Not every disulfide lasts forever: Disulfide bond formation as a redox switch

Antioxidants and Redox Signaling

Volumn 5, Issue 4, 2003, Pages 425-434

  Linke, Katrin ^a   Jakob, Ursula ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; CHAPERONE; DISULFIDE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 33; PROTEIN RSRA; REACTIVE OXYGEN METABOLITE; SIGMA FACTOR; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR OXYR; TRANSCRIPTION FACTOR YAP1; UNCLASSIFIED DRUG;

BINDING AFFINITY; CELL COMPARTMENTALIZATION; CELLULAR DISTRIBUTION; CHEMICAL BINDING; CYTOSOL; ENVIRONMENTAL FACTOR; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN BINDING; REVIEW;

EID: 0042763566     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/152308603768295168     Document Type: Review

References (74)

1. Aliev G, Smith MA, Seyidov D, Neal ML, Lamb BT, Nunomura A, Gasimov EK, Vinters HV, Perry G, LaManna JC, and Friedland RP. The role of oxidative stress in the pathophysiology of cerebrovascular lesions in Alzheimer's disease. Brain Pathol 12: 21-35, 2002.
2. Aslund F and Beckwith J. Bridge over troubled waters: sensing stress by disulfide bond formation. Cell 96: 751-753, 1999.
3. Aslund F, Zheng M, Beckwith J, and Storz G. Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status. Proc Natl Acad Sci USA 96: 6161-6165, 1999.
4. Barbirz S, Jakob U, and Glocker MO. Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone. J Biol Chem 275: 18759-18766, 2000.
5. Berlett BS and Stadtman ER. Protein oxidation in aging, disease, and oxidative stress. J Biol Chem 272: 20313-20316, 1997.
6. Carmel-Harel O and Storz G. Roles of the glutathione- and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress. Annu Rev Microbiol 54: 439-461, 2000.
7. Choi H, Kim S, Mukhopadhyay P, Cho S, Woo J, Storz G, and Ryu S. Structural basis of the redox switch in the OxyR transcription factor. Cell 105: 103-113, 2001.
8. Christman MF, Storz G, and Ames BN. OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins. Proc Natl Acad Sci USA 86: 3484-3488, 1989.
9. Claiborne A, Yeh JI, Mallett TC, Luba J, Crane EJ 3rd, Charrier V, and Parsonage D. Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation. Biochemistry 38: 15407-15416, 1999.
10. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Bartell BG, et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence Nature 393: 537-544, 1998.
11. Coleman ST, Epping EA, Steggerda SM, and Moye-Rowley WS. Yap1p activates gene transcription in an oxidant-specific fashion. Mol Cell Biol 19: 8302-8313, 1999.
12. Collet JF and Bardwell JC. Oxidative protein folding in bacteria. Mol Microbiol 44: 1-8, 2002.
13. Darby N and Creighton TE. Disulfide bonds in protein folding and stability. Methods Mol Biol 40: 219-252, 1995.
14. 2 sensing through oxidation of the Yap1 transcription factor. EMBO J 19: 5157-5166, 2000.
15. 2 receptor and redox-transducer in gene activation. Cell 111: 471-481, 2002.
16. Finkel T and Holbrook NJ. Oxidants, oxidative stress and the biology of ageing. Nature 408: 239-247, 2000.
17. Frand AR and Kaiser CA. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol Cell 4: 469-477, 1999.
18. Fuangthong M and Helmann JD. The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative. Proc Natl Acad Sci USA 99: 6690-6695, 2002.
19. Gasch AP, Spellman PT, Kao CM, Carmel-Harel O, Eisen MB, Storz G, Botstein D, and Brown PO. Genomic expression programs in the response of yeast cells to environmental changes. Mol Biol Cell 11: 4241-4757, 2000.
20. Gilbert HF. Molecular and cellular aspects of thioldisulfide exchange. Adv Enzymol Relat Areas Mol Biol 63: 69-172, 1990.
21. 2 stimulon in Saccharomyces cerevisiae. J Biol Chem 273: 22480-22489, 1998.
22. Graf PCF and Jakob U. Redox regulated molecular chaperones. Cell Mol Life Sci 59: 1624-1631, 2002.
23. Graumann J, Lilie H, Tang X, Tucker KA, Hoffmann JH, Vijayalakshmi J, Saper M, Bardwell JC, and Jakob U. Activation of the redox-regulated molecular chaperone Hsp33 - a two-step mechanism. Structure (Camb) 9: 377-387, 2001.
24. Hausladen A, Privalle CT, Keng T, DeAngelo J, and Stamler JS. Nitrosative stress: activation of the transcription factor OxyR. Cell 86: 719-729, 1996.
25. Hightower KE and Fierke CA. Zinc-catalyzed sulfur alkyation: insights from protein farnesyltransferase. Curr Opin Chem Biol 3: 176-181, 1999.
26. Hirata D, Yano K, and Miyakawa T. Stress-induced transcriptional activation mediated by YAP1 and YAP2 genes that encode the Jun family of transcriptional activators in Saccharomyces cerevisiae. Mol Gen Genet 242: 250-256, 1994.
27. Hoyos B, Imam A, Korichneva I, Levi E, Chua R, and Hammerling U. Activation of c-Raf kinase by ultraviolet light. Regulation by retinoids. J Biol Chem 277: 23949-23957, 2002.
28. Humphries KM, Juliano C, and Taylor SS. Regulation of cAMP-dependent protein kinase activity by glutathionylation. J Biol Chem 277: 43505-43511, 2002.
29. Jacob C, Maret W, and Vallee BL. Control of zinc transfer between thionein, metallothionein, and zinc proteins. Proc Natl Acad Sci USA 95: 3489-3494, 1998.
30. Jakob U, Muse W, Eser M, and Bardwell JC. Chaperone activity with a redox switch. Cell 96: 341-352, 1999.
31. Jakob U, Eser M, and Bardwell JC. Redox switch of hsp33 has a novel zinc-binding motif. J Biol Chem 275: 38302-38310, 2000.
32. Kang JG, Paget MS, Seok YJ, Hahn MY, Bae JB, Hahn JS, Kleanthous C, Buttner MJ, and Roe JH. RsrA, an anti-sigma factor regulated by redox change. EMBO J 18: 4292-4298, 1999.
33. Kim SJ, Jeong DG, Chi SW, Lee JS, and Ryu SE. Crystal structure of proteolytic fragments of the redox-sensitive Hsp33 with constitutive chaperone activity. Nat Struct Biol 8: 459-466, 2001.
34. Kim SO, Merchant K, Nudelman R, Beyer WF Jr, Keng T, DeAngelo J, Hausladen A, and Stamler JS. OxyR: a molecular code for redox-related signaling. Cell 109: 383-396, 2002.
35. Knapp LT and Klann E. Superoxide-induced stimulation of protein kinase C via thiol modification and modulation of zinc content. J Biol Chem 275: 24136-24145, 2000.
36. Kosower NS and Kosower EM. Diamide: an oxidant probe for thiols. Methods Enzymol 251: 123-133, 1995.
37. Kovacic P and Jacintho JD. Mechanisms of carcinogenesis: focus on oxidative stress and electron transfer. Curr Med Chem 8: 773-796, 2001.
38. Kuge S, Jones N, and Nomoto A. Regulation of yAP-1 nuclear localization in response to oxidative stress. EMBO J 16:1710-1720, 1997.
39. Kuge S, Toda T, Iizuka N, and Nomoto A. Crm1 (XpoI) dependent nuclear export of the budding yeast transcription factor yAP-1 is sensitive to oxidative stress. Genes Cells 3: 521-532, 1998.
40. Kuge S, Arita M, Murayama A, Maeta K, Izawa S, Inoue Y, and Nomoto A. Regulation of the yeast Yap1p nuclear export signal is mediated by redox signal-induced reversible disulfide bond formation. Mol Cell Biol 21: 6139-6150, 2001.
41. Kullik I, Stevens J, Toledano MB, and Storz G. Mutational analysis of the redox-sensitive transcriptional regulator OxyR: regions important for DNA binding and multimerization. J Bacteriol 177: 1285-1291, 1995.
42. Kullik I, Toledano MB, Tartaglia LA, and Storz G. Mutational analysis of the redox-sensitive transcriptional regulator OxyR: regions important for oxidation and transcriptional activation. J Bacteriol 177: 1275-1284, 1995.
43. Kunst F, Ogasawara N, Moszer I, Albertini AM, Alloni G, Azevedo V, Bertero MG, Bessieres P, Bolotin A, Borchert S, Borriss R, Boursier L, Brans A, Braun M, Brignell SC, Bron S, Brouillet S, Bruschi CV, Caldwell B, Capuano V, Carter NM, Choi SK, Codani JJ, Connerton IF, Danchin A, et al. The complete genome sequence of the gram-positive bacterium Bacillus subtilis. Nature 390: 249-256, 1997.
44. Lee J, Godon C, Lagniel G, Spector D, Garin J, Labarre J, and Toledano MB, Yap1 and Skn7 control two specialized oxidative stress response regulons in yeast. J Biol Chem 274: 16040-16046, 1999.
45. Martindale JL and Holbrook NJ. Cellular response to oxidative stress: signaling for suicide and survival. J Cell Physiol 192: 1-15, 2002.
46. Maynard AT and Covell DG. Reactivity of zinc finger cores: analysis of protein packing and electrostatic screening. J Am Chem Soc 123: 1047-1058, 2001.
47. Miller R and Britigan B. Role of oxidants in microbial pathophysiology. Clin Microbiol Rev 10: 1-18, 1997.
48. Newman JD, Falkowski MJ, Schilke BA, Anthony LC, and Donohue TJ. The Rhodobacter sphaeroides ECF sigma factor, sigma(E), and the target promoters cycA P3 and rpoE P1. J Mol Biol 294: 307-320, 1999.
49. Ortenberg R and Beckwith J. Functions of thiol-disulfide oxidoreductases in E. coli: redox myths, realities, and practicalities. Antioxid Redox Signal 5: 403-411, 2003.
50. Paget MS, Kang JG, Roe JH, and Buttner MJ. sigmaR, an RNA polymerase sigma factor that modulates expression of the thioredoxin system in response to oxidative stress in Streptomyces coelicolor A3(2). EMBO J 17: 5776-5782, 1998.
51. Paget MS, Bae JB, Hahn MY, Li W, Kleanthous C, Roe JH, and Buttner MJ. Mutational analysis of RsrA, a zinc-binding anti-sigma factor with a thiol-disulphide redox switch. Mol Microbiol 39: 1036-1047, 2001.
52. Paget MS, Molle V, Cohen G, Aharonowitz Y, and Buttner MJ. Defining the disulphide stress response in Streptomyces coelicolor A3 (2): identification of the sigmaR regulon. Mol Microbiol 42: 1007-1020, 2001.
53. Pomposiello PJ and Demple B. Redox-operated genetic switches: the SoxR and OxyR transcription factors. Trends Biotechnol 19: 109-114, 2001.
54. Raman B, Siva Kumar LV, Ramakrishna T, and Mohan Rao C. Redox-regulated chaperone function and conformational changes of Escherichia coli Hsp33. FEBS Lett 489: 19-24, 2001.
55. Richmond CS, Glasner JD, Mau R, Jin H, and Blattner FR. Genome-wide expression profiling in Escherichia coli K-12. Nucleic Acids Res 27: 3821-3835, 1999.
56. Ritz D and Beckwith J. Roles of thiol-redox pathways in bacteria. Annu Rev Microbiol 55: 21-48, 2001.
57. Schnell N, Krems B, and Entian KD. The PAR1 (YAP1/ SNQ3) gene of Saccharomyces cerevisiae, a c-jun homologue, is involved in oxygen metabolism. Curr Genet 21: 269-273, 1992.
58. Scott C and Green J. Miscoordination of the iron-sulfur clusters of the anaerobic transcription factor, FNR, allows simple repression but not activation. J Biol Chem 277: 1749-1754, 2002.
59. Sies H. Role of reactive oxygen species in biological processes. Klin Wochenschr 69: 965-968, 1991.
60. Snyder GH, Cennerazzo MJ, Karalis AJ, and Field D. Electrostatic influence of local cysteine environments on disulfide exchange kinetics. Biochemistry 20: 6509-6519, 1981.
61. Stewart EJ, Aslund F, and Beckwith J. Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins. EMBO J 17: 5543-5550, 1998.
62. Storz G and Imlay JA. Oxidative stress. Curr Opin Microbiol 2: 188-194, 1999.
63. Storz G and Tartaglia LA. OxyR: a regulator of antioxidant genes. J Nutr 122: 627-630, 1992.
64. Sutton HC and Winterbourn CC. On the participation of higher oxidation states of iron and copper in Fenton reactions. Free Radic Biol Med 6: 53-60, 1989.
65. Toledano MB, Kullik I, Trinh F, Baird PT, Schneider TD, and Storz G. Redox-dependent shift of OxyR-DNA contacts along an extended DNA-binding site: a mechanism for differential promoter selection. Cell 78: 897-909, 1994.
66. Toone WM, Morgan BA, and Jones N. Redox control of AP-1-like factors in yeast and beyond. Oncogene 20: 2336-2346, 2001.
67. Vijayalakshmi J, Mukhergee MK, Graumann J, Jakob U, and Saper MA. The 2. 2 A crystal structure of Hsp33: a heat shock protein with redox-regulated chaperone activity. Structure (Camb) 9: 367-375, 2001.
68. Webster KA, Prentice H, and Bishopric NH. Oxidation of zinc finger transcription factors: physiological consequences. Antioxid Redox Signal 3: 535-548, 2001.
69. Wedemeyer WJ, Welker E, Narayan M, and Scheraga HA. Disulfide bonds and protein folding. Biochemistry 39: 4207-4216, 2000.
70. Wilcox DE, Schenk AD, Feldman BM, and Xu Y. Oxidation of zinc-binding cysteine residues in transcription factor proteins. Antioxid Redox Signal 3: 549-564, 2001.
71. Zander T, Phadke ND, and Bardwell JC. Disulfide bond catalysts in Escherichia coli. Methods Enzymol 290: 59-74, 1998.
72. Zheng M and Storz G. Redox sensing by prokaryotic transcription factors. Biochem Pharmacol 59: 1-6, 2000.
73. Zheng M, Aslund F, and Storz G. Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279: 1718-1721, 1998.
74. Zheng M, Wang X, Templeton LJ, Smulski DR, LaRossa RA, and Storz G. DNA microarray-mediated transcriptional profiling of the Escherichia coli response to hydrogen peroxide. J Bacteriol 183: 4562-4570, 2001.