Evidence map›Paper›PMID 22570477›Full record

ArticleThe Journal of biological chemistry2012

Structure and cellular dynamics of Deinococcus radiodurans single-stranded DNA (ssDNA)-binding protein (SSB)-DNA complexes.

Nicholas P George, Khanh V Ngo, Sindhu Chitteni-Pattu, Cédric A Norais, John R Battista, Michael M Cox, James L Keck

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.8field-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

35 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Review
  3. Characterization of the Chimeric PriB-SSBc Protein.International journal of molecular sciences · 2021
    Article
  4. Article
  5. Article
  6. Article
  7. The Essential, Ubiquitous Single-Stranded DNA-Binding Proteins.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  8. Article
  9. A structural view of bacterial DNA replication.Protein science : a publication of the Protein Society · 2019
    Review
  10. Article
  11. Article
  12. Structure-specific DNA replication-fork recognition directs helicase and replication restart activities of the PriA helicase.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
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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

7 authors at 3 institutions in 2 countries.

Nicholas P GeorgeDepartment of Biomolecular Chemistry, University of Wisconsin School of Medicine and Public Health, Madison, Wisconsin 53706, USA.
Khanh V Ngo
Sindhu Chitteni-Pattu
Cédric A Norais
John R Battista
Michael M Cox
James L Keck
University of Wisconsin–Madison · USCentre National de la Recherche Scientifique · FRLouisiana State University · US

Funding

THE BIOCHEMISTRY OF GENETIC RECOMBINATION/RECA PROTEINR01GM032335 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI COX, MICHAEL M. · 1985 to 2014
$6.8M
Structure and Function of Bacterial RecQ ProteinR01GM068061 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI KECK, JAMES L · 2003 to 2011
$2.7M
Mechanisms and applications of recombinational DNA repairU01GM032335 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI COX, MICHAEL M. · 2015 to 2018
$1.7M
NIGMS NIH HHS GM068061NIGMS NIH HHS GM32335NIGMS NIH HHS R01 GM032335NIGMS NIH HHS R01 GM068061NIGMS NIH HHS U01 GM032335
6 · The paper itself

Abstract

The single-stranded DNA (ssDNA)-binding protein from the radiation-resistant bacterium Deinococcus radiodurans (DrSSB) functions as a homodimer in which each monomer contains two oligonucleotide-binding (OB) domains. This arrangement is exceedingly rare among bacterial SSBs, which typically form homotetramers of single-OB domain subunits. To better understand how this unusual structure influences the DNA binding and biological functions of DrSSB in D. radiodurans radiation resistance, we have examined the structure of DrSSB in complex with ssDNA and the DNA damage-dependent cellular dynamics of DrSSB. The x-ray crystal structure of the DrSSB-ssDNA complex shows that ssDNA binds to surfaces of DrSSB that are analogous to those mapped in homotetrameric SSBs, although there are distinct contacts in DrSSB that mediate species-specific ssDNA binding. Observations by electron microscopy reveal two salt-dependent ssDNA-binding modes for DrSSB that strongly resemble those of the homotetrameric Escherichia coli SSB, further supporting a shared overall DNA binding mechanism between the two classes of bacterial SSBs. In vivo, DrSSB levels are heavily induced following exposure to ionizing radiation. This accumulation is accompanied by dramatic time-dependent DrSSB cellular dynamics in which a single nucleoid-centric focus of DrSSB is observed within 1 h of irradiation but is dispersed by 3 h after irradiation. These kinetics parallel those of D. radiodurans postirradiation genome reconstitution, suggesting that DrSSB dynamics could play important organizational roles in DNA repair.

Indexed as

Crystallography, X-RayDeinococcusDNA-Binding ProteinsDNA DamageDNA, Single-StrandedEscherichia coliKineticsMicroscopy, ElectronMicroscopy, FluorescenceModels, MolecularOligonucleotidesProtein BindingProtein Structure, TertiaryRadiation, IonizingRecombination, GeneticSaltsDNA-Binding ProteinsDNA, Single-StrandedOligonucleotidesSalts

Identifiers

PMID22570477
PMCPMC3381170
OpenAlexW2096578308

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.