Irreversible thermal denaturation of glutathione transferase P1-1. Evidence for varying structural stability of different domains

International Journal of Biochemistry and Cell Biology

Volumn 30, Issue 1, 1998, Pages 155-163

  Dragani, Beatrice ^a   Iannarelli, Vincenzina ^a   Allocati, Nerino ^a   Masulli, Michele ^a   Cicconetti, Mario ^a   Aceto, Antonio ^a  

^a UNIVERSITY OF CHIETI   (Italy)

Author keywords

Domain; Glutathione transferase; Thermal denaturation

Indexed keywords

GLUTATHIONE TRANSFERASE;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME DENATURATION; ENZYME STRUCTURE; HUMAN; HUMAN TISSUE; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE; THERMAL ANALYSIS;

EID: 0032546415     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(97)00071-X     Document Type: Article

References (23)

1. Aceto A., Caccuri A. M., Sacchetta P., Bucciarelli T., Dragani B., Rosato N., Federici G., Di Ilio C. Dissociation and unfolding of Pi-class glutathione transferase. Biochem. J. 285:1992;241-245.
2. Aceto A., Dragani B., Allocati N., Angelucci S., Bucciarelli T., Sacchetta P., Di Ilio C., Martini F. Analysis by limited proteolysis of domain organization and GSH-site arrangement of bacterial glutathione transferase B1-1. Int. J. Biochem. Cell Biol. 27:1995;1033-1041.
3. Aceto A., Sacchetta P., Bucciarelli T., Dragani B., Angelucci S., Radatti G. L., Di Ilio C. Structural and functional properties of the 34 kDa fragment produced by the N-terminal chymotriptic cleavage of glutathione transferase P1-1. Arch. Biochem. Biophys. 316:1995;873-878.
4. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
5. Buetler T. M., Eaton D. L. Glutathione transferases: amino acid sequence comparison, classification and phylogenetic relationship. Environ. Carcino. Ecotox. Rev. 10:1992;181-203.
6. Creighton T. E. Protein folding. Biochem. J. 270:1990;1-16.
7. Graminski G. F., Kubo Y., Armstrong R. N. Spectroscopicand kinetic evidence for the thiolate anion of glutathione at the active site of glutathione S-transferase. Biochemistry. 28:1989;3562-3568.
8. Habig W. H., Jakoby W. B. Assays for differentiation of glutathione S-transferases. Meth. Enzymol. 77:1981;398-405.
9. Hayes J. D., Pulford D. J. The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit. Rev. Biochem. Mol. Biol. 30:1995;445-600.
10. Ji X., Zhang P., Armstrong R. N., Gilliland G. L. The three-dimensional structure of glutathione S-transferase from the Mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2-Å, resolution. Biochemistry. 31:1992;10169-10184.
11. Ketterer B., Meyer D. J. and Clark A. G. (1988) Soluble glutathione transferase isoenzymes. In Glutathione Conjugation, Mechanisms and Biological Significance (Edited by H. Sies and B. Ketterer), pp. 73-135. Academic Press, London.
12. Kong K. H., Nishida M., Inoue H., Takahashi K. Tyrosine-7 is an essential residue for the catalytic activity of human class Pi glutathione S-transferase: chemical modification and site-directed mutagenesis studies. Biochem. Biophys. Res. Commun. 182:1992;1122-1129.
13. Liu S., Zhang P., Ji X., Johnson W. W., Gilliland G. L., Takahashi K. Contribution of tyrosine 6 to the catalytic mechanism of isoenzyme 3-3 of glutathione S-transferase. J. Biol. Chem. 267:1992;4296-4299.
14. Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M. K., Warholm M., Jornvall H. Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data enzymatic properties. Proc. Natl. Acad. Sci. USA. 82:1985;7203-7206.
15. Mannervik B., Danielson U. H. Glutathione transferases. Structure and catalytic activity. Crit. Rev. Biochem. 23:1988;283-337.
16. Meyer D. J., Coles B., Pemble S. E., Gilmore K. S., Fraser G. M., Ketterer B. Theta, a new class of glutathione transferases purified from rat, and man. Biochem. J. 274:1991;409-414.
17. Reinemer P., Dirr H. W., Ladenstein R., Huber R., Lo Bello M., Federici G., Parker M. W. Three-dimensional structure of class Pi Glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 Å resolution. J. Mol. Biol. 227:1992;214-226.
18. Reinemer P., Dirr H. W., Ladenstein R., Schäffer J., Gallay O., Huber R. The three-dimensional structure of class pi glutathione S-transferase in complex with glutathione sulfonate at 2.3 Å resolution. EMBO J. 10:1991;1997-2005.
19. Sacchetta P., Aceto A., Bucciarelli T., Dragani B., Santarone S., Allocati N., Di Ilio C. Multiphasic denaturation of glutathione transferase B1-1 by guanidinium chloride. Eur. J. Biochem. 215:1993;741-754.
20. Sinning I., Kleywegt G. J., Cowan S. W., Reinemer P., Dirr H. W., Huber R., Gilliland G. L., Armstrong R. N., Ji X. H., Board P. G., Olin B., Mannervik B., Jones T. A. Structure determination and refinement of human-Alpha class glutathione transferase A1-1, and a comparison with the Mu-class and Pi-class enzymes. J. Mol. Biol. 232:1993;192-212.
21. Stemberg G., Board P. G., Mannervik B. Mutation of an evolutionary conserved tyrosine residue in the active site of human class alpha glutathione transferase. FEBS Lett. 293:1991;153-155.
22. Wang R. W., Newton D. J., Huskey S. E. W., McKeever B. M., Pickett C. B., Lu A. Y. H. Site-directed mutagenesis of glutathione S-transferase YaYa: functional studies of histidine, cysteine and tryptophan mutants. Arch. Biochem. Biophys. 297:1992;86-91.
23. Wilce M. C. J., Board P. G., Feil S. C., Parker M. W. Crystal structure of a theta-class glutathione transferase. EMBO J. 14:1995;2133-2143.