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J. Biol. Chem., Vol. 277, Issue 50, 48366-48371, December 13, 2002
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,,§, and¶
From the We have used the chromatin immunoprecipitation
technique to analyze the formation of the androgen receptor (AR)
transcription complex onto prostate-specific antigen (PSA) and
kallikrein 2 promoters in LNCaP cells. Our results show that loading of
holo-AR and recruitment of RNA polymerase II to the promoters occur
transiently. The cyclic nature of AR transcription complex assembly is
also illustrated by transient association of coactivators GRIP1 and CREB-binding protein and acetylated histone H3 with the PSA promoter. Treatment of cells with the pure antiandrogen bicalutamide also elicits
occupancy of the promoter by AR. In contrast to the agonist-liganded AR, bicalutamide-bound receptor is not capable of recruiting polymerase II, GRIP1, or CREB-binding protein, indicating that the conformation of
AR bound to anti-androgen is not competent to assemble transcription complexes. Proteasome is involved in the regulation of
AR-dependent transcription, as a proteasome inhibitor,
MG-132, prevents the release of the receptor from the PSA promoter, and
it also blocks the androgen-induced PSA mRNA accumulation.
Furthermore, occupancy of the PSA promoter by the 19 S proteasome
subcomplex parallels that by AR. Collectively, formation of the AR
transcription complex, encompassing AR, polymerase II, and
coactivators, on a regulated promoter is a cyclic process involving
proteasome function.
Biomedicum Helsinki, Institute of
Biomedicine (Physiology), the ¶ Institute of Biotechnology, and
the § Department of Clinical Chemistry, University of
Helsinki and Helsinki University Central Hospital,
FIN-00014 Helsinki, Finland
To whom correspondence should be addressed: Biomedicum
Helsinki, Institute of Biomedicine, Rm. C103b, P. O. Box 63 (Haartmaninkatu 8), University of Helsinki, FIN-00014 Helsinki,
Finland. Tel.: 358-9-191-25291; Fax: 358-9-191-25302; E-mail:
jorma.palvimo@helsinki.fi.
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