Evidence map›Paper›PMID 20207730›Full record

ArticleThe Journal of biological chemistry2010

Ring-shaped Rad51 paralog protein complexes bind Holliday junctions and replication forks as visualized by electron microscopy.

Sarah A Compton, Sezgin Ozgür, Jack D Griffith

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

16 citing papers in PubMed, 31 citations in OpenAlex.

  1. Novel insights into RAD51 activity and regulation during homologous recombination and DNA replication.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2016
    Review
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  7. DNA repair pathways in trypanosomatids: from DNA repair to drug resistance.Microbiology and molecular biology reviews : MMBR · 2014
    Review
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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

3 authors at 1 institution in 1 country.

Sarah A ComptonLineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, North Carolina 27599, USA. compton@med.unc.edu
Sezgin Ozgür
Jack D Griffith
University of North Carolina at Chapel Hill · US

Funding

HOMOLOOUS RECOMBINATION: ITS MOLECULAR CYTOLOGYR01GM031819 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI GRIFFITH, JACK D · 1985 to 2017
$5.2M
Nucleoprotein structures formed at sites of DNA damageR01ES013773 · NIEHS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI GRIFFITH, JACK D · 2005 to 2015
$3.2M
Remodeling of Telomeres by Telomere Associated ProteinsF32GM077900 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI COMPTON, SARAH A · 2006 to 2007
$77k
NIEHS NIH HHS ES013773NIEHS NIH HHS R01 ES013773NIGMS NIH HHS F32 GM077900NIGMS NIH HHS GM077900NIGMS NIH HHS GM31819NIGMS NIH HHS R01 GM031819
6 · The paper itself

Abstract

In mammals, there are five Rad51 paralogs that form two distinct complexes in vivo. One complex is composed of Rad51B-Rad51C-Rad51D-Xrcc2 (BCDX2) and the other Rad51C-Xrcc3 (CX3). We co-expressed and purified human BCDX2 and CX3 protein complexes from insect cells and investigated their binding preferences and structure using transmission electron microscopy (TEM). We visualized the binding of BCDX2 and CX3 to DNA templates containing replication forks and Holliday junctions, intermediates observed during DNA replication and recombination, respectively. We show that both complexes bind with exceptionally high specificity to the DNA junctions with little binding observed elsewhere on the DNAs. Further analysis of the structure of free or DNA-bound BCDX2 and CX3 complexes revealed a multimeric ring structure whose subunits are arranged into a flat disc around a central channel. This work provides the first EM visualization of BCDX2 and CX3 binding to Holliday junctions and forked DNAs and suggests the complexes form ring-shaped structures.

Indexed as

Microscopy, Electron, TransmissionAnimalsDNA-Binding ProteinsDNA, CruciformDNA ReplicationHumansMultiprotein ComplexesProtein Structure, QuaternaryRecombinant ProteinsSpodopteraDNA-Binding ProteinsDNA, CruciformMultiprotein ComplexesRAD51C protein, humanRecombinant ProteinsX-ray repair cross complementing protein 3XRCC2 protein, human

Identifiers

PMID20207730
PMCPMC2859493
OpenAlexW2020120289

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.