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

Biological Chemistry

Volumn 385, Issue 12, 2004, Pages 1185-1192

  Brodegger, Thomas ^a   Stockmann, Anja ^a   Oberstraß, Jürgen ^a   Nellen, Wolfgang ^a   Follmann, Hartmut ^a  

^a UNIVERSITY OF KASSEL   (Germany)

Author keywords

Alcohol dehydrogenase; Disulfide formation; Elongation factors; Enzyme regulation; Thioredoxin oligomers; Thioredoxins

Indexed keywords

ALCOHOL DEHYDROGENASE; COMPLEMENTARY DNA; ELONGATION FACTOR 1ALPHA; GLUTATHIONE; OXIDOREDUCTASE; RIBONUCLEOTIDE REDUCTASE; THIOREDOXIN;

AFFINITY CHROMATOGRAPHY; AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; DICTYOSTELIUM DISCOIDEUM; DNA LIBRARY; ENZYME MECHANISM; IN VITRO STUDY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN TARGETING; SCREENING TEST; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; TWO HYBRID SYSTEM; YEAST;

ALCOHOL DEHYDROGENASE; ANIMALS; CHROMATOGRAPHY, AFFINITY; CROSS-LINKING REAGENTS; DICTYOSTELIUM; DISULFIDES; DNA, COMPLEMENTARY; ENZYME INHIBITORS; GENE LIBRARY; KINETICS; MUTAGENESIS, SITE-DIRECTED; OXIDOREDUCTASES; PEPTIDE ELONGATION FACTOR 1; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RIBONUCLEOTIDE REDUCTASES; RIBOSOMES; SACCHAROMYCES CEREVISIAE; THIOREDOXIN;

ANIMALIA; DICTYOSTELIUM; DICTYOSTELIUM DISCOIDEUM;

EID: 12144268343     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2004.153     Document Type: Article

References (40)

1. Arnér, E.S.J., and Holmgren, A. (2000). Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 267, 6102-6109.
2. Balmer, Y., and Schürmann, P. (2001). Heterodimer formation between thioredoxin f and fructose- 1,6-bisphosphatase from spinach chloroplasts. FEBS Lett. 492, 58-61.
3. 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. USA 100, 370-375.
4. 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. USA 101, 2642-2647.
5. 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. Biochemistry 13, 3418-3420.
6. Bergmeyer, H.U. (1974). Methoden der enzymatischen Analyse. 3rd Edition (Weinheim, Germany: Verlag Chemie), pp. 458-459, 1552-1554.
7. Brodegger, T. (2002). Molekularbiologische Funktionsanalysen von Thioredoxinen aus Dictyostelium discoideum. PhD thesis (Kassel, Germany: University of Kassel).
8. 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.
9. 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.
10. 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. USA 88, 9578-9582.
11. Condeelis, J. (1995). Elongation factor 1α-, translation and the cytoskeleton. Trends Biochem. Sci. 20, 169-170.
12. Dagert, M., and Ehrlich, S.D. (1979). Prolonged incubation in calcium chloride improves the competence of Escherichia coli cells. Gene 6, 23-28.
13. 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.
14. Devreotes, P., and Janetopolous, C. (2003). Eukaryotic chemotaxis: distinctions between directional sensing and polarization. J. Biol. Chem. 278, 20445-20448.
15. 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.
16. Follmann, H., and Häberlein, I. (1995). Thioredoxins: universal, yet specific thiol-disulfide redox cofactors. BioFactors 5 147-156.
17. Gietz, R.D., and Woods, R.A. (1995). Transforming yeast with DNA. Methods Mol. Cell. Biol. 5, 255-269.
18. 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.
19. 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.
20. 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.
21. Jörnvall, H. (1977). Differences between alcohol dehydrogenases. Eur. J. Biochem. 72, 443-452.
22. 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. USA 87, 2264-2268.
23. Kern, R., Malki, A., Holmgren, A., and Richarme, G. (2003). Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase. Biochem. J. 371, 965-972.
24. Kuspa, A., Dingermann, T., and Nellen, W. (1995). Analysis of gene function in Dictyostelium. Experientia 51, 1116-1123.
25. 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.
26. Maeda, Y., Inouye, K., and Takeuchi, I. (1997). Dictyostelium - A Model System for Cell and Developmental Biology (Tokyo, Japan: Universal Academy Press).
27. 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.
28. Marcus, F., and Harrsch, P.B. (1990). Amino acid sequence of chloroplast fructose-1,6-bisphosphatase. Arch. Biochem. Biophys. 279 151-157.
29. 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.
30. 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.
31. Porqué, P.G., Baldesten, A., and Reichard, P. (1970). Purification of a thioredoxin system from yeast. J. Biol. Chem. 245 2363-2370.
32. 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.
33. 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.
34. Stockmann, A. (2002). Analyse der Wechselwirkungen zwischen Thioredoxin 1 und Elongationsfaktor 1α. Diploma (MSc) thesis (Kassel, Germany: University of Kassel).
35. Villeret, V., Huang, S., Zhang, Y., Xue, Y., and Lipscomb, W.N. (1995). Crystal structure of spinach chloroplast fructose-1,6-bisphosphatase. Biochemistry 34, 4299-4306.
36. 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.
37. 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.
38. 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.
39. 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.
40. 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. Nature 347, 494-496.