Evidence map›Paper›PMID 35115525›Full record

ArticleNature communications2022

The toposiomerase IIIalpha-RMI1-RMI2 complex orients human Bloom's syndrome helicase for efficient disruption of D-loops.

Gábor M Harami, János Pálinkás, Yeonee Seol, Zoltán J Kovács, Máté Gyimesi, Hajnalka Harami-Papp, Keir C Neuman, Mihály Kovács

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.6field-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

10 citing papers in PubMed, 21 citations in OpenAlex.

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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 2 institutions in 2 countries.

Gábor M Harami *ELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány P. s. 1/c, H-1117, Budapest, Hungary. gabor.harami@ttk.elte.hu.ORCID 0000-0001-7234-2710
János Pálinkás *ELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány P. s. 1/c, H-1117, Budapest, Hungary.
Yeonee SeolLaboratory of Single Molecule Biophysics, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland, 20892, USA.
Zoltán J KovácsELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány P. s. 1/c, H-1117, Budapest, Hungary.
Máté GyimesiELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány P. s. 1/c, H-1117, Budapest, Hungary.
Hajnalka Harami-PappELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány P. s. 1/c, H-1117, Budapest, Hungary.
Keir C NeumanLaboratory of Single Molecule Biophysics, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland, 20892, USA.
Mihály KovácsELTE-MTA "Momentum" Motor Enzymology Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány P. s. 1/c, H-1117, Budapest, Hungary. mihaly.kovacs@ttk.elte.hu.ORCID 0000-0002-1200-4741
Eötvös Loránd University · HUNational Institutes of Health · US

Funding

Single-molecule measurements of DNA topology and topoisomerasesZIAHL001056 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI NEUMAN, KEIR · 2009 to 2025
$22.6M
Single-molecule measurements of DNA topology and topoisomerasesZ01HL001056 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI NEUMAN, KEIR · 2007 to 2008
$2.9M
Intramural NIH HHS Z01 HL001056
6 · The paper itself

Abstract

Homologous recombination (HR) is a ubiquitous and efficient process that serves the repair of severe forms of DNA damage and the generation of genetic diversity during meiosis. HR can proceed via multiple pathways with different outcomes that may aid or impair genome stability and faithful inheritance, underscoring the importance of HR quality control. Human Bloom's syndrome (BLM, RecQ family) helicase plays central roles in HR pathway selection and quality control via unexplored molecular mechanisms. Here we show that BLM's multi-domain structural architecture supports a balance between stabilization and disruption of displacement loops (D-loops), early HR intermediates that are key targets for HR regulation. We find that this balance is markedly shifted toward efficient D-loop disruption by the presence of BLM's interaction partners Topoisomerase IIIα-RMI1-RMI2, which have been shown to be involved in multiple steps of HR-based DNA repair. Our results point to a mechanism whereby BLM can differentially process D-loops and support HR control depending on cellular regulatory mechanisms.

Indexed as

DNA-Binding ProteinsDNA, CruciformDNA Topoisomerases, Type IHumansKineticsModels, GeneticMultiprotein ComplexesProtein BindingRecombinational DNA RepairRecQ HelicasesBloom syndrome proteinDNA-Binding ProteinsDNA, CruciformDNA Topoisomerases, Type IMultiprotein ComplexesRecQ HelicasesRMI1 protein, humanRMI2 protein, human

Identifiers

PMID35115525
PMCPMC8813930
OpenAlexW4210753195

What OpenQuestion holds

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Registered trials

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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.