The general validity of the subunit model of the progesterone receptor from chick oviduct appears questionable. Comparison of progesterone and estrogen receptor.
Estrogen and progesterone receptors from chick oviduct were compared with respect to their chromatographic behaviour on DEAE-cellulose and their DNA-binding ability to test the general validity of the subunit model from O'Malley and coworkers. Both hormone-receptor complexes can be separated on DEAE-cellulose into 2 components A and B. The 2 progesterone-receptor components appear to occur in equimolar amounts, whereas in the case of the estrogen receptor the amount of component A is always significantly larger. After trypsin treatment the estrogen component B disappears. The remaining A is a receptor fragment with reduced molecular weight. This and other data indicate that the estrogen component B represents an aggregated form of the estrogen receptor and not a receptor subunit. The trypsinated progesterone-receptor fragments, however, are still separable into 2 components, even though also reduced in molecular weight. Our DNA-binding data of the progesterone-receptor components are almost consistent with earlier data from O'Malley and coworkers, even though we find some DNA-binding ability also for component B. Both estrogen-receptor components exhibit affinity for DNA and significantly more than 50% (up to 80%) of the total estrogen-receptor complex are able to bind to DNA. Furthermore we could show that the estrogen-receptor from chick oviduct can be transformed from a DNA-non-binding to a DNA-binding form, similar to other steroid-hormone receptors. This is not compatible with pre-existing receptor subunits in equimolar amounts, one with and the other without affinity for DNA.[1]References
- The general validity of the subunit model of the progesterone receptor from chick oviduct appears questionable. Comparison of progesterone and estrogen receptor. Gschwendt, M. Mol. Cell. Endocrinol. (1980) [Pubmed]
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