.
13. Aguilar F., Brunner B., Gardet-Salvi L., Stutz E., Schürmann P. Biosynthesis of active spinach-chloroplast thioredoxin f in transformed E. coli. Plant Mol. Biol. 20:1992;301-306.
14. Capitani G., Markovic-Housley Z., Jansonius J.N., del Val G., Morris M., Schürmann P. Crystal structures of thioredoxins f and m from spinach chloroplasts. Garab G. Photosynthesis: Mechanisms and Effects (Proceedings of the XIth International Congress on Photosynthesis, Budapest, Hungary). 3:1998;1939-1942 Kluwer, Dordrecht.
15. Schürmann P., Gardet-Salvi L., Kamo M., Yano K., Tsugita A. Primary structures of regulatory proteins of the ferredoxin-thioredoxin system of spinach chloroplasts. Baltscheffsky M. Current Research in Photosynthesis. 4:1990;167-170 Kluwer, Dordrecht.
16. Weichsel A., Gasdaska J.R., Powis G., Montfort W.R. Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer. Structure. 4:1996;735-751.
17. López-Jaramillo J., Chueca A., Sahrawy M., Hermoso R., Lázaro J.J., Prado F.E., Gorgé J.L. Cloning and sequencing of a pea cDNA fragment coding for thioredoxin m. Plant Physiol. 105:1994;1021-1022.
18. Stein M., Jacquot J.-P., Jeannette E., Decottignies P., Hodges M., Lancelin J.-M., Mittard V., Schmitter J.-M., Miginiac-Maslow M. Chlamydomonas reinhardtii thioredoxins: structure of the genes coding for the chloroplastic m and cytosolic h isoforms; expression in Escherichia coli of the recombinant proteins, purification and biochemical properties. Plant Mol. Biol. 28:1995;487-503.
19. Lunn J.E., Agostino A., Hatch M.D. Regulation of NADP-malate dehydrogenase in C4 plants: activity and properties of maize thioredoxin m and the significance of non-active site thiol groups. Aust. J. Plant Physiol. 22:1995;577-584.
20. López-Jaramillo J., Chueca A., Jacquot J.P., Hermoso R., Lázaro J.J., Sahrawy M., Gorgé J.L. High-yield expression of pea thioredoxin m and assessment of its efficiency in chloroplast fructose-1,6-bisphosphatase activation. Plant Physiol. 114:1997;1169-1175.
21. Hirasawa M., Schürmann P., Jacquot J.-P., Manieri W., Jacquot P., Keryer E., Hartman F.C., Knaff D.B. Oxidation-reduction properties of chloroplast thioredoxins, ferredoxin:thioredoxin reductase and thioredoxin f-regulated enzymes. Biochemistry. 38:1999;5200-5205.
22. Lamotte-Guéry F.d., Miginiac-Maslow M., Decottignies P., Stein M., Minard P., Jacquot J.-P. Mutation of a negatively charged amino acid in thioredoxin modifies its reactivity with chloroplastic enzymes. Eur. J. Biochem. 196:1991;287-294.
23. Mora-García S., Rodriguez-Suárez R.J., Wolosiuk R.A. Role of electrostatic interactions on the affinity of thioredoxin for target proteins. Recognition of chloroplast fructose-1,6-bisphosphatase by mutant Escherichia coli thioredoxins. J. Biol. Chem. 273:1998;16273-16280.
24. Geck M.K., Larimer F.W., Hartman F.C. Identification of residues of spinach thioredoxin f that influence interactions with target enzymes. J. Biol. Chem. 271:1996;24736-24740.
25. Kunkel T.A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA. 82:1985;488-492.
26. P. Schürmann, The ferredoxin/thioredoxin system. In: L. Packer (Ed.), Methods in Enzymology, Academic Press, Orlando, Florida vol. 252, 1995, pp. 274-283.
27. Laemmli U.K., Favre M. Maturation of the head of bacteriophage T 4. J. Mol. Biol. 80:1973;575-599.
28. Hodges M., Miginiac-Maslow M., Decottignies P., Jacquot J.-P., Stein M., Lepiniec L., Crétin C., Gadal P. Purification and characterization of pea thioredoxin f expressed in Escherichia coli. Plant Mol. Biol. 26:1994;225-234.
29. Brandes H.K., Larimer F.W., Geck M.K., Stringer C.D., Schürmann P., Hartman F.C. Direct identification of the primary nucleophile of thioredoxin f. J. Biol. Chem. 268:1993;18411-18414.
30. Foyer C.H., Halliwell B. The presence of glutathione and glutathione reductase in chloroplasts: a proposed role in ascorbic acid metabolism. Planta. 133:1976;21-25.
31. Tsugita A., Maeda K., Schürmann P. Spinach chloroplast thioredoxins in evolutionary drift. Biochem. Biophys. Res. Commun. 115:1983;1-7.
32. Soulié J.-M., Buc J., Rivière M., Ricard J. Equilibrium binding of thioredoxin fb to chloroplastic fructose bisphosphatase. Evidence for a thioredoxin site distinct from the active site. Eur. J. Biochem. 152:1985;565-568.
33. Jeanmougin F., Thompson J.D., Gouy M., Higgins D.G., Gibson T.J. Multiple sequence alignment with Clustal X. Trends Biochem. Sci. 23:1998;403-405.