Evidence map›Paper›PMID 26381353›Full record

ArticleeLife2015

Imaging and energetics of single SSB-ssDNA molecules reveal intramolecular condensation and insight into RecOR function.

Jason C Bell, Bian Liu, Stephen C Kowalczykowski

Open access · goldAbstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
5.9field-weighted citation impact, top 4% 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

48 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. NProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. The Role of the RecFOR Complex in Genome Stability.International journal of molecular sciences · 2025
    Review
  6. Review
  7. Article
  8. Article
  9. Generation and Repair of Postreplication Gaps in Escherichia coli.Microbiology and molecular biology reviews : MMBR · 2023
    Review
  10. Article
  11. Article
  12. Regulation of phosphate starvation-specific responses inMicrobiology (Reading, England) · 2023
    Review
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. 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

3 authors at 1 institution in 1 country.

Jason C BellGraduate Group in Biochemistry and Molecular Biology, University of California, Davis, Davis, United States.ORCID http://orcid.org/0000-0001-5480-7975
Bian LiuDepartment of Microbiology and Molecular Genetics, University of California, Davis, Davis, United States.ORCID http://orcid.org/0000-0001-8806-820X
Stephen C KowalczykowskiDepartment of Microbiology and Molecular Genetics, University of California, Davis, Davis, United States.ORCID http://orcid.org/0000-0002-9127-3949
University of California, Davis · US

Funding

UC Davis MCB T32 Administrative Supplement to Recognize Excellence in Diversity, Equity, Inclusion, and Accessibility (DEIA) MentorshipT32GM007377 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI CHEDIN, FREDERIC LOUIS · 1985 to 2023
$9.9M
Mechanistic Studies of Genetic RecombinationR01GM062653 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI KOWALCZYKOWSKI, STEPHEN CHARLES · 2010 to 2018
$4.4M
Single-Molecule Assembly of Protein-DNA ComplexesR01GM064745 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI KOWALCZYKOWSKI, STEPHEN CHARLES · 2002 to 2018
$4.3M
MECHANISTIC STUDIES OF GENETIC RECOMBINATIONR37GM062653 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI KOWALCZYKOWSKI, STEPHEN CHARLES · 2000 to 2009
$3.6M
NIGMS NIH HHS GM-62653NIGMS NIH HHS GM-64745NIGMS NIH HHS R01 GM062653NIGMS NIH HHS R01 GM064745NIGMS NIH HHS R37 GM062653NIGMS NIH HHS T32 GM007377
6 · The paper itself

Abstract

Escherichia coli single-stranded DNA (ssDNA) binding protein (SSB) is the defining bacterial member of ssDNA binding proteins essential for DNA maintenance. SSB binds ssDNA with a variable footprint of ∼30-70 nucleotides, reflecting partial or full wrapping of ssDNA around a tetramer of SSB. We directly imaged single molecules of SSB-coated ssDNA using total internal reflection fluorescence (TIRF) microscopy and observed intramolecular condensation of nucleoprotein complexes exceeding expectations based on simple wrapping transitions. We further examined this unexpected property by single-molecule force spectroscopy using magnetic tweezers. In conditions favoring complete wrapping, SSB engages in long-range reversible intramolecular interactions resulting in condensation of the SSB-ssDNA complex. RecO and RecOR, which interact with SSB, further condensed the complex. Our data support the idea that RecOR--and possibly other SSB-interacting proteins-function(s) in part to alter long-range, macroscopic interactions between or throughout nucleoprotein complexes by microscopically altering wrapping and bridging distant sites.

Indexed as

DNA-Binding ProteinsDNA, Single-StrandedEscherichia coliEscherichia coli ProteinsOptical ImagingProtein BindingProtein ConformationProtein MultimerizationDNA-Binding ProteinsDNA, Single-StrandedEscherichia coli ProteinsRecO protein, E coliRecR protein, E coliSSB protein, E colibiochemistrybiophysicsDNA recombinationDNA repairE. colimagnetic tweezersRecORssDNA binding proteinstructural biologytotal internal reflection fluorescence microscopy

Identifiers

PMID26381353
PMCPMC4652220
OpenAlexW2180536020

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.