Physiological levels of glutathione enhance Zn(II) binding by a Cys4 zinc finger

Biochemical and Biophysical Research Communications

Volumn 389, Issue 2, 2009, Pages 265-268

  Piatek, Katarzyna ^a   Hartwig, Andrea ^b   Bal, Wojciech ^a,c  

^a INSTITUTE OF BIOCHEMISTRY AND BIOPHYSICS   (Poland)

^b TECHNISCHE UNIVERSITÄT BERLIN   (Germany)

^c Ctrl Inst for Labour Protection   (Poland)

Author keywords

Dissociation constant; Fluorescence spectroscopy; Glutathione; Mass spectrometry; Zinc binding; Zinc finger

Indexed keywords

CADMIUM; COBALT; CYSTEINE 4 ZINC FINGER PROTEIN; DISULFIDE; GLUTATHIONE; METAL COMPLEX; METALLOTHIONEIN; UNCLASSIFIED DRUG; XERODERMA PIGMENTOSUM GROUP A PROTEIN; ZINC FINGER PROTEIN; ZINC ION;

ARTICLE; CONTROLLED STUDY; DISSOCIATION CONSTANT; ELECTROSPRAY MASS SPECTROMETRY; FLUORESCENCE SPECTROSCOPY; METAL BINDING; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; ULTRAVIOLET SPECTROSCOPY; ZINC FINGER MOTIF;

ANIMALS; CYSTEINE; FLUORESCENCE; GLUTATHIONE; HUMANS; PEPTIDES; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; XERODERMA PIGMENTOSUM GROUP A PROTEIN; ZINC; ZINC FINGERS;

EID: 70349336671     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.08.128     Document Type: Article

References (26)

1. Maret W. Zinc and sulfur: a critical biological partnership. Biochemistry 43 (2004) 3301-3309
2. Witkiewicz-Kucharczyk A., and Bal W. Damage of zinc fingers in DNA repair proteins, a novel molecular mechanism in carcinogenesis. Toxicol. Lett. 162 (2006) 29-42
3. Kre{ogonek}żel A., and Maret W. Thionein/metallothionein control Zn(II) availability and the activity of enzymes. J. Biol. Inorg. Chem. 13 (2008) 401-409
4. Meister A., and Anderson M.A. Glutathione. Ann. Rev. Biochem. 52 (1983) 711-760
5. Bellomo G., Vairetti M., Stivala L., Mirabelli F., Richelmi P., and Orrenius S. Demonstration of nuclear compartmentalization of glutathione in hepatocytes. Proc. Natl. Acad. Sci. USA 89 (1992) 4412-4416
6. Maret W., and Kre{ogonek}żel A. Dual nanomolar and picomolar Zn(II) binding properties of metallothionein. J. Am. Chem. Soc. 129 (2007) 10911-10921
7. Kre{ogonek}żel A., and Bal W. The coordination chemistry of glutathione. Acta Biochim. Pol. 46 (1999) 567-580
8. A. Kre{ogonek}żel J. Wjcik, M. Maciejczyk, W. Bal, May GSH and L-His contribute to intracellular binding of zinc? Thermodynamic and solution structural study of a ternary complex, Chem. Comm. (2003) 704-705.
9. 2+ complexation. J. Inorg. Biochem. 101 (2007) 1442-1456
10. Kre{ogonek}żel A., and Bal W. Studies of zinc(II) and nickel(II) complexes of GSH, GSSG and their analogs shed more light on their biological relevance. Bioinorg. Chem. Appl. 2 (2004) 293-305
11. Bal W., Schwerdtle T., and Hartwig A. Mechanism of nickel assault on the zinc finger of DNA repair protein XPA. Chem. Res. Toxicol. 16 (2003) 242-248
12. II in the zinc finger derived from the DNA repair protein XPA, demonstrating a variety of potential mechanisms of toxicity. Chem. Res. Toxicol. 17 (2004) 1452-1458
13. Blessing H., Krauss S., Heindl P., Bal W., and Hartwig A. Interaction of selenium compounds with zinc finger proteins involved in DNA repair. Eur. J. Biochem. 271 (2004) 3190-3199
14. 2. Anal. Biochem. 369 (2007) 226-231
15. Smirnova J., Zhukova L., Witkiewicz-Kucharczyk A., Kopera E., Ole{ogonek}dzki J., Wysłouch-Cieszyńska A., Palumaa P., Hartwig A., and Bal W. Reaction of the XPA zinc finger with GSNO. Chem. Res. Toxicol. 21 (2008) 386-392
16. Pia{ogonek}tek K., Schwerdtle T., Hartwig A., and Bal W. Monomethylarsonous acid destroys a tetrathiolate zinc finger much more efficiently than inorganic arsenite. Mechanistic considerations and consequences for DNA repair inhibition. Chem. Res. Toxicol. 21 (2008) 600-606
17. McCall K.A., and Fierke C.A. Colorimetric and fluorimetric assays to quantitate micromolar concentrations of transition metals. Anal. Biochem. 284 (2000) 307-315
18. Magyar J.S., and Godwin H.A. Spectropotentiometric analysis of metal binding to structural zinc-binding sites: accounting quantitatively for pH and metal ion buffering effects. Anal. Biochem. 320 (2003) 39-54
19. 2, a putative metal binding sequence of histone H3. Chem. Res. Toxicol. 9 (1996) 435-440
20. Banerjea D., Kaden T.A., and Sigel H. Enhanced stability of ternary complexes in solution through the participation of heteroaromatic N bases. Comparison of the coordination tendency of pyridine, imidazole, ammonia, acetate, and hydrogen phosphate toward metal ion nitrilotriacetate complexes. Inorg. Chem. 20 (1981) 2586-2590
21. Buchko G.W., Hess N.J., and Kennedy M.A. Human nucleotide excision repair protein XPA: summary of EXAFS studies on the Zn(II), Co(II) and Cd(II) associated minimal DNA-binding domain. Protein Pept. Lett. 7 (2000) 49-56
22. Brouwer M., Hoexum-Brouwer T., and Cashon R.E. A putative glutathione-binding site in CdZn-metallothionein identified by equilibrium binding and molecular-modelling studies. Biochem. J. 294 (1993) 219-225
23. Heinz U., Kiefer M., Tholey A., and Adolph H.-.W. On the competition for available zinc. J. Biol. Chem. 280 (2005) 3197-3207
24. Reddi A.R., and Gibney B.R. Role of protons in the thermodynamic contribution of a Zn(II)-Cys4 site toward metalloprotein stability. Biochemistry 46 (2007) 3745-3758
25. Koch S., Volkmar C.M., Kolb-Bachofen V., Korth H.-.G., Kirsch M., Horn A.H.C., Sticht H., Pallua N., and Suschek C.V. A new redox-dependent mechanism of MMP-1 activity control comprising reduced low-molecular-weight thiols and oxidizing radicals. J. Mol. Med. 87 (2009) 261-272
26. Zhang W., Wang L., Liu Y., Xu J., Zhu G., Cang H., Li X., Bartlam M., Hensley K., Li G., Rao Z., and Zhang X.C. Structure of human lanthionine synthetase C-like protein 1 and its interaction with Eps8 and glutathione. Genes Dev. 23 (2009) 1387-1392