Redox regulation of c-Jun DNA binding by reversible S-glutathiolation

FASEB Journal

Volumn 13, Issue 12, 1999, Pages 1481-1490

  Klatt, Peter ^a   Molina, Estela Pineda ^a   De Lacoba, Mario García ^a   Padilla, C Alicia ^b   Martínez Galisteo, Emilia ^b   Bárcena, J Antonio ^b   Lamas, Santiago ^a  

^a CENTRO DE INVESTIGACIONES BIOLÓGICAS   (Spain)

^b UNIVERSITY OF CÓRDOBA   (Spain)

Author keywords

Glutathione; Redox regulation; S; Thiolation; Transcription factor

Indexed keywords

CYSTEINE; GLUTATHIONE; TRANSCRIPTION FACTOR;

ARTICLE; BINDING SITE; DISULFIDE BOND; DNA BINDING; MOLECULAR MODEL; NUCLEOTIDE SEQUENCE; OXIDATION; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; REGULATORY MECHANISM;

EID: 0032826055     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.13.12.1481     Document Type: Article

References (38)

1. Meister, A., and Anderson, M. E. (1983) Glutathione. Annu. Rev. Biochem. 52, 711-760
2. Gilbert, H. F. (1995) Thiol/disulfide exchange equilibria and disulfide bond stability. Methods Enzymol. 251, 8-28
3. Thomas, J. A., Poland, B., and Honzatko, R. (1995) Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation. Arch. Biochem. Biophys. 319, 1-9
4. Cotgreave, I. A., and Gerdes, R. G. (1998) Recent trends in glutathione biochemistry - glutathione-protein interactions: a molecular link between oxidative stress and cell proliferation. Biochem. Biophys. Res. Commun. 242, 1-9
5. Sun, Y., and Oberley, L. W. (1996) Redox regulation of transcriptional activators. Free Rad. Biol. Med. 21, 335-348
6. Sen, C. K., and Packer, L. (1996) Antioxidant and redox regulation of gene transcription. FASEB J. 10, 709-720
7. Nakamura, H., Nakamura, K., and Yodoi, J. (1997) Redox regulation of cellular activation. Annu. Rev. Immunol. 15, 351-369
8. Glover, J. N. M., and Harrison, S. C. (1995) Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA. Nature (London) 373, 257-261
9. Abate, C., Patel, L., Rauscher, F.J., and Curran, T. (1990) Redox regulation of Fos and Jun DNA-binding activity in vitro. Science 249, 1157-1161
10. Oehler, T., Pintzas, A., Stumm, S., Darling, A., Gillespie, D., and Angel, P. (1993) Mutation of a phosphorylation site in the DNA-binding domain is required for redox-independent transactivation of AP1-dependent genes by v-jun. Oncogene 8, 1141-1147
11. Bannister, A. J., Cook, A., and Kouzarides, T. (1991) In vitro DNA binding activity of Fos/Jun and BZLF1 but not C/EBP is affected by redox changes. Oncogene 6, 1243-1250
12. Holmgren, A., and Bjornstedt, M. (1995) Thioredoxin and thioredoxin reductase. Methods Enzymol. 252, 199-208
13. Padilla, C. A., Spyrou, G., and Holmgren, A. (1996) High-level expression of fully active human glutaredoxin (thioltransferase) in E. coli and characterization of Cys7 to Ser mutant protein. FEBS Lett. 378, 69-73
14. Pajares, M. A., Durán, C., Corrales, F., Pliego, M. M., and Mato, J. M. (1992) Modulation of rat liver S-adenosylmethionine synthetase activity by glutathione. J. Biol. Chem. 267, 17598-17605
15. Ellman, G. L. (1959) Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82, 70-77
16. Gergel, D., and Cederbaum, A. I. (1996) Inhibition of the catalytic activity of alcohol dehydrogenase by nitric oxide is associated with S-nitrosylation and the release of zinc. Biochemistry 35, 16186-16194
17. Sies, H., and Summer, K.-H. (1975) Hydroperoxide-metabolizing systems in rat liver. Eur. J. Biochem. 57, 503-512
18. Xanthoudakis, S., and Curran, T. (1994) Analysis of c-Fos and c-Jun redox-dependent DNA binding activity. Methods Enzymol. 234, 163-175
19. Luthman, M., and Holmgren, A. (1982) Glutaredoxin from calf thymus. Purification to homogeneity. J. Biol. Chem. 257, 6686-6690
20. Holmgren, A. (1979) Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J. Biol. Chem. 254, 9627-9632
21. Junius, F. K., O'Donoghue, S. I., Nilges, M., Weiss, A. S., and King, G. F. (1996) High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer. J. Biol. Chem. 271, 13663-13667
22. Weiner, S. J., Kollman, P. A., Nguyen, D. T., and Case, D. A. (1986) An all atom force field for simulations of proteins and nucleic acids. J. Camp. Chem. 7, 230-246
23. Tietze, F. (1969) Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal. Biochem. 27, 502-522
24. Gilbert, H. F. (1984) Redox control of enzyme activities by thiol/disulfide exchange. Methods Enzymol. 107, 330-351
25. Ziegler, D. M. (1985) Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation. Annu. Rev. Biochem. 54, 305-329
26. Figueiredo Pereira, M. E., Yakushin, S., and Cohen, G. (1998) Disruption of the intracellular sulfhydryl homeostasis by cadmium-induced oxidative stress leads to protein thiolation and ubiquitination in neuronal cells. J. Biol. Chem. 273, 12703-12709
27. Jahngen-Hodge, J., Obin, M. S., Gong, X., Shang, F., Nowell, T. R., Gong, J., Abasi, H., Blumberg, J., and Taylor, A. (1997) Regulation of ubiquitin-conjugating enzymes by glutathione following oxidative stress. J. Biol. Chem. 272, 28218-28226
28. Bandyopadhyay, S., Starke, D. W., Mieyal, J. J., and Gronostajski, R. M. (1998) Thioltransferase (glutaredoxin) reactivates the DNA-binding activity of oxidation-inactivated nuclear factor 1. J. Biol. Chem. 273, 392-397
29. Jung, C. H., and Thomas, J. A. (1996) S-glutathiolated hepatocyte proteins and insulin disulfides as substrates for reduction by glutaredoxin, thioredoxin, protein disulfide isomerase and glutathione. Arch. Biochem. Biophys. 335, 61-72
30. Nikitovic, D., Holmgren, A., and Spyrou, G. (1998) Inhibition of AP-1 DNA binding by nitric oxide involving conserved cysteine residues in Jun and Fos. Biochem. Biophys. Res. Commun. 242, 109-112
31. Xanthoudakis, S., Miao, G., Wang, F., Pan, Y.-C. E., and Curran, T. (1992) Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. EMBO J. 11, 3323-3335
32. Hirota, H., Matsui, M., Iwata, S., Nishiyama, A., Mori, K., and Yodoi, J. (1997) AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1. Proc. Natl. Acad. Sci. USA 94, 3633-3638
33. Chai, Y.-C., Ashraf, S. S., Rokutan, K., Johnston, R. B., and Thomas, J. A. (1994) S-Thiolation of individual human neutrophil proteins including actin by stimulation of the respiratory burst: evidence against a role for glutathione disulfide. Arch. Biochem. Biophys. 310, 273-281
34. Chai, Y.-C., Hendrich, S., and Thomas, J. A. (1994) Protein S-thiolation in hepatocytes stimulated by t-butyl hydroperoxide, menadione, and neutrophils. Arch. Biochem. Biophys. 310, 264-272
35. Dirr, H., Reinemer, P., and Huber, R. (1994) X-ray crystal structures of cytosolic glutathione S-transferases - implications for protein architecture, substrate recognition, and catalytic function. Eur. J. Biochem. 220, 645-661
36. Bushweller, J. H., Billeter, M., Holmgren, A., and Wüthrich, K. (1997) The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin (C14S) and glutathione. J. Mol. Biol. 235, 1585-1597
37. Epp, O., Ladenstein, R., and Wendel, A. (1983) The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution. Eur. J. Biochem. 133, 51-69
38. Davis, D. A., Newcomb, F. M., Starke, D. W., Ott, D. E., Mieyal, J. J., and Yarchoan, R. (1997) Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro. J. Biol. Chem. 272, 25935-25940