The HDQVH-motif in domain E of the estradiol receptor α is responsible for zinc-binding and zinc-induced hormone release

Molecular and Cellular Endocrinology

Volumn 153, Issue 1-2, 1999, Pages 71-78

  Humeny, Andreas ^a   Bökenkamp, Dirk ^a   Thole, Hubert H ^a,b  

^a MAX PLANCK INSTITUTE FOR BIOPHYSICAL CHEMISTRY   (Germany)

^b OE 6724 D 30623   (Germany)

Author keywords

Estradiol; Estrogen receptor; Ligand binding domain; Metal binding; Swine; Zn

Indexed keywords

17ALPHA ESTRADIOL; ESTRADIOL RECEPTOR; ZINC;

AMINO ACID SEQUENCE; ARTICLE; HORMONE RECEPTOR INTERACTION; HORMONE RELEASE; LIGAND BINDING; METAL BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; SWINE;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CATIONS, DIVALENT; COPPER; DEOXYRIBONUCLEASE ECORI; DEOXYRIBONUCLEASE HINDIII; ESTRADIOL; METALLOENDOPEPTIDASES; MUTAGENESIS; NICKEL; PEPTIDE FRAGMENTS; POLYMERASE CHAIN REACTION; RECEPTORS, ESTRADIOL; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; SWINE; TRITIUM; ZINC;

EID: 0344654863     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0303-7207(99)00089-1     Document Type: Article

References (37)

1. Arnold F.H., Haymore B.L. Engineered metal-binding proteins: purification to protein folding. Science. 252:1991;1796-1797.
2. Atkinson H.C., Ratajczak T., Hähnel R. Interaction of bovine estrogen receptor with immobilized zinc. Steroids. 55:1990;405-409.
3. Bökenkamp D., Jungblut P.W., Thole H.H. The C-terminal half of the porcine estradiol receptor contains no post-translational modification: determination of the primary structure. Mol. Cell. Endocrinol. 104:1994;163-172.
4. Brzozowski A.M., Pike A.C.W., Dauter Z. et al. Molecular basis of agonism and antagonism in the oestrogen receptor. Nature. 389:1997;753-758.
5. Chambraud B., Berry M., Redeuilh G., Chambon P., Baulieu E.E. Several regions of human estrogen receptor are involved in the formation of receptor-heat shock protein 90 complexes. J. Biol. Chem. 265:1990;20686-20691.
6. Darimont B.D., Wagner R.L., Apriletti J.W. et al. Structure and specificity of nuclear receptor-coactivator interactions. Genes Dev. 12:1998;3343-3356.
7. Enmark E., Pelto-Huikko M., Grandien K. et al. Human estrogen receptor beta-gene structure, chromosomal localization, and expression pattern. J. Clin. Endocrinol. Metab. 82:1997;4258-4265.
8. Fawell S.E., Lees J.A., White R., Parker M.G. Characterization and colocalization of steroid binding and dimerization activities in the mouse estrogen receptor. Cell. 60:1990;953-962.
9. Green S., Walter P., Kumar V., Krust A., Bornert J.-M., Argos P., Chambon P. Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A. Nature. 320:1986;134-139.
10. Greene G.L., Gilna P., Waterfield M., Baker A., Hort Y, Shine J. Sequence and expression of human estrogen receptor complementary DNA. Science. 231:1986;1150-1154.
11. Heery D.M., Kalkhoven E., Hoare S., Parker M.G. A signature motif in transcriptional coactivators mediates binding to nuclear receptors. Nature. 387:1997;654-655.
12. Heyns W., van Baelen H., De Moor P. Study of steroid-protein binding by means of competitive adsoption: application to cortisol binding in plasma. Clin. Chim. Acta. 18:1967;361-365.
13. Humeny A., Thole H.H. Detection of Zn-binding in domain E of the porcine estradiol receptor. Biochem. Biophys. Res. Commun. 194:1993;1248-1255.
14. Hutchens T.W., Li C.M., Sato Y., Yip T.-T. Multiple DNA-binding estrogen receptor forms resolved by interaction with immobilized metal ions: identification of a metal-binding domain. J. Biol. Chem. 264:1989;17206-17212.
15. Jensen E.V., Hurst D.J., DeSombre E.R., Jungblut P.W. Sulfhydryl groups and estradiol-receptor interaction. Science. 158:1967;385-387.
16. Jiang W., Bond J.S. Families of metalloendopeptidases and their relationships. FEBS Lett. 312:1992;110-114.
17. Jongeneel C.V., Bouvier J., Bairoch A. A unique signature identifies a family of zinc-dependent metallopeptidases. FEBS Lett. 242:1989;211-214.
18. Kumar V., Green S., Staub A., Chambon P. Localisation of the oestradiol-binding and putative DNA-binding domains of the human oestrogen receptor. EMBO J. 5:1986;2231-2236.
19. Little M., Szendro P.I., Jungblut P.W. Hormone-mediated dimerization of microsomal estradiol receptor Hoppe-Seyler's. Z. Physiol. Chem. 354:1973;1599-1610.
20. Lutwak-Mann C., McIntosh J.E. Zinc and carbonic anhydrase in the rabbit uterus. Nature. 221:1969;1111-1114.
21. Mazen A., Gradwohl G., de Muricia G. Zinc-binding proteins detected by protein blotting. Anal. Biochem. 172:1988;39-42.
22. Medici N., Minucci S., Nigro V., Abbondanza C., Armetta I., Molinari A.M., Puca G.A. Metal binding sites of the estradiol receptor from calf uterus and their possible role in the regulation of receptor function. Biochemistry. 28:1989;212-219.
23. Molinari A.M., Abbondanza C., Armetta I. et al. Proteolytic activity of the purified hormone-binding subunit in the estrogen receptor. Proc. Natl. Acad. Sci. USA. 88:1991;4463-4467.
24. Nolte R.T., Wisely G.B., Westin S. et al. Ligand binding and coactivator assembly of the peroxisome proliferator-activated receptor-gamma. Nature. 395:1998;137-143.
25. Orti E., Bodwell J.E., Munck A. Phosphorylation of steroid hormone receptors. Endocr. Rev. 13:1992;105-128.
26. Picard D., Kumar V., Chambon P., Yamamoto K.R. Signal transduction by steroid hormones: nuclear localization is differentially regulated in estrogen and glucocorticoid receptors. Cell Regul. 1:1990;291-299.
27. Saiki R.K., Gelfand D.H., Stoffel S. et al. Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase. Science. 239:1988;487-491.
28. Sanger F., Nicklen S., Coulson A.R. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA. 74:1977;5463-5467.
29. Schwabe J.W., Neuhaus D., Rhodes D. Solution structure of the DNA-binding domain of the oestrogen receptor. Nature. 348:1990;458-461.
30. Shiau A.K., Barstad D., Loria P.M., Cheng L., Kushner P.J., Agard D.A., Greene G.L. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell. 95:1998;927-937.
31. Thole H.H. The side chains responsible for the dimerization of the estradiol receptor by ionic bonds are lost in a 17 kDa fragment extending downstream from aa 303. J. Steroid Biochem. Mol. Biol. 48:1994;463-466.
32. Thole H.H., Jakob F. Characterization of five monoclonal antibodies raised against domain E of the porcine estradiol receptor. Exp. Clin. Endo. 101:1993;112-118.
33. Thole H.H., Jungblut P.W. The ligand-binding site of the estradiol receptor resides in a non-covalent complex of two consecutive peptides of 17 and 7 kDa. Biochem. Biophys. Res. Commun. 199:1994;826-833.
34. Thole H.H., Jungblut P.W., Jakob F. The proton-driven dissociation of oestradiol-receptor dimers as a preparative tool: isolation of a 32 kDa fragment from porcine uteri and assignment of C-terminal origin by partial sequencing. Biochem. J. 276:1991;709-714.
35. Vallee B.L., Auld D.S. Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry. 29:1990;5647-5659.
36. Wolf B., Dickson R.B., Hanover J.A. A nuclear localization signal in steroid hormone receptors? TIPS. 8:1987;119-121.
37. Young P.C., Cleary R.E., Ragan W.D. Effect of metal ions on the binding of 17beta-estradiol to human endometrial cytosol. Fert. Steril. 28:1977;459-463.