The role of cysteine residues as redox-sensitive regulatory switches

Current Opinion in Structural Biology

Volumn 14, Issue 6, 2004, Pages 679-686

  Barford, David ^a  

^a INSTITUTE OF CANCER RESEARCH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; CYSTEINE; FUNGAL PROTEIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 33; HYDROGEN PEROXIDE; PEROXIDASE; PEROXIREDOXIN; PROTEIN TYROSINE PHOSPHATASE; REACTIVE OXYGEN METABOLITE; SULFENAMIDE DERIVATIVE; SULFENIC ACID DERIVATIVE; SULFONIC ACID DERIVATIVE; THIOL DERIVATIVE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR OXYR; TRANSCRIPTION FACTOR YAP 1; UNCLASSIFIED DRUG;

COVALENT BOND; DISULFIDE BOND; GENE EXPRESSION REGULATION; MOLECULAR MECHANICS; NONHUMAN; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN CONFORMATION; REVIEW; SIGNAL TRANSDUCTION;

ANIMALS; BINDING SITES; CATALYSIS; CYSTEINE; GENE EXPRESSION REGULATION; HUMANS; MODELS, BIOLOGICAL; MODELS, CHEMICAL; MODELS, MOLECULAR; OXIDATION-REDUCTION; OXIDATIVE STRESS; PROTEIN BINDING; PROTEIN CONFORMATION; SIGNAL TRANSDUCTION; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 9944235916     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2004.09.012     Document Type: Review

References (45)

1. T. Finkel Redox-dependent signal transduction FEBS Lett 476 2000 52 54
2. T. Finkel Oxidant signals and oxidative stress Curr Opin Cell Biol 15 2003 247 254
3. S.G. Rhee, Y.S. Bae, S.R. Lee, and K. Jaeyul Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation Sci STKE 2000 2000 PE1
4. M.S. Paget, and M.J. Buttner Thiol-based regulatory switches Annu Rev Genet 37 2003 91 121
5. M.B. Toledano, A. Delaunay, L. Monceau, and F. Tacnet Microbial H(2)O(2) sensors as archetypical redox signaling modules Trends Biochem Sci 29 2004 351 357
6. G. Storz, L.A. Tartaglia, and B.N. Ames Transcriptional regulator of oxidative stress-inducible genes: direct activation by oxidation Science 248 1990 189 194
7. M.B. Toledano, I. Kullik, F. Trinh, P.T. Baird, T.D. Schneider, and G. Storz Redox-dependent shift of OxyR-DNA contacts along an extended DNA-binding site: a mechanism for differential promoter selection Cell 78 1994 897 909
8. F. Aslund, M. Zheng, J. Beckwith, and G. Storz Regulation of the OxyR transcription factor by hydrogen peroxide and the cellular thiol-disulfide status Proc Natl Acad Sci USA 96 1999 6161 6165
9. I. Kullik, M.B. Toledano, L.A. Tartaglia, and G. Storz Mutational analysis of the redox-sensitive transcriptional regulator OxyR: regions important for oxidation and transcriptional activation J Bacteriol 177 1995 1275 1284
10. M. Zheng, F. Aslund, and G. Storz Activation of the OxyR transcription factor by reversible disulfide bond formation Science 279 1998 1718 1721
11. H. Choi, S. Kim, P. Mukhopadhyay, S. Cho, J. Woo, G. Storz, and S. Ryu Structural basis of the redox switch in the OxyR transcription factor Cell 105 2001 103 113
12. S.O. Kim, K. Merchant, R. Nudelman, W.F. Beyer Jr., T. Keng, J. DeAngelo, A. Hausladen, and J.S. Stamler OxyR: a molecular code for redox-related signaling Cell 109 2002 383 396
13. A. Hausladen, C.T. Privalle, T. Keng, J. DeAngelo, and J.S. Stamler Nitrosative stress: activation of the transcription factor OxyR Cell 86 1996 719 729
14. 2 receptor and redox-transducer in gene activation Cell 111 2002 471 481
15. Z.A. Wood, E. Schroder, J. Robin Harris, and L.B. Poole Structure, mechanism and regulation of peroxiredoxins Trends Biochem Sci 28 2003 32 40
16. H.H. Jang, K.O. Lee, Y.H. Chi, B.G. Jung, S.K. Park, J.H. Park, J.R. Lee, S.S. Lee, J.C. Moon, and J.W. Yun Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function Cell 117 2004 625 635 The authors report the conversion of PrxI and PrxII from peroxidase activity to a molecular chaperone, accompanied by oxidation of the peroxidate cysteine residue and concomitant oligomerisation.
17. 2) at the catalytic site of a peroxiredoxin to a free thiol.
18. J.L. Martin Thioredoxin-a fold for all reasons Structure 3 1995 245 250
19. Z.A. Wood, L.B. Poole, and P.A. Karplus Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling Science 300 2003 650 653
20. U. Jakob, W. Muse, M. Eser, and J.C. Bardwell Chaperone activity with a redox switch Cell 96 1999 341 352
21. U. Jakob, M. Eser, and J.C. Bardwell Redox switch of hsp33 has a novel zinc-binding motif J Biol Chem 275 2000 38302 38310
22. J. Vijayalakshmi, M.K. Mukhergee, J. Graumann, U. Jakob, and M.A. Saper The 2.2 Å crystal structure of Hsp33: a heat shock protein with redox-regulated chaperone activity Structure 9 2001 367 375
23. S. Barbirz, U. Jakob, and M.O. Glocker Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone J Biol Chem 275 2000 18759 18766
24. J. Graumann, H. Lilie, X. Tang, K.A. Tucker, J.H. Hoffmann, J. Vijayalakshmi, M.A. Saper, C.A. Bardwell, and U. Jakob Activation of the redox-regulated molecular chaperone Hsp33-a two-step mechanism Structure (Camb) 9 2001 377 387
25. P.C. Graf, M. Martinez-Yamout, S. VanHaerents, H. Lilie, H.J. Dyson, and U. Jakob Activation of the redox-regulated chaperone Hsp33 by domain unfolding J Biol Chem 279 2004 20529 20538
26. B. Raman, L.V. Siva Kumar, T. Ramakrishna, and C. Mohan Rao Redox-regulated chaperone function and conformational changes of Escherichia coli Hsp33 FEBS Lett 489 2001 19 24
27. S.G. Ahn, and D.J. Thiele Redox regulation of mammalian heat shock factor 1 is essential for Hsp gene activation and protection from stress Genes Dev 17 2003 516 528
28. Salmeen A, Barford D: Functions and mechanisms of redox regulation of cysteine-based phosphatases. Antioxid Redox Signal 2004, in press.
29. M.P. Czech, J.C. Lawrence Jr., and W.S. Lynn Evidence for the involvement of sulfhydryl oxidation in the regulation of fat cell hexose transport by insulin Proc Natl Acad Sci USA 71 1974 4173 4177
30. J.M. Denu, and K.G. Tanner Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation Biochemistry 37 1998 5633 5642
31. Y.S. Bae, S.W. Kang, M.S. Seo, I.C. Baines, E. Tekle, P.B. Chock, and S.G. Rhee Epidermal growth factor (EGF)-induced generation of hydrogen peroxide J Biol Chem 272 1997 217 221
32. K. Mahadev, A. Zilbering, L. Zhu, and B.J. Goldstein Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade J Biol Chem 276 2001 21938 21942
33. T.C. Meng, T. Fukada, and N.K. Tonks Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo Mol Cell 9 2002 387 399
34. T.C. Meng, D.A. Buckley, S. Galic, T. Tiganis, and N.K. Tonks Regulation of insulin signaling through reversible oxidation of the protein tyrosine phosphatases TC45 and PTP1B J Biol Chem 279 2004 37716 37725
35. 2, accompanied by conformational changes of the catalytic site. The authors show that this is reversed by thiols and provide evidence of its occurrence in solution.
36. R.L. van Montfort, M. Congreve, D. Tisi, R. Carr, and H. Jhoti Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B Nature 423 2003 773 777 The oxidation-dependent formation of a cyclic sulfenamide bond at the catalytic site of PTP1B is described.
37. Z. Jia, D. Barford, A.J. Flint, and N.K. Tonks Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B Science 268 1995 1754 1758
38. C. Blanchetot, L.G. Tertoolen, and J. den Hertog Regulation of receptor protein-tyrosine phosphatase alpha by oxidative stress EMBO J 21 2002 493 503
39. A. Alonso, J. Sasin, N. Bottini, I. Friedberg, A. Osterman, A. Godzik, T. Hunter, J. Dixon, and T. Mustelin Protein tyrosine phosphatases in the human genome Cell 117 2004 699 711
40. E.B. Fauman, J.P. Cogswell, B. Lovejoy, W.J. Rocque, W. Holmes, V.G. Montana, H. Piwnica-Worms, M.J. Rink, and M.A. Saper Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A Cell 93 1998 617 625
41. R.A. Reynolds, A.W. Yem, C.L. Wolfe, M.R. Deibel Jr., C.G. Chidester, and K.D. Watenpaugh Crystal structure of the catalytic subunit of Cdc25B required for G2/M phase transition of the cell cycle J Mol Biol 293 1999 559 568
42. P. Chiarugi, T. Fiaschi, M.L. Taddei, D. Talini, E. Giannoni, G. Raugei, and G. Ramponi Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation J Biol Chem 276 2001 33478 33487
43. 2 J Biol Chem 273 1998 32554 32560
44. M.W. Foster, T.J. McMahon, and J.S. Stamler S-nitrosylation in health and disease Trends Mol Med 9 2003 160 168
45. M.J. Wood, G. Storz, and N. Tjandra Structural basis for redox regulation of Yap1 transcription factor localization Nature 430 2004 917 921