Characterization of an estrogen-binding protein in the yeast Saccharomyces cerevisiae

Burshell, A., Stathis, P. A., Do, Y., Miller, S. C. and Feldman, D. (1984) Characterization of an estrogen-binding protein in the yeast Saccharomyces cerevisiae. Journal of Biological Chemistry, 259 6: 3450-3456.

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Author Burshell, A.
Stathis, P. A.
Do, Y.
Miller, S. C.
Feldman, D.
Title Characterization of an estrogen-binding protein in the yeast Saccharomyces cerevisiae
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
1083-351X
Publication date 1984-01-01
Sub-type Article (original research)
Open Access Status File (Publisher version)
Volume 259
Issue 6
Start page 3450
End page 3456
Total pages 7
Place of publication Bethesda, MD, United States
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Formatted abstract
This paper further characterizes the estrogen-binding protein we have described in the cytosol of the yeast Saccharomyces cerevisiae. [3H]Estradiol was used as the radioprobe, and specific binding of cytosol fractions was measured by chromatography on Sephadex minicolumns. Other 3H-steroids did not exhibit specific binding. [3H]Estradiol binding was destroyed by treatment with trypsin, but not RNase, DNase, or phospholipase; N-ethylmaleimide substantially decreased the binding. The yeast did not metabolize estradiol added to medium, and extraction and chromatography of the bound moiety showed it to be unmetabolized estradiol. Scatchard analysis of cytosol from both a and α mating types as well as the a/α diploid cell revealed similar binding properties: an apparent dissociation constant or K(d)(25°) for [3H]estradiol of 1.6-1.8 nM and a maximal binding capacity or N(max) of ~2000-2800 fmol/mg of cytosol protein. Gel exclusion chromatography on Sephacryl S-200 and high performance liquid chromatography suggested a Stokes radius of ~30 Å. Sucrose gradient centrifugation showed a sedimentation coefficient of ~5 S, and the complex did not exhibit ionic dependent aggregation. The estrogen binder in S. cerevisiae differed in its steroidal specificities from classical mammalian estrogen receptors in rat uterus. 17β-Estradiol was the best competitor, 17α-estradiol had about 5% the activity, and diethylstilbestrol exhibited negligible binding affinity as did tamoxifen, nafoxidine, and the zearalenones. In summary, a high affinity, stereospecific, steroid-selective binding protein has been demonstrated in the cytosol of the simple yeast S. cerevisiae. We speculate that this molecule may represent a primitive hormone receptor system, possibly for an estrogen-like message molecule.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: School of Medicine Publications
 
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Created: Mon, 14 Mar 2011, 18:49:27 EST