Ribonucleic acid association with androgen receptor from rat submandibular gland.
The transformed androgen receptor from rat submandibular gland converts to a faster sedimenting form (6-8S) on a glycerol gradient centrifugation after withdrawal of a transformation-inducing reagent (KCl or ATP). In this report, the association of cytosolic RNA with the transformed androgen receptor was investigated as a possible mechanism of molecular conversion of the androgen receptor. When the transformed and converted androgen receptors were treated with RNase A, these receptors sedimented at 4.5S in a low-salt glycerol gradient. Addition of RNA from rat submandibular gland to the RNase-Sepharose-treated transformed receptor caused a shift of receptor peak from 4.5S to 5.8S. RNA from rat submandibular gland, yeast RNA and E. coli rRNA inhibited DNA-cellulose binding of a RNase-treated transformed receptor in the absence of molybdate. These observations suggest that conversion from the transformed 4S androgen receptor to a 6-8S form resulted from the association of RNA(s) with the transformed receptor.
D000818:Animals; D004268:DNA-Binding Proteins / Q000502:physiology; D005260:Female; D012313:RNA / Q000378:metabolism* / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains; D011944:Receptors, Androgen / Q000187:drug effects / Q000378:metabolism* / Q000502:physiology; D012259:Ribonuclease, Pancreatic / Q000494:pharmacology; D012685:Sepharose / Q000494:pharmacology; D013363:Submandibular Gland / Q000378:metabolism*
D004268:DNA-Binding Proteins; D011944:Receptors, Androgen; D012313:RNA; D012685:Sepharose; D012259:Ribonuclease, Pancreatic