Evidence map›Paper›PMID 39797730›Full record

ArticleNucleic acids research2025

A mobile genetic element-derived primase-polymerase harbors multiple activities implicated in DNA replication and repair.

Pan Fu, Yuwei Wang, Yanqiu Liu, Zhenhao Han, Zhangzhong Peng, Linfeng Liu, Wenyuan Han

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nucleic acids research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Article
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

7 authors.

Pan FuState Key Laboratory of Agricultural Microbiology and College of Life Science and Technology, Hubei Hongshan Laboratory, Huazhong Agricultural University, Shizishan Road No.1, Hongshan District, 430070 Wuhan, China.
Yuwei WangState Key Laboratory of Agricultural Microbiology and College of Life Science and Technology, Hubei Hongshan Laboratory, Huazhong Agricultural University, Shizishan Road No.1, Hongshan District, 430070 Wuhan, China.
Yanqiu LiuState Key Laboratory of Agricultural Microbiology and College of Life Science and Technology, Hubei Hongshan Laboratory, Huazhong Agricultural University, Shizishan Road No.1, Hongshan District, 430070 Wuhan, China.
Zhenhao HanState Key Laboratory of Agricultural Microbiology and College of Life Science and Technology, Hubei Hongshan Laboratory, Huazhong Agricultural University, Shizishan Road No.1, Hongshan District, 430070 Wuhan, China.
Zhangzhong PengState Key Laboratory of Agricultural Microbiology and College of Life Science and Technology, Hubei Hongshan Laboratory, Huazhong Agricultural University, Shizishan Road No.1, Hongshan District, 430070 Wuhan, China.
Linfeng LiuState Key Laboratory of Agricultural Microbiology and College of Life Science and Technology, Hubei Hongshan Laboratory, Huazhong Agricultural University, Shizishan Road No.1, Hongshan District, 430070 Wuhan, China.
Wenyuan HanState Key Laboratory of Agricultural Microbiology and College of Life Science and Technology, Hubei Hongshan Laboratory, Huazhong Agricultural University, Shizishan Road No.1, Hongshan District, 430070 Wuhan, China.ORCID 0000-0002-9636-6415

Funding

Foundation of Hubei Hongshan Laboratory 2021hszd022Fundamental Research Funds for Central Universities of China 2662020SKPY001National Key Research and Development Program of China 2022YFA0912200National Natural Science Foundation of China 31970545Natural Science Foundation of Hubei Province 2024AFB193
6 · The paper itself

Abstract

Primase-polymerases (PrimPols) play divergent functions from DNA replication to DNA repair in all three life domains. In archaea and bacteria, numerous and diverse PPs are encoded by mobile genetic elements (MGEs) and act as the replicases for their MGEs. However, their varying activities and functions are not fully understood. In this study, we characterized a group of PrimPols that are genetically associated with prokaryotic argonaute proteins (pAgos). The pAgo-associated PrimPol (AgaPP) is likely derived from a MGE. AgaPP has polymerase and primase activities and physically interacts with a helicase encoded by its downstream gene, suggesting that they constitute a functional replication module. Further, AgaPP performs translesion DNA synthesis, terminal transfer and microhomology-mediated end joining (MMEJ), showing striking similarity to human DNA repair polymerase θ. AgaPP can promote the MMEJ repair of Cas9-induced double-stranded DNA breaks and increase cell survival post DNA damage in Escherichia coli. In addition, the MMEJ activity of AgaPP can be repurposed to assist DNA assembly in vitro. Together, the findings reveal dual role of AgaPP in both DNA replication and repair.

Indexed as

DNA-Directed DNA PolymeraseDNA PrimaseDNA RepairDNA ReplicationInterspersed Repetitive SequencesArgonaute ProteinsDNA End-Joining RepairDNA HelicasesEscherichia coliHumansArgonaute ProteinsDNA-Directed DNA PolymeraseDNA HelicasesDNA Primase

Identifiers

PMID39797730
PMCPMC11724360

What Socratic holds

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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 Socratic graph.