The loosely bound non-histone chromosomal proteins of rat prostate in androgen action.

Rat prostatic chromatin was fractionated by sequential salt extractions into 0.35 M NaCl-soluble (the loosely bound non-histone chromosomal proteins), 2 M NaCl-soluble and -insoluble (the residual proteins) fractions. Homologous and heterologous chromatins were reconstituted with these chromosomal fractions from castrated rats injected with testosterone for 2 h and from castrated control. Chromatin reconstituted with all hormone-treated fractions showed 30% more binding with polylysine and transcriptional template activity than did chromatin reconstituted with castrated fractions. Similar analyses of reconstituted heterologous chromatins indicated that the androgen-induced changes in chromatin were mainly determined by the androgenic state of the 0.35 M NaCl-soluble fraction. The 0.35 M NaCl-soluble fraction also contained 18% more total high mobility group protein than did the corresponding castrated fraction. Limited digestion of 5 alpha-[3H]dihydrotestosterone-bound nuclei with pancreatic DNAase 1 to 5% acid-soluble resulted in a rapid release of the nuclear-bound 3H-labelled androgen and protein, in contrast to similar digestion with microsomal nuclease. Since a large portion of the translocation androgen-receptor is bound to protein(s) in the 0.35 M NaCl-soluble fraction, these results suggest that the component(s) in the 0.35 M NaCl-soluble fraction to which androgen-receptor binds is associated with actively transcribing sequences on chromatin.