Evidence map›Paper›PMID 31799622›Full record

ArticleNucleic acids research2020

DSS1 interacts with and stimulates RAD52 to promote the repair of DSBs.

Barbora Stefanovie, Sarah R Hengel, Jarmila Mlcouskova, Jana Prochazkova, Mario Spirek, Fedor Nikulenkov, Daniel Nemecek, Brandon G Koch, Fletcher E Bain, Liping Yu and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

25 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Review
  3. Targeting RAD52 overcomes PARP inhibitor resistance in preclinicalbioRxiv : the preprint server for biology · 2025
    Article
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  19. Making Choices: DNA Replication Fork Recovery Mechanisms.Seminars in cell & developmental biology · 2021
    Review
  20. Single-Strand Annealing in Cancer.International journal of molecular sciences · 2021
    Review
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

12 authors at 4 institutions in 2 countries.

Barbora StefanovieDepartment of Biology, Masaryk University, 62500 Brno, Czech Republic.
Sarah R HengelDepartment of Biochemistry, University of Iowa Carver College of Medicine, 51 Newton Road, Iowa City, IA 52242, USA.
Jarmila MlcouskovaDepartment of Biology, Masaryk University, 62500 Brno, Czech Republic.
Jana ProchazkovaInternational Clinical Research Center, St. Anne's University Hospital in Brno, 62500 Brno, Czech Republic.
Mario SpirekDepartment of Biology, Masaryk University, 62500 Brno, Czech Republic.
Fedor NikulenkovInternational Clinical Research Center, St. Anne's University Hospital in Brno, 62500 Brno, Czech Republic.
Daniel NemecekCEITEC, Masaryk University, 62500 Brno, Czech Republic.
Brandon G KochDepartment of Biochemistry, University of Iowa Carver College of Medicine, 51 Newton Road, Iowa City, IA 52242, USA.
Fletcher E BainDepartment of Biochemistry, University of Iowa Carver College of Medicine, 51 Newton Road, Iowa City, IA 52242, USA.
Liping YuDepartment of Biochemistry, University of Iowa Carver College of Medicine, 51 Newton Road, Iowa City, IA 52242, USA.
Maria SpiesDepartment of Biochemistry, University of Iowa Carver College of Medicine, 51 Newton Road, Iowa City, IA 52242, USA.
Lumir KrejciDepartment of Biology, Masaryk University, 62500 Brno, Czech Republic.
University of Iowa · USSt. Anne's University Hospital Brno · CZMasaryk University · CZCentral European Institute of Technology – Masaryk University · CZ

Funding

Viral VectorP30CA086862 · NCI · UNIVERSITY OF IOWA · PI Christopher K Laubenthal · 2000 to 2026
$70.0M
The Role of Human RAD52 Protein in Genome StabilityR01CA232425 · NCI · UNIVERSITY OF IOWA · PI Maria Spies · 2019 to 2026
$3.1M
NCI NIH HHS P30 CA086862NCI NIH HHS R01 CA232425Wellcome Trust
6 · The paper itself

Abstract

The proper repair of deleterious DNA lesions such as double strand breaks prevents genomic instability and carcinogenesis. In yeast, the Rad52 protein mediates DSB repair via homologous recombination. In mammalian cells, despite the presence of the RAD52 protein, the tumour suppressor protein BRCA2 acts as the predominant mediator during homologous recombination. For decades, it has been believed that the RAD52 protein played only a back-up role in the repair of DSBs performing an error-prone single strand annealing (SSA). Recent studies have identified several new functions of the RAD52 protein and have drawn attention to its important role in genome maintenance. Here, we show that RAD52 activities are enhanced by interacting with a small and highly acidic protein called DSS1. Binding of DSS1 to RAD52 changes the RAD52 oligomeric conformation, modulates its DNA binding properties, stimulates SSA activity and promotes strand invasion. Our work introduces for the first time RAD52 as another interacting partner of DSS1 and shows that both proteins are important players in the SSA and BIR pathways of DSB repair.

Indexed as

BRCA2 ProteinCarcinogenesisDNA-Binding ProteinsDNA Breaks, Double-StrandedDNA RepairGenome, HumanGenomic InstabilityHomologous RecombinationHumansOsteosarcomaProteasome Endopeptidase ComplexProtein BindingRad52 DNA Repair and Recombination ProteinSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsBRCA2 ProteinBRCA2 protein, humanDNA-Binding ProteinsProteasome Endopeptidase ComplexRad52 DNA Repair and Recombination ProteinRAD52 protein, humanRAD52 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSEM1 protein, human

Identifiers

PMID31799622
PMCPMC6954417
OpenAlexW2993322295

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.