Protein composition: Single subunit. To date, all TFIIB proteins are between 35 and 40 kilodaltons.
Features: A zinc finger domain at the N-terminus and a direct repeat in a proteolytically stable C-terminal domain.
Interactions: Binds directly to TBP, recruits RNA polymerase II, in part through an interaction with the small subunit of TFIIF. Several acidic activators can bind TFIIB in vitro.
Functions: Stabilizes TBP binding to TATA element. Required for association of RNA polymerase II to the initiation complex. May be a target for regulatory transcription factors.
Three views: Front, Side, and Top.
TATA-Binding Protein is shown in green, TFIIB in red.
Additional search terms can be typed into the boxes.