Purification and characterization of a DNA polymerase beta promoter initiator element-binding transcription factor from bovine testis.


A low-abundance DNA-binding protein for the DNA polymerase beta ...
A low-abundance DNA-binding protein for the DNA polymerase beta (beta-pol) promoter initiator element was purified from bovine testis. The transcriptional initiator element (Inr) of the mammalian beta-pol promoters characterized is highly conserved, and the bovine beta-pol promoter Inr has the sequence -11CAGAGGCGGCCATTGTT+6. The purified initiator element-binding protein (Inr-BP) binds with high affinity to an oligonucleotide corresponding to the beta-pol promoter Inr (Kd = 5 pM), and increasing ionic strength decreases stability of the protein-DNA complex. Mutational analysis of the Inr shows that the purified Inr-BP binds with sequence specificity to the sequence CCAT at -2 to +2 of the Inr, but that seven residues on the 5' side and three residues on the 3' side of the CCAT sequence are required also. Using an in vitro transcription assay with HeLa cell nuclear extract, we find that the endogenous Inr-BP is required for transcriptional activity of the beta-pol promoter; addition of purified Inr-BP restores activity to the nuclear extract depleted in Inr-BP by affinity chromatography. These results, based upon the sequence specificity for DNA binding, indicate that Inr-BP is a YY1-like protein and suggest that it is a required transcription factor in beta-pol gene expression.




new topics/pols set partial results complete validated


No results available for this paper.

Entry validated by:

Using Polbase tables:


Tables may be sorted by clicking on any of the column titles. A second click reverses the sort order. <Ctrl> + click on the column titles to sort by more than one column (e.g. family then name).


It is also possible to filter the table by typing into the search box above the table. This will instantly hide lines from the table that do not contain your search text.