DNA polymerase epsilon interacts with proliferating cell nuclear antigen in primer recognition and elongation.

Biochemistry (1995), Volume 34, Page 891

Abstract:

Kinetic analysis of DNA polymerase epsilon in its interaction with the homopolymeric template-primer poly(dA)/oligo(dT) and a singly-primed synthetic oligonucleotide of defined sequence indicated that primer utilization is inhibited by single-stranded DNA. Long single-stranded DNA regions appear to sequester DNA polymerase epsilon via nonproductive binding, thus reducing its catalytic efficiency. Proliferating cell nuclear antigen can reduce this nonproductive effect by increasing the rate of primer binding by DNA polymerase epsilon. Once the complex between DNA polymerase epsilon and the primer is formed, proliferating cell nuclear antigen can increase the rate of nucleotide incorporation. The results suggested a dual role of proliferating cell nuclear antigen in stimulating the activity of DNA polymerase epsilon, namely, first to facilitate primer binding and second to stimulate the synthetic activity itself. A model for the interaction between these two proteins in DNA synthesis is discussed.

Polymerases:

Topics:

Status:

new topics/pols set partial results complete validated

Results:

No results available for this paper.

Entry validated by:

Log in to edit reference All References

Using Polbase tables:

Sorting:

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).

Filtering:

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.