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Genes 2016, 7(9), 67; doi:10.3390/genes7090067

DNA Polymerase θ: A Unique Multifunctional End-Joining Machine

Fels Institute for Cancer Research, Department of Medical Genetics and Molecular Biochemistry, Temple University Lewis Katz School of Medicine, Philadelphia, PA 19140, USA
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Academic Editor: Paolo Cinelli
Received: 11 August 2016 / Revised: 2 September 2016 / Accepted: 8 September 2016 / Published: 21 September 2016
(This article belongs to the Special Issue Replication and Transcription Associated DNA Repair)
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Abstract

The gene encoding DNA polymerase θ (Polθ) was discovered over ten years ago as having a role in suppressing genome instability in mammalian cells. Studies have now clearly documented an essential function for this unique A-family polymerase in the double-strand break (DSB) repair pathway alternative end-joining (alt-EJ), also known as microhomology-mediated end-joining (MMEJ), in metazoans. Biochemical and cellular studies show that Polθ exhibits a unique ability to perform alt-EJ and during this process the polymerase generates insertion mutations due to its robust terminal transferase activity which involves template-dependent and independent modes of DNA synthesis. Intriguingly, the POLQ gene also encodes for a conserved superfamily 2 Hel308-type ATP-dependent helicase domain which likely assists in alt-EJ and was reported to suppress homologous recombination (HR) via its anti-recombinase activity. Here, we review our current knowledge of Polθ-mediated end-joining, the specific activities of the polymerase and helicase domains, and put into perspective how this multifunctional enzyme promotes alt-EJ repair of DSBs formed during S and G2 cell cycle phases. View Full-Text
Keywords: DNA polymerase; DNA repair; microhomology-mediated end-joining; alternative end-joining; replication repair; genome instability; cancer DNA polymerase; DNA repair; microhomology-mediated end-joining; alternative end-joining; replication repair; genome instability; cancer
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Black, S.J.; Kashkina, E.; Kent, T.; Pomerantz, R.T. DNA Polymerase θ: A Unique Multifunctional End-Joining Machine. Genes 2016, 7, 67.

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