Evidence map›Paper›PMID 27819052›Full record

ArticleScience advances2016

Structure and mechanism of human PrimPol, a DNA polymerase with primase activity.

Olga Rechkoblit, Yogesh K Gupta, Radhika Malik, Kanagalaghatta R Rajashankar, Robert E Johnson, Louise Prakash, Satya Prakash, Aneel K Aggarwal

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

55 citing papers in PubMed, 82 citations in OpenAlex.

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  7. Mouse PrimPol Outperforms Its Human Counterpart as a Robust DNA Primase.International journal of molecular sciences · 2025
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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

8 authors at 3 institutions in 1 country.

Olga RechkoblitDepartment of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, Box 1677, 1425 Madison Avenue, New York, NY 10029, USA.ORCID 0000-0003-4270-7242
Yogesh K GuptaDepartment of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, Box 1677, 1425 Madison Avenue, New York, NY 10029, USA.ORCID 0000-0001-6372-5007
Radhika MalikDepartment of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, Box 1677, 1425 Madison Avenue, New York, NY 10029, USA.
Kanagalaghatta R RajashankarDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.; Northeastern Collaborative Access Team, Advanced Photon Source, Argonne National Laboratory, Argonne, IL 60439, USA.
Robert E JohnsonDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch, 301 University Boulevard, Galveston, TX 77755-1061, USA.ORCID 0000-0002-6809-7123
Louise PrakashDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch, 301 University Boulevard, Galveston, TX 77755-1061, USA.
Satya PrakashDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch, 301 University Boulevard, Galveston, TX 77755-1061, USA.
Aneel K AggarwalDepartment of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, Box 1677, 1425 Madison Avenue, New York, NY 10029, USA.
Icahn School of Medicine at Mount Sinai · USThe University of Texas Medical Branch at Galveston · USArgonne National Laboratory · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
NCRR NIH HHS S10 RR029205NIGMS NIH HHS P41 GM103403
6 · The paper itself

Abstract

PrimPol is a novel human enzyme that contains both DNA primase and DNA polymerase activities. We present the first structure of human PrimPol in ternary complex with a DNA template-primer and an incoming deoxynucleoside triphosphate (dNTP). The ability of PrimPol to function as a DNA primase stems from a simple but remarkable feature-almost complete lack of contacts to the DNA primer strand. This, in turn, allows two dNTPs to bind initiation and elongation sites on the enzyme for the formation of the first dinucleotide. PrimPol shows the ability to synthesize DNA opposite ultraviolet (UV) lesions; however, unexpectedly, the active-site cleft of the enzyme is constrained, which precludes the bypass of UV-induced DNA lesions by conventional translesion synthesis. Together, the structure addresses long-standing questions about how DNA primases actually initiate synthesis and how primase and polymerase activities combine in a single enzyme to carry out DNA synthesis.

Indexed as

DNADNA-Directed DNA PolymeraseDNA PrimaseDNA RepairHumansMultifunctional EnzymesProtein DomainsStructure-Activity RelationshipUltraviolet RaysDNADNA-Directed DNA PolymeraseDNA PrimaseMultifunctional EnzymesPrimPol protein, humanDNA polymeraseDNA repairDNA replicationgenomic stability

Identifiers

PMID27819052
PMCPMC5088642
OpenAlexW2537276668

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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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.