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. 2014 Mar 20;42(9):5830–5845. doi: 10.1093/nar/gku214

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© The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 3. — Polymerase activity and fidelity of human PrimPol. (A) Human PrimPol was incubated with dNTPs and substrate at 1, 3, 5 and 30 min time points. PrimPol was proficient at extending an undamaged oligonucleotide template using dNTPs. Human PrimPol did not require an intact zinc finger in order to carry out primer extension, as evidenced by the extension of primers by PrimPol_ZF-KO and PrimPol_1–354. PrimPol_1–487 that lacked the unstructured C-terminus of the protein was also polymerase proficient. PrimPol_1–354 exhibited a higher rate of polymerase activity compared to the other constructs. (B) Incorporation of nucleotides opposite two templating cytosine bases. PrimPol was incubated for 5 min with the DNA substrate and each of the dNTPs. All four of these PrimPol constructs inserted two guanine nucleotides opposite two cytosines in Watson–Crick base-pairing manner. PrimPol_1–354 could additionally incorporate a single adenine opposite the first cytosine.