DNA and ribonucleotide binding characteristics of two forms of the androgen receptor from rat prostates.
Androgen receptors (sedimentation value approximately 4S and Stokes radius 2.8 nm) present in the cytoplasmic fraction obtained from prostates of castrated rats bind to DNA-Sepharose and double stranded DNA. A receptor fragment (sedimentation value approximately 3S and Stokes radius 2.3 nm) obtained from rat prostates in the course of a purification procedure showed greatly diminished binding affinity for both DNA-Sepharose and soluble DNA. In contrast, both the 4S cytosol receptor and the 3S receptor form interacted with equal affinity with prostate RNA or poly(UG). These observations provide evidence that for DNA binding a different or additional part of the receptor molecule is required than for RNA and polyribonucleotide binding.
D000818:Animals; D003593:Cytoplasm / Q000378:metabolism; D004247:DNA / Q000378:metabolism*; D008297:Male; D008970:Molecular Weight; D011467:Prostate / Q000378:metabolism*; D012313:RNA / Q000378:metabolism*; D051381:Rats; D011944:Receptors, Androgen / Q000378:metabolism*; D011987:Receptors, Steroid / Q000378:metabolism*
D011944:Receptors, Androgen; D011987:Receptors, Steroid; D012313:RNA; D004247:DNA