Chemical modification at subunit 1 of rat kidney Alpha class glutathione transferase with 2,3,5,6-tetrachloro-1,4-benzoquinone: Close structural connectivity between glutathione conjugation activity and non-substrate ligand binding

Biochemical Pharmacology

Volumn 71, Issue 11, 2006, Pages 1629-1636

  O'Sullivan, Siobhan M ^a   McCarthy, Ronan M ^a   Vargo, Melissa A ^b   Colman, Roberta F ^b   Sheehan, David ^a  

^a UNIVERSITY COLLEGE CORK   (Ireland)

^b UNIVERSITY OF DELAWARE   (United States)

Author keywords

Affinity label; Alpha class; Chemical modification; Cysteine; Glutathione transferase; Structure; Tetrachlorobenzoquinone

Indexed keywords

1 CHLORO 2,4 DINITROBENZENE; CHLORANIL; CYSTEINE; GLUTATHIONE TRANSFERASE; PENTACHLOROPHENOL; TRYPTOPHAN;

ALPHA HELIX; ARTICLE; CATALYSIS; CHEMICAL MODIFICATION; CORRELATION ANALYSIS; FLUORESCENCE; GLUTATHIONE METABOLISM; HYDROPHOBICITY; KIDNEY; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; RAT; SEQUENCE HOMOLOGY; STOICHIOMETRY; STRUCTURE ANALYSIS;

ANIMALS; CATALYTIC DOMAIN; CHLORANIL; GLUTATHIONE; GLUTATHIONE TRANSFERASE; ISOENZYMES; KIDNEY; LIGANDS; MALE; MODELS, MOLECULAR; PROTEIN SUBUNITS; RATS; RATS, WISTAR;

EID: 33646470296     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2006.03.002     Document Type: Article

References (36)

1. Sheehan D., Meade G., Foley V.M., and Dowd C. Structure, function and evolution of glutathione transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem J 360 (2001) 1-16
2. Hayes J.D., Flanagan J.U., and Jowsey I.R. Glutathione transferases. Ann Rev Pharmacol Toxicol 45 (2005) 51-88
3. Jakobsson P.J., Morgenstern R., Mancini J., Ford-Hutchinson A., and Persson B. Common structural features of MAPEG-a widespread superfamily of membrane-associated proteins with highly divergent functions in eicosanoid and glutathione metabolism. Protein Sci 8 (1999) 689-692
4. Listowsky I., Abramowitz M., Hanuna H., and Nitu Y. Intracellular binding and transport of hormones and xenobiotics by glutathione S-transferase. Drug Metab Rev 19 (1988) 305-318
5. Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M., et al. Identification of three classes of cytosolic glutathione transferases common to several mammalian species: correlation between structural data and enzymatic properties. Proc Natl Acad Sci USA 82 (1985) 7202-7206
6. Meyer D.J., Coles B., Pemble S.E., Gilmore K.S., Fraser G.M., and Ketterer B. Theta, a novel class of glutathione S-transferases purified from rat and man. Biochem J 274 (1991) 409-414
7. Buetler T.M., and Eaton D.L. Glutathione S-transferases-amino acid sequence comparison, classification and phylogenetic relationship. Environ Carcinogen Ecotoxicol Rev C10 (1992) 181-203
8. Pemble S.E., Wardle A.F., and Taylor J.B. Glutathione S-transferase class Kappa: characterization by the cloning of mitochondrial GST and identification of a human homologue. Biochem J 319 (1996) 749-754
9. Rossjohn J., Polekhina G., Feil S.C., Allocati N., Masulli M., Di Ilio C., et al. A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications. Structure 6 (1998) 721-734
10. Board P.G., Coggan M., Chelvanayagam G., Eastal S., Jermin L.S., Schulte G.K., et al. Identification, characterization and crystal structure of the Omega class glutathione transferases. J Biol Chem 275 (2000) 24798-24806
11. Scully N.C., and Mantle T.J. Tissue distribution and subunit structures of the multiple forms of glutathione S-transferase in the rat. Biochem J 193 (1981) 367-370
12. Rowe J.D., Nieves E., and Listowsky I. Subunit diversity and tissue distribution of human glutathione S-transferases: interpretations based on electrospray ionisation-MS and peptide sequence-specific antisera. Biochem J 325 (1997) 481-486
13. Hubatsch I., Ridderstrom M., and Mannervik B. Human glutathione transferase A4-4: an Alpha class enzyme with high catalytic efficiency in the conjugation of 4-hydroxynonenal and other genotoxic products of lipid peroxidation. Biochem J 330 (1998) 175-179
14. Bruns C.M., Hubatsch I., Ridderstrom M., Mannervik B., and Tainer J.A. Human glutathione transferase A4-4 crystal structures and mutagenesis reveal the basis of high catalytic efficiency with toxic lipid peroxidation products. J Mol Biol 288 (1999) 427-439
15. Sinning I., Kleywegt G.J., Cowan S.W., Reinemer P., Dirr H.W., Huber R., et al. Structure determination and refinement of human alpha class glutathione S-transferase A1-1, and a comparison with the mu and pi class enzymes. J Mol Biol 232 (1993) 192-212
16. Cameron A.D., Sinning I., L'Hermite G., Olin B., Board P.G., Mannervik B., et al. Structural analysis of human Alpha-class glutathione transferase A1-1 in the apo-form and in complex with ethacrynic acid and its glutathione conjugate. Structure 3 (1995) 717-727
17. Vargo M.A., and Colman R.F. Affinity labelling of rat glutathione S-transferase isozyme 1-1 by 17-beta-iodoacetoxy-estradiol-3-sulphate. J Biol Chem 276 (2001) 2031-2036
18. Nilsson L.O., Edalat M., Pettersson P.L., and Mannervik B. Aromatic residues in the C-terminal region of glutathione transferase A1-1 influence rate-determining steps in the catalytic mechanism. Biochim Biophys Acta 1598 (2002) 157-163
19. Kuhnert D.C., Sayed Y., Mosebi S., Sayed S.M., Sewel Tl, and Dirr H.W. Tertiary interactions stabilise the C-terminal region of human glutathione transferase A1-1: a crystallographic and calorimetric Study. J Mol Biol 349 (2005) 825-838
20. Chang L.H., Wang L.Y., and Tam M.F. The single cysteine residue on an Alpha family chick liver glutathione S-transferase CL 3-3 is not functionally important. Biochem Biophys Res Commun 180 (1991) 323-328
21. Nishihira J., Ishibashi T., Sakai M., Nishi S., Kumazaki T., Hatanaka Y., et al. Characterization of cysteine residues of glutathione S-transferase P-Evidence for steric hindrance of substrate binding by a bulky adduct to cysteine-47. Biochem Biophys Res Commun 188 (1992) 424-432
22. Hu L.Q., and Colman R.F. Resonance energy transfer between sites in rat liver glutathione S-transferase, 1-1, selectively modified at cysteine-17 and cysteine-111. Biochemistry 36 (1997) 1635-1645
23. van der Aar E.M., Tan K.T., Commandeur J.N.M., and Vermeulen N.P.E. Strategies to characterize the mechanisms of action and the active sites of glutathione S-transferases: a review. Drug Metab Rev 30 (1998) 569-643
24. van Ommen B., Adang A., Müller F., and van Bladeren P.J. The microsomal metabolism of pentachlorophenol and its covalent binding to protein and DNA. Chem-Biol Interactions 60 (1986) 1-11
25. van Ommen B., den Besten C., Rutten A.L.M., Ploemen J.H.T.M., Vos R.M.E., Müller F., et al. Active site-directed irreversible inhibition of glutathione S-transferases by the glutathione conjugate of tetrachloro-1,4-benzoquinone. J Biol Chem 263 (1988) 12939-12942
26. Ploemen J.H.T.M., van Ommen B., and van Bladeren P.J. Irreversible inhibition of human glutathione S-transferase isoenzymes by tetrachloro-1,4-benzoquinone and its glutathione conjugate. Biochem Pharmacol 41 (1991) 1665-1669
27. Carne C., Tipping E., and Ketterer B. The binding and catalytic activities of forms of ligandin after modification of its thiol groups. Biochem J 177 (1979) 433-439
28. McCarthy R., Farmer P., and Sheehan D. Binding of 2-hydroxy-5-nitrobenzyl alcohol to rat alpha class glutathione S-transferases: evidence for binding at tryptophan-21. Biochim Biophys Acta 1293 (1997) 185-190
29. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
30. Habig W.H., Pabst M.J., and Jakoby W.B. Glutathione S-transferases: the first step in mercapturic acid formation. J Biol Chem 249 (1974) 7130-7139
31. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
32. Cleland W.W. Statistical analysis of enzyme kinetic data. Methods Enzymol 63 (1979) 103-138
33. Valladon P. http://www.geneinfinity.org/rastop/; 2000.
34. Kitz R., and Wilson I.B. Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase. J Biol Chem 237 (1962) 3245-3249
35. Wang J., Baumann S., and Colman R.F. Probing subunit interactions in alpha class rat liver glutathione S-transferase with the photoaffinity label glutathionyl S-[4-(succinimidyl)benzophenone]. J Biol Chem 275 (2000) 5493-5503
36. Vargo M.A., Nguyen L., and Colman R.F. Subunit interface residues of glutathione S-transferase A1-1 that are important in the monomer-dimer equilibrium. Biochemistry 43 (2004) 3327-3335