The interaction of oestrogen receptor with oligodeoxynucleotides
The interaction of oestrogen receptor with oligodeoxynucleotides
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雌激素受体与寡脱氧核苷酸的相互作用
DOI：
10.1042/bst0120322
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发表时间：
1984
影响因子：
3.9
通讯作者：
L. Myatt
中科院分区：
文献类型：
--
作者：
S. Hyder;M. Elder;L. Lim;L. Myatt
其作用可能仅仅是由于磷钼酸盐复合物的形成或寡核苷酸结合位点中的一些其他直接相互作用（见上文）。 4°C 标记 1 小时后，[3H]雌二醇在 29°C 磷酸盐缓冲液中与受体的解离速率常数为 k l 0.09+0.02min-l 和 k 2 3 .28k1 .56~ 10-3min-1（平均值.D.；n= 12）。以缓慢解离形式存在的受体比例为21.6％和5.5％。上述任何程序均未改变该比例（相当于能够与寡（dT）-纤维素结合的受体的最大比例）和速率常数。因此，受体的缓慢解离形式的出现发生在激活至核苷酸结合状态之前，但似乎决定了寡核苷酸结合的总体程度。可以与寡核苷酸结合的具有缓慢解离动力学的受体的量可以通过受体寡核苷酸位点的变化来调节，所述寡核苷酸位点涉及低分子量组分的解离、还原的硫醇基团的存在以及可能的磷酸化/去磷酸化机制。当阻止受体与寡(dT)纤维素结合时，钼酸盐可以发挥多种作用。受体对核苷酸结合形式的总体激活涉及两个独立的过程，介导解离动力学的变化和核苷酸结合位点的暴露。
its effect may be simply due to formation of phosphomolybdate complexes or by some other direct interaction in the oligonucleotide-binding site (see above). The dissociation rate constants for [3H]oestradiol from receptor in phosphate buffer at 29°C after l h of labelling at 4°C were k l 0.09+0.02min-l and k 2 3 .28k1 .56~ 10-3min-1 (meanks.D.;n= 12). Theproportion of receptor present as the slow-dissociating form was 21.6 & 5.5%. Neither this proportion, which was equivalent to the maximum proportion of receptor capable of binding to oligo(dT)-cellulose, nor the rate constants were altered by any of the procedures described above. Therefore appearance of the slow-dissociating form of receptor occurs before activation to a nucleotide-binding state, but appears to determine overall the extent of oligonucleotide binding. The amount of receptor with slow dissociation kinetics that can bind to a oligonucleotide can be regulated by changes in the receptor's oligonucleotide site involving dissociation of low-molecular-weight components, the presence of reduced thiol groups and possibly a phosphorylation/dephosphorylation mechanism. Molybdate may exert a plurality of effects when preventing receptor binding to oligo(dT)cellulose. Overall activation of receptor to a nucleotidebinding form involves two separate processes mediating changes in dissociation kinetics and exposure of the nucleotide-binding site.