English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

The humanDINB1 gene shares a high degree of homology with theEscherichia coli dinB gene. Here, we purify thehDINB1- 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 acis-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.

The human DINB1 gene encodes the DNA polymerase Polθ