TY - JOUR
T1 - Activation of oestrogen receptor complexes
T2 - Evidence for the distinct regulation of ligand and oligonucleotide binding sites
AU - Myatt, Leslie
AU - Cukier, David
AU - Elder, Murdoch G.
AU - White, John O.
PY - 1985/5/30
Y1 - 1985/5/30
N2 - The activation of the rat uterine oestrogen receptor has been measured in vitro by its binding to oligodeoxythymidylate cellulose (oligo(dT)) and was found to be sensitive to the time and temperature of prior incubation of cytosol with oestradiol. The presence of 20 mM dithiothreitol promoted receptor activation and was partially inhibited by 10 mM molybdate; molybdate also inhibited the time- and temperature-dependent activation of receptor. The nucleotides GTP, ATP, ADP, CTP and UTP all promoted receptor activation; the effect of GTP was significantly greater than that of ATP. It is unlikely that phosphate donation is involved in receptor activation as the effects of GTP could be reproduced by p[NH]ppG (guanosine 5′-[β,γ-imido]triphosphate), while PPi was also effective in activating receptor. The results provide evidence for the distinct regulation of the oligonucleotide- and ligand-binding domains, since manipulations which promoted binding to oligo(dT) did not affect either ligand binding capacity or the rate constant and composition the biphasic dissociation of the ligand receptor complex.
AB - The activation of the rat uterine oestrogen receptor has been measured in vitro by its binding to oligodeoxythymidylate cellulose (oligo(dT)) and was found to be sensitive to the time and temperature of prior incubation of cytosol with oestradiol. The presence of 20 mM dithiothreitol promoted receptor activation and was partially inhibited by 10 mM molybdate; molybdate also inhibited the time- and temperature-dependent activation of receptor. The nucleotides GTP, ATP, ADP, CTP and UTP all promoted receptor activation; the effect of GTP was significantly greater than that of ATP. It is unlikely that phosphate donation is involved in receptor activation as the effects of GTP could be reproduced by p[NH]ppG (guanosine 5′-[β,γ-imido]triphosphate), while PPi was also effective in activating receptor. The results provide evidence for the distinct regulation of the oligonucleotide- and ligand-binding domains, since manipulations which promoted binding to oligo(dT) did not affect either ligand binding capacity or the rate constant and composition the biphasic dissociation of the ligand receptor complex.
KW - Binding site regulation
KW - Estrogen receptor
KW - Oligonucleotide
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U2 - 10.1016/0167-4889(85)90192-2
DO - 10.1016/0167-4889(85)90192-2
M3 - Article
C2 - 2986723
AN - SCOPUS:0021795675
SN - 0167-4889
VL - 845
SP - 304
EP - 310
JO - BBA - Molecular Cell Research
JF - BBA - Molecular Cell Research
IS - 2
ER -