The binding of androgen receptor to DNA and RNA.
The androgen receptor from mouse kidney cytosol has been studied for its nucleic acid binding properties by DNA-cellulose centrifugation assay. The receptor appears to bind to RNA (mRNA, tRNA, rRNA) as well as to DNA. Salt and heat activation of the androgen receptor enhances both DNA and RNA binding. The receptor binds slightly better to denatured DNA than to native DNA. The androgen receptor binds about 2-fold tighter to poly(dG-dC) than to poly (dA-dT). The interaction of the receptor with DNA is not greatly affected by the BrdUrd substitution. The observation that androgen receptor shows a significant affinity to RNA may imply that androgen receptor-RNA interaction could play a role in gene regulation.
D000818:Animals; D003600:Cytosol / Q000378:metabolism; D004247:DNA / Q000378:metabolism*; D013196:Dihydrotestosterone / Q000378:metabolism; D005260:Female; D066298:In Vitro Techniques; D007668:Kidney / Q000378:metabolism; D008297:Male; D051379:Mice; D008815:Mice, Inbred Strains; D011067:Poly dA-dT / Q000378:metabolism; D011089:Polydeoxyribonucleotides / Q000378:metabolism; D012313:RNA / Q000378:metabolism*; D011944:Receptors, Androgen / Q000378:metabolism*; D011987:Receptors, Steroid / Q000378:metabolism*
D011089:Polydeoxyribonucleotides; D011944:Receptors, Androgen; D011987:Receptors, Steroid; D013196:Dihydrotestosterone; D011067:Poly dA-dT; C019530:poly(dC-dG); D012313:RNA; D004247:DNA