Evidence map›Paper›PMID 28069956›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Shuttling along DNA and directed processing of D-loops by RecQ helicase support quality control of homologous recombination.

Gábor M Harami, Yeonee Seol, Junghoon In, Veronika Ferencziová, Máté Martina, Máté Gyimesi, Kata Sarlós, Zoltán J Kovács, Nikolett T Nagy, Yuze Sun and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

30 citing papers in PubMed, 42 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

13 authors at 4 institutions in 2 countries.

Gábor M HaramiDepartment of Biochemistry, Eötvös Loránd University-Hungarian Academy of Sciences "Momentum" Motor Enzymology Research Group, Eötvös Loránd University, H-1117 Budapest, Hungary.
Yeonee SeolLaboratory of Single Molecule Biophysics, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
Junghoon InLaboratory of Single Molecule Biophysics, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
Veronika FerencziováDepartment of Biochemistry, Eötvös Loránd University-Hungarian Academy of Sciences "Momentum" Motor Enzymology Research Group, Eötvös Loránd University, H-1117 Budapest, Hungary.
Máté MartinaDepartment of Biochemistry, Eötvös Loránd University-Hungarian Academy of Sciences "Momentum" Motor Enzymology Research Group, Eötvös Loránd University, H-1117 Budapest, Hungary.
Máté GyimesiDepartment of Biochemistry, Eötvös Loránd University-Hungarian Academy of Sciences "Momentum" Motor Enzymology Research Group, Eötvös Loránd University, H-1117 Budapest, Hungary.
Kata SarlósDepartment of Biochemistry, Eötvös Loránd University-Hungarian Academy of Sciences "Momentum" Motor Enzymology Research Group, Eötvös Loránd University, H-1117 Budapest, Hungary.
Zoltán J KovácsDepartment of Biochemistry, Eötvös Loránd University-Hungarian Academy of Sciences "Momentum" Motor Enzymology Research Group, Eötvös Loránd University, H-1117 Budapest, Hungary.
Nikolett T NagyDepartment of Biochemistry, Eötvös Loránd University-Hungarian Academy of Sciences "Momentum" Motor Enzymology Research Group, Eötvös Loránd University, H-1117 Budapest, Hungary.
Yuze SunLaboratory of Single Molecule Biophysics, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
Tibor VellaiDepartment of Genetics, Eötvös Loránd University, H-1117 Budapest, Hungary.
Keir C NeumanLaboratory of Single Molecule Biophysics, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892; mihaly.kovacs@ttk.elte.hu neumankc@mail.nih.gov.
Mihály KovácsDepartment of Biochemistry, Eötvös Loránd University-Hungarian Academy of Sciences "Momentum" Motor Enzymology Research Group, Eötvös Loránd University, H-1117 Budapest, Hungary; mihaly.kovacs@ttk.elte.hu neumankc@mail.nih.gov.
Hungarian Academy of Sciences · HUEötvös Loránd University · HUNational Heart Lung and Blood Institute · USNational 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

Cells must continuously repair inevitable DNA damage while avoiding the deleterious consequences of imprecise repair. Distinction between legitimate and illegitimate repair processes is thought to be achieved in part through differential recognition and processing of specific noncanonical DNA structures, although the mechanistic basis of discrimination remains poorly defined. Here, we show that Escherichia coli RecQ, a central DNA recombination and repair enzyme, exhibits differential processing of DNA substrates based on their geometry and structure. Through single-molecule and ensemble biophysical experiments, we elucidate how the conserved domain architecture of RecQ supports geometry-dependent shuttling and directed processing of recombination-intermediate [displacement loop (D-loop)] substrates. Our study shows that these activities together suppress illegitimate recombination in vivo, whereas unregulated duplex unwinding is detrimental for recombination precision. Based on these results, we propose a mechanism through which RecQ helicases achieve recombination precision and efficiency.

Indexed as

Homologous RecombinationDNADNA RepairEscherichia coliEscherichia coli ProteinsInverted Repeat SequencesRecQ HelicasesDNAEscherichia coli ProteinsRecQ HelicasesRecQ protein, E coliDNA unwindinghelicasemagnetic tweezersRecQsingle molecule

Identifiers

PMID28069956
PMCPMC5278487
OpenAlexW2568264723

What OpenQuestion holds

Textmetadata
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.