|
|
|
| Untersuchte Arbeit: Seite: 14, Zeilen: 1 ff. (entire page) |
Quelle: SABiosciences Androgen Signaling 2009 Seite(n): online, Zeilen: - |
|---|---|
| PIAS (Protein Inhibitor of Activated Signal Transducer and Activator of Transcription STAT) family of proteins and ANPK ( Androgen Receptor-Interacting Nuclear Kinase) play major function. Transcriptional activation by AR ultimately requires the recruitment of RNA Pol II( RNA polymerase II) to the promoter of target genes. RNA Pol II recruitment is mediated through the assembly of GTFs (General Transcription Factor)to form the pre-initiation complex, the first step of which is the binding of TBP (TATA box-Binding Protein)near the transcriptional start site . TBP is part of multiprotein complex, the first step of which is the binding of TBP near the transcriptional start site. TBP is part of multiprotein complex which includes TFIID (Transcriptional Factor –IID) that induces DNA bending , bringing sequences upstream of the TATA element in closer proximity, and presumably enabling interaction between GTFs and steroid receptor-coregulators complexes. TFIIB binds directly to TBP and recruits the TFIIF-RNA Pol II complex. TFIIF interacts with TFIIB and RNA Pol II and has a role in transcription initiation and elongation. | PIAS [Protein Inhibitor of Activated Signal Transducer and Activator of Transcription (STAT)] family of proteins and ANPK (Androgen Receptor-Interacting Nuclear Kinase) also interact with and coactivate AR. Transcriptional activation by AR ultimately requires the recruitment of RNA Pol II (RNA polymerase-II) to the promoter of target genes. RNA Pol II recruitment is mediated through the assembly of GTFs (General Transcription Factors) to form the preinitiation complex, the first step of which is the binding of TBP (TATA box-Binding Protein) near the transcriptional start site. TBP is part of a multiprotein complex, TFIID (Transcription Factor-IID), which also contains general and promoter-specific TAFII (TBP-Associated Factors) proteins. TBP binding induces DNA bending, bringing sequences upstream of the TATA element in closer proximity, presumably enabling interaction between GTFs and steroid receptor-coregulator complexes. TFIIB binds directly to TBP and functions to recruit the TFIIF-RNA Pol II complex. TFIIF domains, in addition to interacting with TFIIB and RNA Pol II, apparently also serve in transcription initiation and elongation. |
The source is not given. |
|