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- W2110934545 abstract "Gene activators contain activation domains that are thought to recruit limiting components of the transcription machinery to a core promoter. VP16, a viral gene activator, has served as a model for studying the mechanistic aspects of transcriptional activation from yeast to human. The VP16 activation domain can be divided into two modules—an N-terminal subdomain (VPN) and a C-terminal subdomain (VPC). This study demonstrates that VPC stimulates core promoters that are either independent or dependent on TAFs (TATA-box Binding Protein-Associated Factors). In contrast, VPN only activates the TAF-independent core promoter and this activity increases in a synergistic fashion when VPN is dimerized (VPN2). Compared to one copy of VPN (VPN1), VPN2 also displays a highly cooperative increase in binding hTFIIB. The increased TFIIB binding correlates with VPN2's increased ability to recruit a complex containing TFIID, TFIIA and TFIIB. However, VPN1 and VPN2 do not increase the assembly of a complex containing only TFIID and TFIIA. The VPN subdomain also facilitates assembly of a complex containing TBP:TFIIA:TFIIB, which lacks TAFs, and provides a mechanism that could function at TAF-independent promoters. Taken together, these results suggest the interaction between VPN and TFIIB potentially initiate a network of contacts allowing the activator to indirectly tether TFIID or TBP to DNA." @default.
- W2110934545 created "2016-06-24" @default.
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- W2110934545 date "2004-07-16" @default.
- W2110934545 modified "2023-09-27" @default.
- W2110934545 title "TFIIB-facilitated recruitment of preinitiation complexes by a TAF-independent mechanism" @default.
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- W2110934545 doi "https://doi.org/10.1093/nar/gkh711" @default.
- W2110934545 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/506799" @default.
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- W2110934545 hasPublicationYear "2004" @default.
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