Evidence map›Paper›PMID 30446656›Full record

ArticleNature communications2018

Dna2 processes behind the fork long ssDNA flaps generated by Pif1 and replication-dependent strand displacement.

Silvia Emma Rossi, Marco Foiani, Michele Giannattasio

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 36 citations in OpenAlex.

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  11. Review
  12. Role and Regulation of Pif1 Family Helicases at the Replication Fork.International journal of molecular sciences · 2022
    Review
  13. Article
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  15. Article
  16. Review
  17. International journal of molecular sciences · 2021
    Review
  18. Article
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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

3 authors at 2 institutions in 1 country.

Silvia Emma RossiIFOM (Fondazione Istituto FIRC di Oncologia Molecolare), Via Adamello 16, Milan, 20139, Italy.
Marco FoianiIFOM (Fondazione Istituto FIRC di Oncologia Molecolare), Via Adamello 16, Milan, 20139, Italy. marco.foiani@ifom.eu.
Michele GiannattasioIFOM (Fondazione Istituto FIRC di Oncologia Molecolare), Via Adamello 16, Milan, 20139, Italy. michele.giannattasio@ifom.eu.ORCID http://orcid.org/0000-0001-7099-5718
University of Milan · ITIFOM · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dna2 is a DNA helicase-endonuclease mediating DSB resection and Okazaki fragment processing. Dna2 ablation is lethal and rescued by inactivation of Pif1, a helicase assisting Okazaki fragment maturation, Pol32, a DNA polymerase δ subunit, and Rad9, a DNA damage response (DDR) factor. Dna2 counteracts fork reversal and promotes fork restart. Here we show that Dna2 depletion generates lethal DNA structures activating the DDR. While PIF1 deletion rescues the lethality of Dna2 depletion, RAD9 ablation relieves the first cell cycle arrest causing genotoxicity after few cell divisions. Slow fork speed attenuates DDR in Dna2 deprived cells. Electron microscopy shows that Dna2-ablated cells accumulate long ssDNA flaps behind the forks through Pif1 and fork speed. We suggest that Dna2 offsets the strand displacement activity mediated by the lagging strand polymerase and Pif1, processing long ssDNA flaps to prevent DDR activation. We propose that this Dna2 function has been hijacked by Break Induced Replication in DSB processing.

Indexed as

DNA ReplicationGene Expression Regulation, FungalRecombinational DNA RepairCell Cycle CheckpointsCell Cycle ProteinsDNA Breaks, Single-StrandedDNA-Directed DNA PolymeraseDNA HelicasesDNA, Single-StrandedGenes, LethalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCell Cycle ProteinsDNA2 protein, S cerevisiaeDNA-Directed DNA PolymeraseDNA HelicasesDNA, Single-StrandedPIF1 protein, S cerevisiaePol32 protein, S cerevisiaerad9 proteinSaccharomyces cerevisiae Proteins

Identifiers

PMID30446656
PMCPMC6240037
OpenAlexW2901867021

What OpenQuestion holds

Textmetadata
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.