The glucocorticoid receptor from @entity19 AtT-20 @entity977 cells exists in three forms. The largest form is an untransformed (non-DNA-binding), oligomeric species (9.1 S, 8.3 nm, Mr 319 000). Two transformed (DNA-binding) forms can be generated. One is an oligomeric protein (5.2 S, 6-8.3 nm, Mr 132 000-182 000), while the other is the monomeric, hormone-binding subunit (3.8 S, 6 nm, Mr 96 000). The composition of the oligomeric, transformed receptor and its relationship to the monomeric protein were examined. The 3.8S monomer can be isolated from DEAE-cellulose (0.12 M step elution) in a form that continues to sediment at about 3.8 S on @entity7051 -containing @entity969 gradients and at about 4.2 S on molybdate-free gradients. Addition of a non-hormone-binding component isolated from the same DEAE-cellulose column (0.5 M @entity4338 step) can apparently interact with the 3.8-4.2 S monomer, increasing its sedimentation coefficient to 5.2 S (on molybdate-containing gradients) or 6.6 S (on low-salt, molybdate-free gradients). This factor is a macromolecule (nondialyzable) and is heat-stable (100 degrees C, 20 min). A dose-dependent shift to the higher sedimentation coefficient is observed when increasing quantities of the 0.5 M step material are added to the receptor monomer. This activity is abolished when the 0.5 M step material is treated with ribonuclease A. Further, when RNA is purified from the 0.5 M step by @entity3971 / @entity3636 extraction, its ability to increase the S value of the monomer is retained. Ribonuclease treatment of the untransformed, 9.1S, oligomeric complex does not cause a significant decrease in sedimentation rate, while the same treatment of the 5.2S, oligomeric, transformed receptor (obtained after Sephadex G-25 transformation) causes a decrease in sedimentation rate to about 3.8 S. The addition of @entity291 liver mRNA and rRNA does not cause a shift in sedimentation rate of the receptor monomer to a discrete, higher sedimenting receptor form. However, the addition of total @entity95 liver tRNA or three distinct tRNA species causes a shift in sedimentation to a similar, but not identical, form as that with the 0.5 M step material. We propose that the 5.2S, oligomeric transformed glucocorticoid receptor is composed of one monomeric hormone-binding, protein subunit (Mr 96 000) and a low molecular weight RNA (Mr 36 000). This interaction may be important for the role of the receptor in regulating gene expression.

Ribonucleic acid is a component of the oligomeric, transformed XXXX AtT-20 cell glucocorticoid receptor.

@entity19 :: ('10090', 'Species') :: ['mouse'] @entity3636 :: ('MESH:D002725', 'Chemical') :: ['chloroform'] @entity95 :: ('9986', 'Species') :: ['rabbit'] @entity3971 :: ('MESH:D019800', 'Chemical') :: ['phenol'] @entity969 :: ('MESH:D013395', 'Chemical') :: ['sucrose'] @entity977 :: ('MESH:D010911', 'Disease') :: ['pituitary tumor'] @entity7051 :: ('MESH:C044659', 'Chemical') :: ['molybdate'] @entity291 :: ('9913', 'Species') :: ['bovine'] @entity4338 :: ('CHEBI:32588', 'Chemical') :: ['KCl']
@entity19 :: (10090,Species) :: ['mouse']
