Evidence map›Paper›PMID 27387285›Full record

ArticleNucleic acids research2016

A structural analysis of DNA binding by hSSB1 (NABP2/OBFC2B) in solution.

Christine Touma, Ruvini Kariawasam, Adrian X Gimenez, Ray E Bernardo, Nicholas W Ashton, Mark N Adams, Nicolas Paquet, Tristan I Croll, Kenneth J O'Byrne, Derek J Richard and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

17 citing papers in PubMed, 31 citations in OpenAlex.

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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

12 authors at 3 institutions in 1 country.

Christine ToumaSchool of Science and Health, Western Sydney University, Penrith, NSW 2751, Australia.
Ruvini KariawasamSchool of Science and Health, Western Sydney University, Penrith, NSW 2751, Australia.
Adrian X GimenezSchool of Science and Health, Western Sydney University, Penrith, NSW 2751, Australia.
Ray E BernardoSchool of Science and Health, Western Sydney University, Penrith, NSW 2751, Australia.
Nicholas W AshtonSchool of Biomedical Research, Institute of Health and Biomedical Innovation at the Translational Research Institute, Queensland University of Technology, Woolloongabba, QLD 4102, Australia.
Mark N AdamsSchool of Biomedical Research, Institute of Health and Biomedical Innovation at the Translational Research Institute, Queensland University of Technology, Woolloongabba, QLD 4102, Australia.
Nicolas PaquetSchool of Biomedical Research, Institute of Health and Biomedical Innovation at the Translational Research Institute, Queensland University of Technology, Woolloongabba, QLD 4102, Australia.
Tristan I CrollSchool of Biomedical Research, Institute of Health and Biomedical Innovation at the Translational Research Institute, Queensland University of Technology, Woolloongabba, QLD 4102, Australia.
Kenneth J O'ByrneSchool of Biomedical Research, Institute of Health and Biomedical Innovation at the Translational Research Institute, Queensland University of Technology, Woolloongabba, QLD 4102, Australia.
Derek J RichardSchool of Biomedical Research, Institute of Health and Biomedical Innovation at the Translational Research Institute, Queensland University of Technology, Woolloongabba, QLD 4102, Australia.
Liza CubedduSchool of Science and Health, Western Sydney University, Penrith, NSW 2751, Australia School of Molecular Biosciences, University of Sydney, NSW 2006, Australia l.cubeddu@westernsydney.edu.au.
Roland GamsjaegerSchool of Science and Health, Western Sydney University, Penrith, NSW 2751, Australia School of Molecular Biosciences, University of Sydney, NSW 2006, Australia r.gamsjaeger@westernsydney.edu.au.ORCID 0000-0003-1095-2569
Translational Research Institute · AUWestern Sydney University · AUThe University of Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single-stranded DNA binding proteins (SSBs) play an important role in DNA processing events such as replication, recombination and repair. Human single-stranded DNA binding protein 1 (hSSB1/NABP2/OBFC2B) contains a single oligosaccharide/oligonucleotide binding (OB) domain followed by a charged C-terminus and is structurally homologous to the SSB from the hyperthermophilic crenarchaeote Sulfolobus solfataricus Recent work has revealed that hSSB1 is critical to homologous recombination and numerous other important biological processes such as the regulation of telomeres, the maintenance of DNA replication forks and oxidative damage repair. Since the ability of hSSB1 to directly interact with single-stranded DNA (ssDNA) is paramount for all of these processes, understanding the molecular details of ssDNA recognition is essential. In this study, we have used solution-state nuclear magnetic resonance in combination with biophysical and functional experiments to structurally analyse ssDNA binding by hSSB1. We reveal that ssDNA recognition in solution is modulated by base-stacking of four key aromatic residues within the OB domain. This DNA binding mode differs significantly from the recently determined crystal structure of the SOSS1 complex containing hSSB1 and ssDNA. Our findings elucidate the detailed molecular mechanism in solution of ssDNA binding by hSSB1, a major player in the maintenance of genomic stability.

Indexed as

Amino Acids, AromaticAmino Acid SequenceDNA-Binding ProteinsDNA Mutational AnalysisDNA, Single-StrandedHeLa CellsHumansHydrogen BondingMagnetic Resonance SpectroscopyMitochondrial ProteinsModels, MolecularProtein BindingProtein DomainsSequence AlignmentSolutionsAmino Acids, AromaticDNA-Binding ProteinsDNA, Single-StrandedMitochondrial ProteinsNABP2 protein, humanSolutions

Identifiers

PMID27387285
PMCPMC5027503
OpenAlexW2470604975

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.