TATA BOX-BINDING PROTEIN (TBP) IS A CONSTITUENT OF THE POLYMERASE I-SPECIFIC TRANSCRIPTION INITIATION-FACTOR TIF-IB (SL1) BOUND TO THE RIBOSOMAL-RNA PROMOTER AND SHOWS DIFFERENTIAL SENSITIVITY TO TBP-DIRECTED REAGENTS IN POLYMERASE-I, POLYMERASE-II, AND POLYMERASE-III TRANSCRIPTION FACTORS
Ca. Radebaugh et al., TATA BOX-BINDING PROTEIN (TBP) IS A CONSTITUENT OF THE POLYMERASE I-SPECIFIC TRANSCRIPTION INITIATION-FACTOR TIF-IB (SL1) BOUND TO THE RIBOSOMAL-RNA PROMOTER AND SHOWS DIFFERENTIAL SENSITIVITY TO TBP-DIRECTED REAGENTS IN POLYMERASE-I, POLYMERASE-II, AND POLYMERASE-III TRANSCRIPTION FACTORS, Molecular and cellular biology, 14(1), 1994, pp. 597-605
The role of the Acanthamoeba castellanii TATA-binding protein (TBP) in
transcription was examined. Specific antibodies against the nonconser
ved N-terminal domain of TBP were used to verify the presence of TBP i
n the fundamental transcription initiation factor for RNA polymerase I
, TIF-IB, and to demonstrate that TBP is part of the committed initiat
ion complex on the rRNA promoter. The same antibodies inhibit transcri
ption in all three polymerase systems, but they do so differentially.
Oligonucleotide competitors were used to evaluate the accessibility of
the TATA-binding site in TIF-IB, TFIID, and TFIIIB. The results sugge
st that insertion of TBP into the polymerase II and III factors is mor
e similar than insertion into the polymerase I factor.