Evidence map›Paper›PMID 32196797›Full record

ArticleProtein science : a publication of the Protein Society2020

The mechanism of Single strand binding protein-RecG binding: Implications for SSB interactome function.

Wenfei Ding, Hui Yin Tan, Jia Xiang Zhang, Luke A Wilczek, Karin R Hsieh, Jeffrey A Mulkin, Piero R Bianco

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
  3. The Role of the RecFOR Complex in Genome Stability.International journal of molecular sciences · 2025
    Review
  4. Identification ofJournal of bacteriology · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Restriction of RecG translocation by DNA mispairing.Biochimica et biophysica acta. General subjects · 2021
    Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. 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

7 authors at 1 institution in 1 country.

Wenfei DingCenter for Single Molecule Biophysics, University at Buffalo, Buffalo, New York, United States.
Hui Yin TanCenter for Single Molecule Biophysics, University at Buffalo, Buffalo, New York, United States.
Jia Xiang ZhangDepartment of Biochemistry, University at Buffalo, Buffalo, New York, United States.
Luke A WilczekCenter for Single Molecule Biophysics, University at Buffalo, Buffalo, New York, United States.
Karin R HsiehCenter for Single Molecule Biophysics, University at Buffalo, Buffalo, New York, United States.
Jeffrey A MulkinCenter for Single Molecule Biophysics, University at Buffalo, Buffalo, New York, United States.
Piero R BiancoCenter for Single Molecule Biophysics, University at Buffalo, Buffalo, New York, United States.ORCID 0000-0003-2974-7952
University 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
Insight into the mechanism of action of the SSB interactomeR01GM144414 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI LYUBCHENKO, YURI L · 2022 to 2025
$1.5M
NIGMS NIH HHS R01 GM100156NIGMS NIH HHS R01 GM144414NIH HHS GM100156
6 · The paper itself

Abstract

The Escherichia coli single-strand DNA binding protein (SSB) is essential to viability where it functions to regulate SSB interactome function. Here it binds to single-stranded DNA and to target proteins that comprise the interactome. The region of SSB that links these two essential protein functions is the intrinsically disordered linker. Key to linker function is the presence of three, conserved PXXP motifs that mediate binding to oligosaccharide-oligonucleotide binding folds (OB-fold) present in SSB and its interactome partners. Not surprisingly, partner OB-fold deletions eliminate SSB binding. Furthermore, single point mutations in either the PXXP motifs or, in the RecG OB-fold, obliterate SSB binding. The data also demonstrate that, and in contrast to the view currently held in the field, the C-terminal acidic tip of SSB is not required for interactome partner binding. Instead, we propose the tip has two roles. First, and consistent with the proposal of Dixon, to regulate the structure of the C-terminal domain in a biologically active conformation that prevents linkers from binding to SSB OB-folds until this interaction is required. Second, as a secondary binding domain. Finally, as OB-folds are present in SSB and many of its partners, we present the SSB interactome as the first family of OB-fold genome guardians identified in prokaryotes.

Indexed as

Binding SitesDNA-Binding ProteinsEscherichia coli ProteinsModels, MolecularOligonucleotidesOligosaccharidesPoint MutationDNA-Binding ProteinsEscherichia coli ProteinsOligonucleotidesOligosaccharidesRecG protein, E coliDNA helicaseOB-foldPXXP motifRecGSH3 domainsingle-strand binding proteinSSB interactome

Identifiers

PMID32196797
PMCPMC7184773
OpenAlexW3012258601

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.