Abstract
The human DINB1 gene shares a high degree of homology with the Escherichia coli dinB gene. Here, we purify the hDINB1-encoded protein and show that it is a DNA polymerase. Because hDinB1 is the eighth eukaryotic DNA polymerase to be described, we have named it DNA polymerase (Pol) θ. hPolθ is unable to bypass a cis-syn thymine-thymine dimer, nor does it bypass a (6- 4) photoproduct or an abasic site. We also examine the fidelity of hPolθ on nondamaged DNA templates by steady-state kinetic analyses and find that hPolθ misincorporates deoxynucleotides with a frequency of about 10-3 to 10-4. We discuss the relationship between the fidelity of hPolθ and its inability to bypass DNA damage.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 3838-3843 |
| Number of pages | 6 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Volume | 97 |
| Issue number | 8 |
| DOIs | |
| State | Published - Apr 11 2000 |
ASJC Scopus subject areas
- General
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