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)|
|Number of pages||6|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|State||Published - Apr 11 2000|
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