Evidence map›Paper›PMID 25923319›Full record

ArticleScientific reports2015

Remodeling of RecG Helicase at the DNA Replication Fork by SSB Protein.

Zhiqiang Sun, Hui Yin Tan, Piero R Bianco, Yuri L Lyubchenko

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

36 citing papers in PubMed, 50 citations in OpenAlex.

  1. Nanoscale Analysis of SSB-RecO Interplay in SSB Interaction with the Target.International journal of molecular sciences · 2026
    Article
  2. Article
  3. Review
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  7. Review
  8. Restriction of RecG translocation by DNA mispairing.Biochimica et biophysica acta. General subjects · 2021
    Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Dynamics of the PriA Helicase at Stalled DNA Replication Forks.The journal of physical chemistry. B · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
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

4 authors at 3 institutions in 1 country.

Zhiqiang SunDepartment of Pharmaceutical Sciences, University of Nebraska Medical Center, Omaha, NE 68198-6025, USA.
Hui Yin TanDepartment of Microbiology and Immunology, University at Buffalo, SUNY, Buffalo, NY 14214, USA.
Piero R BiancoDepartment of Microbiology and Immunology, University at Buffalo, SUNY, Buffalo, NY 14214, USA.
Yuri L LyubchenkoDepartment of Pharmaceutical Sciences, University of Nebraska Medical Center, Omaha, NE 68198-6025, USA.
University of Nebraska Medical Center · USBuffalo State University · USUniversity at Buffalo, State University of New York · US

Funding

Mechanistic studies of stalled DNA replication fork rescueR01GM100156 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI BIANCO, PIERO R, LYUBCHENKO, YURI L · 2013 to 2021
$4.0M
NIGMS NIH HHS GM100156NIGMS NIH HHS R01 GM100156
6 · The paper itself

Abstract

The RecG DNA helicase a key player in stalled replication fork rescue. The single-stranded DNA binding protein (SSB) participates in this process, but its role in the interaction of RecG with the fork remains unclear. We used atomic force microscopy (AFM) to visualize the interaction of RecG with a fork DNA in the presence of SSB. We discovered that SSB enhances RecG loading efficiency onto the DNA fork by threefold. Additionally, SSB interacts with RecG leading to the RecG remodeling. As a result, RecG separates from the fork, but remains bound to the DNA duplex. Moreover, in this new binding mode RecG is capable of translocation along the parental duplex DNA. We propose a model of RecG interaction with the replication fork involving two RecG binding modes. SSB plays the role of a remodeling factor defining the mode of RecG binding to the fork mediated by the SSB C-terminus. In the translocating mode, RecG remains in the vicinity of the fork and is capable of initiating the fork regression. Our results afford novel mechanistic insights into RecG interaction with the replication fork and provide the basis for further structural studies.

Indexed as

Binding SitesDNA-Binding ProteinsDNA HelicasesDNA ReplicationDNA, Single-StrandedEscherichia coliEscherichia coli ProteinsDNA-Binding ProteinsDNA HelicasesDNA, Single-StrandedEscherichia coli ProteinsRecG protein, E coli

Identifiers

PMID25923319
PMCPMC4894433
OpenAlexW2061713612

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.