Clamping the TBP stirrup

Article Abstract:

The interaction of the transcription factor TFIIB with TATA-binding protein (TBP) and DNA stimulates RNA polymerase II, which in turn initiates the transcription of RNA. The carboxy-terminal core of TFIIB binds to the DNA backbone. Since this binding is asymmetrical, transcription is in one direction only. Despite the failure of the binding of TFIIB to the TBP-DNA complex to alter the structure of the complex, the conformation of bound and unbound TFIIB is different.

Observations, Genetic regulation, Protein binding, DNA-ligand interactions, DNA binding

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Model for binding of transcription factor TFIIB to the TBP-DNA complex

Article Abstract:

Gel mobility-shift assays and hydroxyl-radical footprinting can be used to determine the binding mechanism of transcription factor TFIIB to the TBP-DNA complex. The formation of a TFIIB-TBP-DNA complex was reasonably easy due to the TATA boxes in each probe but stable complexes required a minimum of seven bases of DNA upstream or downstream from the TATA boxes. TFIIB was shown to be a monomer of great length, allowing it to interact with both ends of bent DNA.

DNA binding proteins

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A transcription reinitiation intermediate that is stabilized by activator

Article Abstract:

Research into reinitiation intermediates for gene transcription by RNA polymerase II is presented. A model is presented for isolation of a reinitiation intermediate which forms a stable scaffold.

RNA polymerases, Letter to the Editor

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