Drosophila nuclear receptor E75 is a thiolate hemoprotein

Biochemistry

Volumn 45, Issue 32, 2006, Pages 9727-9734

  De Rosny, Eve ^a,c   De Groot, Arjan ^b   Jullian Binard, Celine ^a   Gaillard, Jacques ^a   Borel, Franck ^a   Pebay Peyroula, Eva ^a   Fontecilla Camps, Juan Carlos ^a   Jouve, Hélène M ^a  

^a CEA GRENOBLE   (France)

^b AIX MARSEILLE UNIVERSITY   (France)

^c INSTITUT DE BIOLOGIE STRUCTURALE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; ESCHERICHIA COLI; HORMONES; MUTAGENESIS; PARAMAGNETIC RESONANCE; PHYSIOLOGY; SYNTHESIS (CHEMICAL);

HORMONE SYNTHESIS REGULATION; HYDROPHOBIC HORMONE LIGANDS; IRON BOUND THIOLATE;

PROTEINS;

CELL NUCLEUS RECEPTOR; CYSTEINE; HEME; HEMIN; HEMOPROTEIN; HISTIDINE; HORMONE; INSECT PROTEIN; IRON; IRON BINDING PROTEIN; LIGAND; MUTANT PROTEIN; PHENYLALANINE; PROTEIN E75; THIOL DERIVATIVE; THIOLATE HEMOPROTEIN; TRANSCRIPTION FACTOR; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; CULTURE MEDIUM; DROSOPHILA; ELECTRON SPIN RESONANCE; ESCHERICHIA COLI; GAS; HORMONE BINDING; HORMONE SYNTHESIS; LIGAND BINDING; LIGAND BINDING DOMAIN; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN FUNCTION; SITE DIRECTED MUTAGENESIS; TRANSCRIPTION REGULATION; ULTRAVIOLET SPECTROPHOTOMETRY;

ALANINE; AMINO ACID SEQUENCE; ANIMALS; CYSTEINE; DNA-BINDING PROTEINS; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; ELECTRON SPIN RESONANCE SPECTROSCOPY; GENE EXPRESSION; HEME; HEMEPROTEINS; HISTIDINE; HUMANS; LIGANDS; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, CYTOPLASMIC AND NUCLEAR; SEQUENCE ALIGNMENT; SOLUBILITY; SPECTROPHOTOMETRY, ULTRAVIOLET; SULFUR; TRANSCRIPTION FACTORS;

ESCHERICHIA COLI; EUKARYOTA;

EID: 33747503960     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060537a     Document Type: Article

References (32)

1. Renaud, J. P., and Moras, D. (2000) Structural studies on nuclear receptors, Cell. Mol. Life Sci. 57, 1748-1769.
2. White, K. P., Hurban, P., Watanabe, T., and Hogness, D. S. (1997) Coordination of Drosophila metamorphosis by two ecdysone-induced nuclear receptors. Science 276, 114-117.
3. Weatherman, R. V., Fletterick, R. J., and Scanlan, T. S. (1999) Nuclear-receptor ligands and ligand-binding domains, Annu. Rev. Biochem. 68, 559-581.
4. Falsone, S. F., Kurkela, R., Chiarandini, G., Vihko, P., and Kungl, A. J. (2001) Ligand affinity, homodimerization, and ligand-induced secondary structural change of the human vitamin d receptor, Biochem. Biophys. Res. Commun. 285, 1180-1185.
5. Moore, L. B., Goodwill, B., Jones, S. A., Wisely, G. B., Serabjit-Singh, C. J., Willson, T. M., Collins, J. L., and Kliewer, S. A. (2000) St. John's wort induces hepatic drug metabolism through activation of the pregnane X receptor, Proc. Natl. Acad. Sci. U.S.A. 97, 7500-7502.
6. Reinking, J., Lam, M. M., Pardee, K., Sampson, H. M., Liu, S., Yang, P., Williams, S., White, W., Lajoie, G., Edwards, A., and Krause, H. M. (2005) The Drosophila nuclear receptor e75 contains heme and is gas responsive, Cell 122, 195-207.
7. Ponting, C. P., and Aravind, L. (1997) PAS: A multifunctional domain family comes to light. Curr. Biol. 7, R674-R677.
8. Gilles-Gonzalez, M. A., and Gonzalez, G. (2005) Heme-based sensors: Defining characteristics, recent developments, and regulatory hypotheses, J. Inorg. Biochem. 99, 1-22.
9. Igarashi, J., Sato, A., Kitagawa, T., Yoshimura, T., Yamauchi, S., Sagami, I., and Shimizu, T. (2004) Activation of heme-regulated eukaryotic initiation factor 2α kinase by nitric oxide is induced by the formation of a five-coordinate NO-heme complex: Optical absorption, electron spin resonance, and resonance Raman spectral studies, J. Biol. Chem. 279, 15752-15762.
10. Lanzilotta, W. N., Schuller, D. J., Thorsteinsson, M. V., Kerby, R. L., Roberts, G. P., and Poulos, T. L. (2000) Structure of the CO sensing transcription activator CooA. Nat. Struct. Biol. 7, 876-880.
11. Omura, T. (2005) Heme-thiolate proteins. Biochem. Biophys. Res. Commun. 338, 404-409.
12. Lee, H. C., Hon, T., Lan, C., and Zhang, L. (2003) Structural environment dictates the biological significance of heme-responsive motifs and the role of Hsp90 in the activation of the heme activator protein Hap1, Mol. Cell. Biol. 23, 5857-5866.
13. Ogawa, K., Sun, J., Taketani, S., Nakajima, O., Nishitani, C., Sassa, S., Hayashi, N., Yamamoto, M., Shibahara, S., Fujita, H., and Igarashi, K. (2001) Heme mediates derepression of Maf recognition element through direct binding to transcription repressor Bachl, EMBO J. 20, 2835-2843.
14. Zhang, L., and Guarente, L. (1995) Heme binds to a short sequence that serves a regulatory function in diverse proteins, EMBO J. 14, 313-320.
15. Lathrop, J. T., and Timko, M. P. (1993) Regulation by heme of mitochondrial protein transport through a conserved amino acid motif. Science 259, 522-525.
16. Ojha, S., Hwang, J., Kabil, O., Penner-Hahn, J. E., and Banerjee, R. (2000) Characterisation of the heme in human cystathionine β-synthase by X-ray absorption and electron paramagnetic resonance spectroscopies, Biochemistry 39, 10542-10547.
17. Cheesman, M. R., Little, P. J., and Berks, B. C. (2001) Novel heme ligation in a c-type cytochrome involved in thiosulfate oxidation: EPR and MCD of SoxAX from Rhodovulum sulfidophilum, Biochemistry 40, 10562-10569.
18. Rieske, J. S., Lipton, S. H., Baum, H., and Silman, H. I. (1967) Factors affecting the binding of antimycin A to complex 3 of the mitochondrial respiratory chain, J. Biol. Chem. 242, 4888-4896.
19. Schwede, T., Kopp, J., Guex, N., and Peitsch, M. C. (2003) SWISS-MODEL: An automated protein homology-modeling server, Nucleic Acids Res. 31, 3381-3385.
20. Pazicni, S., Lukat-Rodgers, G. S., Oliveriusova, J., Rees, K. A., Parks, R. B., Clark, R. W., Rodgers, K. R., Kraus, J. P., and Burstyn, J. N. (2004) The redox behavior of the heme in cystathionine β-synthase is sensitive to pH, Biochemistry 43, 14684-14695.
21. Lawson, R. J., Leys, D., Sutcliffe, M. J., Kemp, C. A., Cheesman, M. R., Smith, S. J., Clarkson, J., Smith, W. E., Haq, I., Perkins, J. B., and Munro, A. W. (2004) Thermodynamic and biophysical characterization of cytochrome P450 Biol from Bacillus subtilis, Biochemistry 43, 12410-12426.
22. Dawson, J. H., and Sono, M. (1987) Cytochrome p-450 and chloroperoxidase: Thiolate-ligated heme enzymes. Spectroscopic determination of their active-site structures and mechanistic implications of thiolate ligation, Chem. Rev. 87, 1255-1276.
23. Clark, R. W., Youn, H., Parks, R. B., Cherney, M. M., Roberts, G. P., and Burstyn, J. N. (2004) Investigation of the role of the N-terminal proline, the distal heme ligand in the CO sensor CooA. Biochemistry 43, 14149-14160.
24. Tsai, A. L., Berka, V., Chen, P. F., and Palmer, G. (1996) Characterization of endothelial nitric-oxide synthase and its reaction with ligand by electron paramagnetic resonance spectroscopy, J. Biol. Chem. 271, 32563-32571.
25. Dawson, J. H., Andersson, L. A., and Sono, M. (1982) Spectroscopic investigations of ferric cytochrome P-450-CAM ligand complexes. Identification of the ligand trans to cysteinate in the native enzyme, J. Biol. Chem. 257, 3606-3617.
26. Dhawan, I. K., Shelver, D., Thorsteinsson, M. V., Roberts, G. P., and Johnson, M. K. (1999) Probing the heme axial ligation in the CO-sensing CooA protein with magnetic circular dichroism spectroscopy. Biochemistry 38, 12805-12813.
27. Sigman, J. A., Pond, A. E., Dawson, J. H., and Lu, Y. (1999) Engineering cytochrome c peroxidase into cytochrome P450: A proximal effect on heme-thiolate ligation, Biochemistry 38, 11122-11129.
28. Neri, F., Indiani, C., Baldi, B., Vind, J., Welinder, K. G., and Smulevich, G. (1999) Role of the distal phenylalanine 54 on the structure, stability, and ligand binding of Coprinus cinereus peroxidase, Biochemistry 38, 7819-7827.
29. Sono, M., Andersson, L. A., and Dawson, J. H. (1982) Sulfur donor ligand binding to ferric cytochrome P-450-CAM and myoglobin. Ultraviolet-visible absorption, magnetic circular dichroism, and electron paramagnetic resonance Spectroscopic investigation of the complexes. J. Biol. Chem. 257, 8308-8320.
30. Wurtz, J. M., Bourguet, W., Renaud, J. P., Vivat, V., Chambon, P., Moras, D., and Gronemeyer, H. (1996) A canonical structure for the ligand-binding domain of nuclear receptors, Nat. Struct. Biol. 3, 87-94.
31. Bialecki, M., Shilton, A., Fichtenberg, C., Segraves, W. A., and Thummel, C. S. (2002) Loss of the ecdysteroid-inducible E75A orphan nuclear receptor uncouples molting from metamorphosis in Drosophila, Dev. Cell 3, 209-220.
32. Renaud, J. P., Harris, J. M., Downes, M., Burke, L. J., and Muscat, G. E. (2000) Structure-function analysis of the Rev-erbA and RVR ligand-binding domains reveals a large hydrophobic surface that mediates corepressor binding and a ligand cavity occupied by side chains, Mol. Endocrinol. 14, 700-717.