Novel thioredoxin targets in Dictyostelium discoideum identified by two-hybrid analysis: interactions of thioredoxin with elongation factor 1α and yeast alcohol dehydrogenase

References

Arnér, E.S.J., and Holmgren, A. (2000). Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem.267, 6102–6109.10.1046/j.1432-1327.2000.01701.xSearch in Google Scholar

Balmer, Y., and Schürmann, P. (2001). Heterodimer formation between thioredoxin f and fructose-1,6-bisphosphatase from spinach chloroplasts. FEBS Lett.492, 58–61.10.1016/S0014-5793(01)02229-3Search in Google Scholar

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. USA100, 370–375.10.1073/pnas.232703799Search in Google Scholar

Balmer, Y., Vensel, W.H., Tanaka, C.K., Hurkman, W.J., Gelhaye, E., Rouhier, N. Jacquot, J.P., Manier, 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. USA101, 2642–2647.10.1073/pnas.0308583101Search in Google Scholar

Belke, C.J., Chin, C.C.Q., and Wold, F. (1974). Effect of pH on the reactivity of the active-site sulfhydryl groups in yeast alcohol dehydrogenase. Biochemistry13, 3418–3420.10.1021/bi00713a037Search in Google Scholar

Bergmeyer, H.U. (1974). Methoden der enzymatischen Analyse. 3rd Edition (Weinheim, Germany: Verlag Chemie), pp. 458–459, 1552–1554.Search in Google Scholar

Brodegger, T. (2002). Molekularbiologische Funktionsanalysen von Thioredoxinen aus Dictyostelium discoideum. PhD thesis (Kassel, Germany: University of Kassel).Search in Google Scholar

Brodegger, T., Stockmann, A., Nellen, W., Follmann, H., and Oberstraß, J. (2001). Identification of new thioredoxin interaction partners by the two-hybrid system. Biol. Chem.382, S167.Search in Google Scholar

Bühner, M., and Sund, H. (1969). Yeast alcohol dehydrogenase. SH groups, disulfide groups, quaternary structure, and reactivation by reductive cleavage of disulfide groups. Eur. J. Biochem.11, 73–79.Search in Google Scholar

Chien, C., Bartel, P.L., Sternglanz, R., and Fields, S. (1991). The two-hybrid system: a method to identify genes for proteins that interact with a protein of interest. Proc. Natl. Acad. Sci. USA88, 9578–9582.10.1073/pnas.88.21.9578Search in Google Scholar

Condeelis, J. (1995). Elongation factor 1α, translation and the cytoskeleton. Trends Biochem. Sci.20, 169–170.10.1016/S0968-0004(00)88998-7Search in Google Scholar

Dagert, M., and Ehrlich, S.D. (1979). Prolonged incubation in calcium chloride improves the competence of Escherichia coli cells. Gene6, 23–28.10.1016/0378-1119(79)90082-9Search in Google Scholar

Deltour, L., Foglio, M.H., and Duester, G. (1999). Metabolic deficiencies in Adh null mutant mice. Overlapping roles of Adh1 and Adh4 in ethanol clearance and metabolism of retinol. J. Biol. Chem.274, 16796–16801.Search in Google Scholar

Devreotes, P., and Janetopolous, C. (2003). Eukaryotic chemotaxis: distinctions between directional sensing and polarization. J. Biol. Chem.278, 20445–20448.10.1074/jbc.R300010200Search in Google Scholar PubMed

Follmann, H. (2000). Light-dark and thioredoxin-mediated metabolic redox control in plant cells. In: The Redox State and Circadian Rhythms, T. Vanden Driessche, ed. (Dordrecht, The Netherlands: Kluwer Academic Publishers), pp. 59–83.10.1007/978-94-015-9556-8_4Search in Google Scholar

Follmann, H., and Häberlein, I. (1995). Thioredoxins: universal, yet specific thiol-disulfide redox cofactors. BioFactors5, 147–156.Search in Google Scholar

Gietz, R.D., and Woods, R.A. (1995). Transforming yeast with DNA. Methods Mol. Cell. Biol.5, 255–269.Search in Google Scholar

Goyer, A., Decottignies, P., Issakidis-Bourguet, E., and Miginiac-Maslow, M. (2001). Sites of interaction of thioredoxin with sorghum NADP malate dehydrogenase. FEBS Lett.505, 405–408.10.1016/S0014-5793(01)02860-5Search in Google Scholar

Hunt, T., Herbert, P., Campbell, E.A., Delidakis, C., and Jackson, R.J. (1983). The use of affinity chromatography reveals a requirement for NADPH, thioredoxin, and thioredoxin reductase for the maintenance of high protein synthesis activity in rabbit reticulocyte lysates. Eur. J. Biochem.131, 303–311.10.1111/j.1432-1033.1983.tb07263.xSearch in Google Scholar

Jacquot, J.P., Vidal, S., Gadal, P., and Schürmann, P. (1978). Evidence for the existence of several enzyme-specific thioredoxins in plants. FEBS Lett.96, 243–246.10.1016/0014-5793(78)80410-4Search in Google Scholar

Jörnvall, H. (1977). Differences between alcohol dehydrogenases. Eur. J. Biochem.72, 443–452.10.1111/j.1432-1033.1977.tb11268.xSearch in Google Scholar

Karlin, S., and Altschul, S.F. (1990). Methods for assessing the statistical significance of molecular sequence features for general scoring schemes. Proc. Natl. Acad. Sci. USA87, 2264–2268.10.1073/pnas.87.6.2264Search in Google Scholar

Kern, R., Malki, A., Holmgren, A., and Richarme, G. (2003). Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase. Biochem. J.371, 965–972.10.1042/bj20030093Search in Google Scholar

Kuspa, A., Dingermann, T., and Nellen, W. (1995). Analysis of gene function in Dictyostelium. Experientia51, 1116–1123.10.1007/BF01944729Search in Google Scholar

Laurent, T.C., Moore, C.E., and Reichard, P. (1964). Enzymatic synthesis of deoxyribonucleotides. Isolation and characterisation of thioredoxin, the hydrogen donor from Escherichia coli. J. Biol. Chem.239, 3436–3444.10.1016/S0021-9258(18)97742-2Search in Google Scholar

Maeda, Y., Inouye, K., and Takeuchi, I. (1997). Dictyostelium– A Model System for Cell and Developmental Biology (Tokyo, Japan: Universal Academy Press).Search in Google Scholar

Makino, Y., Yoshikawa, N., Okamoto, K., Hirota, K., Yodoi, J., Makino, I., and Tanaka, H. (1999). Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function. J. Biol. Chem.274, 3182–3188.10.1074/jbc.274.5.3182Search in Google Scholar

Marcus, F., and Harrsch, P.B. (1990). Amino acid sequence of chloroplast fructose-1,6-bisphosphatase. Arch. Biochem. Biophys.279, 151–157.10.1016/0003-9861(90)90475-ESearch in Google Scholar

Mazzurco, M., Sulaman, W., Elina, H., Cock, J.M., and Goring, D.R. (2001). Further analysis of the interactions between Brassica S receptor kinase and three interacting proteins in the yeast two-hybrid system. Plant Mol. Biol.45, 365–376.10.1023/A:1006412329934Search in Google Scholar

Nissen, P., Thirup, S., Kjeldgaard, M., and Nyborg, J. (1999). The crystal structure of Cys-tRNACys-EF-Tu-GDPNP. Struct. Fold Des.7, 143–156.10.1016/S0969-2126(99)80021-5Search in Google Scholar

Porqué, P.G., Baldesten, A., and Reichard, P. (1970). Purification of a thioredoxin system from yeast. J. Biol. Chem.245, 2363–2370.10.1016/S0021-9258(18)63161-8Search in Google Scholar

Russell, D.W., Smith, M., Williamson, V.M., and Young, E.T. (1983). Nucleotide sequence of the yeast alcohol dehydrogenase II gene. J. Biol. Chem.258, 2674–2682.10.1016/S0021-9258(18)32979-XSearch in Google Scholar

Schägger, H., and von Jagow, G. (1987). Tricine SDS polyacrylamide gel electrophoresis for the separation of proteins in the range of 1–100 kDa. Anal. Biochem.166, 368–379.10.1016/0003-2697(87)90587-2Search in Google Scholar

Stockmann, A. (2002). Analyse der Wechselwirkungen zwischen Thioredoxin 1 und Elongationsfaktor 1α. Diploma (MSc) thesis (Kassel, Germany: University of Kassel).Search in Google Scholar

Villeret, V., Huang, S., Zhang, Y., Xue, Y., and Lipscomb, W.N. (1995). Crystal structure of spinach chloroplast fructose-1,6-bisphosphatase. Biochemistry34, 4299–4306.10.1021/bi00013a019Search in Google Scholar

Wallenfels, K., and Sund, H. (1957). Über den Mechanismus der Wasserstoffübertragung mit Pyridinnucleotiden. Freie SH-Gruppen und Aktivität bei Alkoholdehydrogenase aus Hefe. Biochem. Z.329, 17–30.Search in Google Scholar

Wetterauer, B., Jacquot, J.P., and Veron, M. (1992a) Thioredoxins from Dictyostelium discoideum are a developmentally regulated multigene family. J. Biol. Chem.267, 9895–9904.10.1016/S0021-9258(19)50177-6Search in Google Scholar

Wetterauer, B., Veron, M., Miginiac-Maslow, M., Decottignies, P., and Jacquot, J.P. (1992b). Biochemical characterisation of thioredoxin 1 from Dictyostelium discoideum. Eur. J. Biochem.209, 643–649.10.1111/j.1432-1033.1992.tb17331.xSearch in Google Scholar PubMed

Yamanaka, H., Maehira, F., Oshiro, M., Asato, T., Yanagawa, Y, Takei, H., and Nakashima, Y. (2000). A possible interaction of thioredoxin with VDUP1 in HeLa cells detected in a yeast two-hybrid system. Biochem. Biophys. Res. Comm.271, 796–800.10.1006/bbrc.2000.2699Search in Google Scholar PubMed

Yang, F., Demma, M., Warren, V., Dharmawardhane, S., and Condeelis, J. (1990). Identification of an actin-binding protein from Dictyostelium discoideum as elongation factor 1α. Nature347, 494–496.10.1038/347494a0Search in Google Scholar PubMed