| Autor: |
Hiremath ST, Maciewicz RA, Wang TY |
| Jazyk: |
angličtina |
| Zdroj: |
Biochimica et biophysica acta [Biochim Biophys Acta] 1981 Mar 26; Vol. 653 (1), pp. 130-8. |
| DOI: |
10.1016/0005-2787(81)90111-8 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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