Identification of tyrosine 79 in the tocopherol binding site of glutathione S-transferase Pi

Biochemistry

Volumn 45, Issue 41, 2006, Pages 12491-12499

  Ralat, Luis A ^a   Colman, Roberta F ^a  

^a UNIVERSITY OF DELAWARE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING ENERGY; CONCENTRATION (PROCESS); CRYSTAL STRUCTURE; ENZYMES; HYDROPHOBICITY;

ALPHA-TOCOPHEROL; GLUTATHIONE S-TRANSFERASE; REACTIVE ANALOGUE;

VITAMINS;

ALANINE; ALPHA TOCOPHEROL; AMINO ACID; GLUTATHIONE DERIVATIVE; GLUTATHIONE TRANSFERASE; LIGAND; PHENYLALANINE; SERINE; TOCOPHEROL; TOCOPHEROL IODOACETATE; TYROSINE; UNCLASSIFIED DRUG;

AFFINITY LABELING; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME SUBSTRATE COMPLEX; ENZYME SUBUNIT; HYDROPHOBICITY; NONLINEAR SYSTEM; PRIORITY JOURNAL; PROTEIN ISOLATION;

ALPHA-TOCOPHEROL; AMINO ACID SUBSTITUTION; BASE SEQUENCE; BINDING SITES; DNA, COMPLEMENTARY; GLUTATHIONE S-TRANSFERASE PI; HUMANS; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; TOCOPHEROLS; TYROSINE;

KOBUS;

EID: 33750073812     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061330k     Document Type: Article

References (48)

1. Armstrong, R. N. (1997) Structure, catalytic mechanism, and evolution of the glutathione transferases, Chem. Res. Toxicol. 10, 2-18.
2. Mannervik, B., and Danielson, U. H. (1988) Glutathione transferases-structure and catalytic activity, CRC Crit. Rev. Biochem. 23, 283-337.
3. Coles, B., and Ketterer, B. (1990) The role of glutathione and glutathione transferases in chemical carcinogenesis, Crit. Rev. Biochem. Mol. Biol. 25, 47-70.
4. Mannervik, B., Board, P. G., Hayes, J. D., Listowsky, I., and Pearson, W. R. (2005) Nomenclature for mammalian soluble glutathione transferases, Methods Enzymol. 401, 1-8.
5. Board, P. G., Coggan, M., Chelvanayagam, G., Easteal, S., Jermiin, L. S., Schulte, G. K., Danley, D. E., Hoth, L. R., Griffor, M. C., Kamath, A. V., Rosner, M. H., Chrunyk, B. A., Perregaux, D. E., Gabel, C. A., Geoghegan, K. F., and Pandit, J. (2000) Identification, characterization, and crystal structure of the Omega class glutathione transferases, J. Biol. Chem. 275, 24798-24806.
6. Tsuchida, S., and Sato, K. (1992) Glutathione transferases and cancer, Crit. Rev. Biochem. Mol. Biol. 27, 337-384.
7. Nakagawa, K., Saijo, N., Tsuchida, S., Sakai, M., Tsunokawa, Y., Yokota, J., Muramatsu, M., Sato, K., Terada, M., and Tew, K. D. (1990) Glutathione-S-transferase pi as a determinant of drug resistance in transfectant cell lines, J. Biol. Chem. 265, 4296-4301.
8. Lee, F. Y., Sciandra, J., and Siemann, D. W. (1989) A study of the mechanism of resistance to Adriamycin in vivo. Glutathione metabolism, P-glycoprotein expression, and drug transport, Biochem. Pharmacol. 38, 3697-3705.
9. Moscow, J. A., Fairchild, C. R., Madden, M. J., Ransom, D. T., Wieand, H. S., O'Brien, E. E., Poplack, D. G., Cossman, J., Myers, C. E., and Cowan, K. H. (1989) Expression of anionic glutathione-S-transferase and P-glycoprotein genes in human tissues and tumors, Cancer Res. 49, 1422-1428.
10. Awasthi, Y. C., Sharma, R., and Singhal, S. S. (1994) Human glutathione S-transferases, Int. J. Biochem. 26, 295-308.
11. Board, P., Coggan, M., Johnston, P., Ross, V., Suzuki, T., and Webb, G. (1990) Genetic heterogeneity of the human glutathione transferases: a complex of gene families, Pharmacol. Ther. 48, 357-369.
12. Adler, V., Yin, Z., Fuchs, S. Y., Benezra, M., Rosario, L., Tew, K. D., Pincus, M. R., Sardana, M., Henderson, C. J., Wolf, C. R., Davis, R. J., and Ronai, Z. (1999) Regulation of JNK signaling by GSTp, EMBO J. 18, 1321-1334.
13. Wang, T., Arifoglu, P., Ronai, Z., and Tew, K. D. (2001) Glutathione S-transferase P1-1 (GSTP1-1) inhibits c-Jun N-terminal kinase (JNK1) signaling through interaction with the C terminus, J. Biol. Chem. 276, 20999-21003.
14. Elsby, R., Kitteringham, N. R., Goldring, C. E., Lovatt, C. A., Chamberlain, M., Henderson, C. J., Wolf, C. R., and Park, B. K. (2003) Increased constitutive c-Jun N-terminal kinase signaling in mice lacking glutathione S-transferase Pi, J. Biol. Chem. 278, 22243-22249.
15. Adler, V., and Pincus, M. R. (2004) Effector peptides from glutathione-S-transferase-pi affect the activation of jun by jun-N-terminal kinase, Ann. Clin. Lab. Sci. 34, 35-46.
16. McIlwain, C. C., Townsend, D. M., and Tew, K. D. (2006) Glutathione S-transferase polymorphisms: cancer incidence and therapy, Oncogene 25, 1639-1648.
17. Manevich, Y., Feinstein, S. I., and Fisher, A. B. (2004) Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires glutathionylation mediated by heterodimerization with pi GST, Proc. Natl. Acad. Sci. U.S.A. 101, 3780-3785.
18. Ralat, L. A., Manevich, Y., Fisher, A. B., and Colman, R. F. (2006) Direct evidence for the formation of a complex between 1-cysteine peroxiredoxin and glutathione S-transferase pi with activity changes in both enzymes, Biochemistry 45, 360-372.
19. Wu, Y., Fan, Y., Xue, B., Luo, L., Shen, J., Zhang, S., Jiang, Y., and Yin, Z. (2006) Human glutathione S-transferase P1-1 interacts with TRAF2 and regulates TRAF2-ASK1 signals, Oncogene (in press) (doi: 10.1038).
20. Habig, W. H., Pabst, M. J., and Jakoby, W. B. (1974) Glutathione S-transferases. The first enzymatic step in mercapturic acid formation, J. Biol. Chem. 249, 7130-7139.
21. Litwack, G., Ketterer, B., and Arias, I. M. (1971) Ligandin: a hepatic protein which binds steroids, bilirubin, carcinogens and a number of exogenous organic anions, Nature 234, 466-467.
22. Tipping, E., and Ketterer, B. (1981) The influence of soluble binding proteins on lipophile transport and metabolism in hepatocytes, Biochem. J. 195, 441-452.
23. Caccuri, A. M., Aceto, A., Piemonte, F., Di Ilio, C., Rosato, N., and Federici, G. (1990) Interaction of hemin with placental glutathione transferase, Eur. J. Biochem. 189, 493-497.
24. Ralat, L. A., and Colman, R. F. (2003) Monobromobimane occupies a distinct xenobiotic substrate site in glutathione S-transferase pi, Protein Sci. 12, 2575-2587.
25. Ralat, L. A., and Colman, R. F. (2004) Glutathione S-transferase pi has at least three distinguishable xenobiotic substrate sites close to its glutathione-binding site, J. Biol. Chem. 279, 50204-50213.
26. van Haaften, R. I., Evelo, C. T., Haenen, G. R., and Bast, A. (2001) Alpha-Tocopherol inhibits human glutathione S-transferase pi, Biochem. Biophys. Res. Commun. 280, 631-633.
27. van Haaften, R. I., Evelo, C. T., Penders, J., Eijnwachter, M. P., Haenen, G. R., and Bast, A. (2001) Inhibition of human glutathione S-transferase P1-1 by tocopherols and alpha-tocopherol derivatives, Biochim. Biophys. Acta 1548, 23-28.
28. van Haaften, R. I., Haenen, G. R., Evelo, C. T., and Bast, A. (2003) Effect of vitamin E on glutathione-dependent enzymes. Drug Metab. Rev. 35, 215-253.
29. van Haaften, R. I., Haenen, G. R., van Bladeren, P. J., Bogaards, J. J., Evelo, C. T., and Bast, A. (2003) Inhibition of various glutathione S-transferase isoenzymes by RRR-alpha-tocopherol, Toxicol. In Vitro 17, 245-251.
30. Kamal-Eldin, A., and Appelqvist, L. A. (1996) The chemistry and antioxidant properties of tocopherols and tocotrienols, Lipids 31, 671-701.
31. Miller, E. R., III, Pastor-Barriuso, R., Dalal, D., Riemersma, R. A., Appel, L. J., and Guallar, E. (2005) Meta-analysis: high-dosage vitamin E supplementation may increase all-cause mortality, Ann. Intern. Med. 142, 37-46.
32. Manoharan, T. H., Gulick, A. M., Puchalski, R. B., Servais, A. L., and Fahl, W. E. (1992) Structural studies on human glutathione S-transferase pi. Substitution mutations to determine amino acids necessary for binding glutathione, J. Biol. Chem. 267, 18940-18945.
33. Pons, M., Nicolas, J. C., Boussioux, A. M., Descomps, B., and Crastes de Paulet, A. I. (1973) Affinity labelling of an histidine of the active site of the human placental 17 beta-oestradiol dehydrogenase, FEBS Lett. 36, 23-26.
34. Penefsky, H. S. (1979) A centrifuged-column procedure for the measurement of ligand binding by beef heart F1, Methods Enzymol. 56, 527-530.
35. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
36. Oakley, A. J., Lo Bello, M., Battistoni, A., Ricci, G., Rossjohn, J., Villar, H. O., and Parker, M. W. (1997) The structures of human glutathione transferase P1-1 in complex with glutathione and various inhibitors at high resolution, J. Mol. Biol. 274, 84-100.
37. Oakley, A. J., Lo Bello, M., Nuccetelli, M., Mazzetti, A. P., and Parker, M. W. (1999) The ligandin (non-substrate) binding site of human Pi class glutathione transferase is located in the electrophile binding site (H-site), J. Mol. Biol. 291, 913-926.
38. Bico, P., Erhardt, J., Kaplan, W., and Dirr, H. (1994) Porcine class glutathione S-transferase: Anionic ligand binding and conformational analysis, Biochim. Biophys. Acta 1247, 225-230.
39. Prade, L., Huber, R., Manoharan, T. H., Fahl, W. E., and Reuter, W. (1997) Structures of class pi glutathione S-transferase from human placenta in complex with substrate, transition-state analogue and inhibitor, Structure 5, 1287-1295.
40. Ji, X., Tordova, M., O'Donnell, R., Parsons, J. F., Hayden, J. B., Gilliland, G. L., and Zimniak, P. (1997) Structure and function of the xenobiotic substrate-binding site and location of a potential non-substrate-binding site in a class pi glutathione S-transferase, Biochemistry 36, 9690-9702.
41. Gate, L., and Tew, K. D. (2001) Glutathione S-transferases as emerging therapeutic targets, Expert Opin. Ther. Targets 5, 477-489.
42. Colman, R. F. (1990) Site-specific modification of enzyme sites, in The Enzymes (Sigman, D. S., and Boyer, P. D., Eds.) 3rd ed., Vol. 19, Chapter 7, pp 283-321, Academic Press, New York.
43. Wilchek, M., and Givol, M. (1977) Haloacetyl derivatives, Methods Enzymol 46, 153-157.
44. Liu, S., Zhang, P., Ji, X., Johnson, W. W., Gilliland, G. L., and Armstrong, R. N. (1992) Contribution of tyrosine 6 to the catalytic mechanism of isoenzyme 3-3 of glutathione S-transferase, J. Biol. Chem. 267, 4296-4299.
45. Stenberg, G., Board, P. G., and Mannervik, B. (1991) Mutation of an evolutionarily conserved tyrosine residue in the active site of a human class Alpha glutathione transferase, FEBS Lett. 293, 153-155.
46. Kolm, R. H., Sroga, G. E., and Mannervik, B. (1992) Participation of the phenolic hydroxyl group of Tyr-8 in the catalytic mechanism of human glutathione transferase P1-1, Biochem. J. 285 (Part 2), 537-540.
47. Lo Bello, M., Oakley, A. J., Battistoni, A., Mazzetti, A. P., Nuccetelli, M., Mazzarese, G., Rossjohn, J., Parker, M. W., and Ricci, G. (1997) Multifunctional role of Tyr 108 in the catalytic mechanism of human glutathione transferase P1-1. Crystallographic and kinetic studies on the Y108F mutant enzyme, Biochemistry 36, 6207-6217.
48. Stenberg, G., Abdalla, A. M., and Mannervik, B. (2000) Tyrosine 50 at the subunit interface of dimeric human glutathione transferase P1-1 is a structural key residue for modulating protein stability and catalytic function, Biochem. Biophys. Res. Commun. 271, 59-63.