Interaction of human RNA polymerase II with the TATA-binding protein

Preincubation of human RNA polymerase II with P-32-labeled oligonucleotides containing the TATA element of the promoter of the human beta-actin gene followed by incubation with the TATA-binding protein in increasing concentrations leads to a proportional drop in the amount of complexes of RNA polymerase II with the oligonucleotides. Preincubation of RNA polymerase II with increasing concentrations of TATA-binding protein followed by incubation with equal amounts of a phosphoramide derivative of P-32-oligonucleotide containing a TATA element showed that as the TATA-binding protein concentration increases, the amount of covalent complexes of RNA polymerase II with the oligonucleotide derivative diminishes. These results imply displacement of TATA-containing oligonucleotides by the TATA-binding protein from complexes with RNA polymerase.