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Article

Activator-induced conformational change in general transcription factor TFIIB.

Nature - 20 Oct 1994

Roberts S G, Green M R

Abstract excerpt

Transcriptional activator proteins (activators) function, at least in part, by increasing preinitiation complex assembly (for reviews see refs 1-4). Previous studies have shown that an acidic activator forms a contact with the general transcription factor TFIIB (refs 5-7) and recruits it into the preinitiation complex. Mutational studies indicate that this interaction between the acidic activator and TFIIB is...

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PMID: 7935820
DOI: 10.1038/371717a0

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Activator-induced conformational change in general transcription factor TFIIB.PMID 7935820Read ↗

Interaction between an acidic activator and transcription factor TFIIB is required for transcriptional activation.Semantic proximity Read ↗

A role for activator-mediated TFIIB recruitment in diverse aspects of transcriptional regulation.Semantic proximity Read ↗

Activator-mediated disruption of sequence-specific DNA contacts by the general transcription factor TFIIB.Semantic proximity Read ↗

Core promoter-dependent TFIIB conformation and a role for TFIIB conformation in transcription start site selection.Semantic proximity Read ↗

Transcription factor IIB acetylates itself to regulate transcription.Semantic proximity Read ↗

Transcriptional activation by TFIIB mutants that are severely impaired in interaction with promoter DNA and acidic activation domains.Semantic proximity Read ↗

Design principles of acidic transcriptional activation domainsSemantic proximity Read ↗

The linker domain of basal transcription factor TFIIB controls distinct recruitment and transcription stimulation functions.Semantic proximity Read ↗

Structural insight into the TFIIE-TFIIH interaction: TFIIE and p53 share the binding region on TFIIH.Semantic proximity Read ↗

The ETS family member ERM contains an alpha-helical acidic activation domain that contacts TAFII60.Semantic proximity Read ↗

xUBF contains a novel dimerization domain essential for RNA polymerase I transcription.Semantic proximity Read ↗

Assembly of transcription factor IIB at a promoter in vivo requires contact with RNA polymerase II.Semantic proximity Read ↗

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