Use of Dimedone-Based Chemical Probes for Sulfenic Acid Detection: Methods to Visualize and Identify Labeled Proteins

Methods in Enzymology

Volumn 473, Issue , 2010, Pages 95-115

  Nelson, Kimberly J ^a   Klomsiri, Chananat ^a   Codreanu, Simona G ^b   Soito, Laura ^a   Liebler, Daniel C ^b   Rogers, LeAnn C ^a   Daniel, Larry W ^a   Poole, Leslie B ^a  

^a WAKE FOREST SCHOOL OF MEDICINE   (United States)

^b VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

5,5 DIMETHYL 1,3 CYCLOHEXANEDIONE; CYCLOHEXANONE DERIVATIVE; PROTEIN; SULFENIC ACID DERIVATIVE;

ANIMAL; BIOTINYLATION; CHEMISTRY; HUMAN; MASS SPECTROMETRY; METHODOLOGY; PROTEIN PROCESSING; REVIEW; STAINING;

ANIMALS; BIOTINYLATION; CYCLOHEXANONES; HUMANS; MASS SPECTROMETRY; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEINS; STAINING AND LABELING; SULFENIC ACIDS;

EID: 77956210622     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/S0076-6879(10)73004-4     Document Type: Chapter

References (33)

1. Chen, C.H., Cheng, T.H., Lin, H., Shih, N.L., Chen, Y.L., Chen, Y.S., Cheng, C.F., Lian, W.S., Meng, T.C., Chiu, W.T., Chen, J.J., Reactive oxygen species generation is involved in epidermal growth factor receptor transactivation through the transient oxidization of Src homology 2-containing tyrosine phosphatase in endothelin-1 signaling pathway in rat cardiac fibroblasts. Mol. Pharmacol. 69 (2006), 1347–1355.
2. Claiborne, A., Yeh, J.I., Mallett, T.C., Luba, J., Crane, E.J. 3rd, Charrier, V., Parsonage, D., Protein-sulfenic acids: Diverse roles for an unlikely player in enzyme catalysis and redox regulation. Biochemistry 38 (1999), 15407–15416.
3. Cotgreave, I.A., Gerdes, R., Schuppe-Koistinen, I., Lind, C., S-glutathionylation of glyceraldehyde-3-phosphate dehydrogenase: Role of thiol oxidation and catalysis by glutaredoxin. Methods Enzymol. 348 (2002), 175–182.
4. Dennehy, M.K., Richards, K.A., Wernke, G.R., Shyr, Y., Liebler, D.C., Cytosolic and nuclear protein targets of thiol-reactive electrophiles. Chem. Res. Toxicol. 19 (2006), 20–29.
5. Fuangthong, M., Helmann, J.D., The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative. Proc. Natl. Acad. Sci. USA 99 (2002), 6690–6695.
6. Hondorp, E.R., Matthews, R.G., Oxidative stress inactivates cobalamin-independent methionine synthase (MetE) in Escherichia coli. PLoS Biol., 2, 2004, e336.
7. Hong, M., Fuangthong, M., Helmann, J.D., Brennan, R.G., Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family. Mol. Cell 20 (2005), 131–141.
8. Hoppe, G., Chai, Y.C., Crabb, J.W., Sears, J., Protein s-glutathionylation in retinal pigment epithelium converts heat shock protein 70 to an active chaperone. Exp. Eye Res. 78 (2004), 1085–1092.
9. Jakob, U., Muse, W., Eser, M., Bardwell, J.C., Chaperone activity with a redox switch. Cell 96 (1999), 341–352.
10. Jones, D.P., Disruption of mitochondrial redox circuitry in oxidative stress. Chem. Biol. Interact. 163 (2006), 38–53.
11. Kang, J.G., Paget, M.S., Seok, Y.J., Hahn, M.Y., Bae, J.B., Hahn, J.S., Kleanthous, C., Buttner, M.J., Roe, J.H., RsrA, an anti-sigma factor regulated by redox change. EMBO J. 18 (1999), 4292–4298.
12. Klomsiri, C., Nelson, K.J., Bechtold, E., Soito, L., Johnson, L.C., Todd Lowther, W., Seong-Eon Ryu, S., King, B., Furdui, C.M., Poole, L.B., Use of dimedone-based chemical probes for sulfenic acid detection. Evaluation of conditions affecting probe incorporation into redox-sensitive proteins. Methods Enzymol. 473 (2010), 77–93.
13. Kuge, S., Arita, M., Murayama, A., Maeta, K., Izawa, S., Inoue, Y., Nomoto, A., Regulation of the yeast Yap1p nuclear export signal is mediated by redox signal-induced reversible disulfide bond formation. Mol. Cell Biol. 21 (2001), 6139–6150.
14. Kwon, J., Lee, S.R., Yang, K.S., Ahn, Y., Kim, Y.J., Stadtman, E.R., Rhee, S.G., Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors. Proc. Natl. Acad. Sci USA 101 (2004), 16419–16424.
15. Kwon, J., Qu, C.K., Maeng, J.S., Falahati, R., Lee, C., Williams, M.S., Receptor-stimulated oxidation of SHP-2 promotes T-cell adhesion through SLP-76-ADAP. EMBO J. 24 (2005), 2331–2341.
16. Lee, S.R., Yang, K.S., Kwon, J., Lee, C., Jeong, W., Rhee, S.G., Reversible inactivation of the tumor suppressor PTEN by H2O2. J. Biol. Chem. 277 (2002), 20336–20342.
17. Leonard, S.E., Reddie, K.G., Carroll, K.S., Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells. ACS Chem. Biol. 4 (2009), 783–799.
18. Meng, T.C., Fukada, T., Tonks, N.K., Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol. Cell 9 (2002), 387–399.
19. a values for the bacterial peroxiredoxin AhpC. Biochemistry 47 (2008), 12860–12868.
20. Panmanee, W., Vattanaviboon, P., Poole, L.B., Mongkolsuk, S., Novel organic hydroperoxide-sensing and responding mechanisms for OhrR, a major bacterial sensor and regulator of organic hydroperoxide stress. J. Bacteriol. 188 (2006), 1389–1395.
21. Poole, L.B., Ellis, H.R., Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins. Biochemistry 35 (1996), 56–64.
22. Poole, L.B., Nelson, K.J., Discovering mechanisms of signaling-mediated cysteine oxidation. Curr. Opin. Chem. Biol. 12 (2008), 18–24.
23. Poole, L.B., Karplus, P.A., Claiborne, A., Protein sulfenic acids in redox signaling. Annu. Rev. Pharmacol. Toxicol. 44 (2004), 325–347.
24. Poole, L.B., Klomsiri, C., Knaggs, S.A., Furdui, C.M., Nelson, K.J., Thomas, M.J., Fetrow, J.S., Daniel, L.W., King, S.B., Fluorescent and affinity-based tools to detect cysteine sulfenic acid formation in proteins. Bioconjug. Chem. 18 (2007), 2004–2017.
25. Rainwater, R., Parks, D., Anderson, M.E., Tegtmeyer, P., Mann, K., Role of cysteine residues in regulation of p53 function. Mol. Cell Biol. 15 (1995), 3892–3903.
26. Reddie, K.G., Seo, Y.H., Muse Iii, W.B., Leonard, S.E., Carroll, K.S., A chemical approach for detecting sulfenic acid-modified proteins in living cells. Mol. Biosyst. 4 (2008), 521–531.
27. Schmalhausen, E.V., Nagradova, N.K., Boschi-Muller, S., Branlant, G., Muronetz, V.I., Mildly oxidized GAPDH: the coupling of the dehydrogenase and acyl phosphatase activities. FEBS Lett. 452 (1999), 219–222.
28. Schneider, C., Pratt, D.A., Porter, N.A., Brash, A.R., Control of oxygenation in lipoxygenase and cyclooxygenase catalysis. Chem. Biol. 14 (2007), 473–488.
29. Shevchenko, A., Tomas, H., Havlis, J., Olsen, J.V., Mann, M., In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1 (2006), 2856–2860.
30. Shin, N.Y., Liu, Q., Stamer, S.L., Liebler, D.C., Protein targets of reactive electrophiles in human liver microsomes. Chem. Res. Toxicol. 20 (2007), 859–867.
31. Thomas, S.R., Witting, P.K., Drummond, G.R., Redox control of endothelial function and dysfunction: molecular mechanisms and therapeutic opportunities. Antioxid. Redox Signal. 10 (2008), 1713–1765.
32. Tonks, N.K., Redox redux: Revisiting PTPs and the control of cell signaling. Cell 121 (2005), 667–670.
33. Zheng, M., Aslund, F., Storz, G., Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 279 (1998), 1718–1721.