The effect of mononucleotides on the cytosolic rat liver glucocorticoid receptor has been studied by the use of aqueous dextran-poly(ethylene glycol) two-phase partitioning. During incubations in 0.4 M KCl at 0 degrees C, millimolar concentrations of ADP and ATP, but not AMP, CTP, UTP and GTP, inhibit the increase in the receptor partition coefficient associated with receptor activation. This inhibition is counteracted by millimolar concentrations of theophylline and MgCl2. Two nonhydrolyzable analogues of ATP, alpha, beta-Methyleneadenosine 5'-triphosphate and beta, gamma-methyleneadenosine 5'-triphosphate, also inhibit the increase in the partition coefficient. alpha, beta-Methyleneadenosine 5'-triphosphate is much more potent than ATP in doing so, and this compound was also shown to reduce the amount of receptor to bind to DNA-Sepharose after the incubations. Thus, adenine nucleotides induce a change in the state of the receptor, apparently consisting in an inhibition of receptor activation.
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