Evidence map›Paper›PMID 29059328›Full record

ArticleNucleic acids research2017

RecQ helicase triggers a binding mode change in the SSB-DNA complex to efficiently initiate DNA unwinding.

Maria Mills, Gábor M Harami, Yeonee Seol, Máté Gyimesi, Máté Martina, Zoltán J Kovács, Mihály Kovács, Keir C Neuman

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. Regulation of Pfh1 helicase activity by nucleic acid interactions and mitochondrial SSB.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Single-stranded DNA binding protein hitches a ride with thebioRxiv : the preprint server for biology · 2024
    Article
  6. Article
  7. Article
  8. Article
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  11. Phase separation by ssDNA binding protein controlled via protein-protein and protein-DNA interactions.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Direct observation of topoisomerase IA gate dynamics.Nature structural & molecular biology · 2018
    Article
  19. Article
  20. Molecular insights into the prototypical single-stranded DNA-binding protein fromCritical reviews in biochemistry and molecular biology
    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

8 authors at 2 institutions in 2 countries.

Maria MillsLaboratory of Single Molecule Biophysics, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Gábor M HaramiDepartment of Biochemistry, ELTE-MTA "Momentum" Motor Enzymology Research Group, 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, MD 20892, USA.
Máté GyimesiDepartment of Biochemistry, ELTE-MTA "Momentum" Motor Enzymology Research Group, Eötvös Loránd University, Pázmány P. s. 1/c, H-1117 Budapest, Hungary.
Máté MartinaDepartment of Biochemistry, ELTE-MTA "Momentum" Motor Enzymology Research Group, Eötvös Loránd University, Pázmány P. s. 1/c, H-1117 Budapest, Hungary.
Zoltán J KovácsDepartment of Biochemistry, ELTE-MTA "Momentum" Motor Enzymology Research Group, Eötvös Loránd University, Pázmány P. s. 1/c, H-1117 Budapest, Hungary.
Mihály KovácsDepartment of Biochemistry, ELTE-MTA "Momentum" Motor Enzymology Research Group, 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, MD 20892, USA.
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
6 · The paper itself

Abstract

The single-stranded DNA binding protein (SSB) of Escherichia coli plays essential roles in maintaining genome integrity by sequestering ssDNA and mediating DNA processing pathways through interactions with DNA-processing enzymes. Despite its DNA-sequestering properties, SSB stimulates the DNA processing activities of some of its binding partners. One example is the genome maintenance protein RecQ helicase. Here, we determine the mechanistic details of the RecQ-SSB interaction using single-molecule magnetic tweezers and rapid kinetic experiments. Our results reveal that the SSB-RecQ interaction changes the binding mode of SSB, thereby allowing RecQ to gain access to ssDNA and facilitating DNA unwinding. Conversely, the interaction of RecQ with the SSB C-terminal tail increases the on-rate of RecQ-DNA binding and has a modest stimulatory effect on the unwinding rate of RecQ. We propose that this bidirectional communication promotes efficient DNA processing and explains how SSB stimulates rather than inhibits RecQ activity.

Indexed as

DNA, BacterialDNA-Binding ProteinsDNA, Single-StrandedEscherichia coliEscherichia coli ProteinsMagneticsModels, MolecularNucleic Acid ConformationOptical TweezersProtein BindingProtein DomainsRecQ HelicasesDNA, BacterialDNA-Binding ProteinsDNA, Single-StrandedEscherichia coli ProteinsRecQ HelicasesSSB protein, E coli

Identifiers

PMID29059328
PMCPMC5714189
OpenAlexW2765731608

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.