Evidence map›Paper›PMID 27311885›Full record

ArticleeLife2016

Polymerase θ is a robust terminal transferase that oscillates between three different mechanisms during end-joining.

Tatiana Kent, Pedro A Mateos-Gomez, Agnel Sfeir, Richard T Pomerantz

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
5.9field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

72 citing papers in PubMed, 105 citations in OpenAlex.

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  13. The Evolutionary Potential of Chromoanagenesis.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
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  18. Review
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  20. Article

12 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

Tatiana KentFels Institute for Cancer Research, Temple University Lewis Katz School of Medicine, Philadelphia, United States.
Pedro A Mateos-GomezSkirball Institute of Biomolecular Medicine, New York University School of Medicine, New York, United States.
Agnel SfeirSkirball Institute of Biomolecular Medicine, New York University School of Medicine, New York, United States.
Richard T PomerantzFels Institute for Cancer Research, Temple University Lewis Katz School of Medicine, Philadelphia, United States.ORCID 0000-0003-1194-9871
New York University · USTemple University · US

Funding

WORD PROCESSING CENTER--COREP30CA006927 · NCI · RESEARCH INST OF FOX CHASE CAN CTR · PI Margaret von Mehren · 1985 to 2026
$138.8M
Mechanisms of Mammalian Double-Strand Break RepairR01GM115472 · NIGMS · THOMAS JEFFERSON UNIVERSITY · PI POMERANTZ, RICHARD T · 2015 to 2019
$1.6M
Mechanisms and Regulation of Human Translesion DNA PolymerasesR00CA160648 · NCI · TEMPLE UNIV OF THE COMMONWEALTH · PI POMERANTZ, RICHARD T · 2013 to 2015
$724k
NCI NIH HHS P30 CA006927NCI NIH HHS R00 CA160648NIGMS NIH HHS R01 GM115472
6 · The paper itself

Abstract

DNA polymerase θ (Polθ) promotes insertion mutations during alternative end-joining (alt-EJ) by an unknown mechanism. Here, we discover that mammalian Polθ transfers nucleotides to the 3' terminus of DNA during alt-EJ in vitro and in vivo by oscillating between three different modes of terminal transferase activity: non-templated extension, templated extension in cis, and templated extension in trans. This switching mechanism requires manganese as a co-factor for Polθ template-independent activity and allows for random combinations of templated and non-templated nucleotide insertions. We further find that Polθ terminal transferase activity is most efficient on DNA containing 3' overhangs, is facilitated by an insertion loop and conserved residues that hold the 3' primer terminus, and is surprisingly more proficient than terminal deoxynucleotidyl transferase. In summary, this report identifies an unprecedented switching mechanism used by Polθ to generate genetic diversity during alt-EJ and characterizes Polθ as among the most proficient terminal transferases known.

Indexed as

DNA End-Joining RepairAnimalsCoenzymesDNADNA-Directed DNA PolymeraseDNA NucleotidylexotransferaseDNA Polymerase thetaEmbryonic Stem CellsManganeseMiceCoenzymesDNADNA-Directed DNA PolymeraseDNA NucleotidylexotransferaseDNA Polymerase thetaManganesealternative end-JoiningbiochemistrychromosomesDNA polymeraseDNA repairgenesgenetic diversitygenetic instabilityhumanmicrohomology-mediated end-joiningmouse

Identifiers

PMID27311885
PMCPMC4912351
OpenAlexW2429819149

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.