Evidence map›Paper›PMID 27694622›Full record

ArticleNucleic acids research2017

The β-isoform of BCCIP promotes ADP release from the RAD51 presynaptic filament and enhances homologous DNA pairing.

Andrew A Kelso, Steven D Goodson, Leah E Watts, LeAnna L Ledford, Sarah M Waldvogel, J Nathaniel Diehl, Shivani B Shah, Amanda F Say, Julie D White, Michael G Sehorn

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

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  14. Roles of BCCIP deficiency in mammary tumorigenesis.Breast cancer research : BCR · 2017
    Article
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

10 authors at 1 institution in 1 country.

Andrew A KelsoDepartment of Genetics and Biochemistry, Clemson University, Clemson, SC 29634, USA.
Steven D GoodsonDepartment of Genetics and Biochemistry, Clemson University, Clemson, SC 29634, USA.
Leah E WattsDepartment of Genetics and Biochemistry, Clemson University, Clemson, SC 29634, USA.
LeAnna L LedfordDepartment of Genetics and Biochemistry, Clemson University, Clemson, SC 29634, USA.
Sarah M WaldvogelDepartment of Genetics and Biochemistry, Clemson University, Clemson, SC 29634, USA.
J Nathaniel DiehlDepartment of Genetics and Biochemistry, Clemson University, Clemson, SC 29634, USA.
Shivani B ShahDepartment of Genetics and Biochemistry, Clemson University, Clemson, SC 29634, USA.
Amanda F SayDepartment of Genetics and Biochemistry, Clemson University, Clemson, SC 29634, USA.
Julie D WhiteDepartment of Genetics and Biochemistry, Clemson University, Clemson, SC 29634, USA.
Michael G SehornDepartment of Genetics and Biochemistry, Clemson University, Clemson, SC 29634, USA msehorn@clemson.edu.
Clemson University · US

Funding

Role of Mei5-Sae3 in meiotic homologous recombinationR01GM098510 · NIGMS · CLEMSON UNIVERSITY · PI SEHORN, MICHAEL G. · 2011 to 2015
$1.2M
Mechanisms of the Human Meiotic Recombinase Dmc1F32GM074529 · NIGMS · YALE UNIVERSITY · PI SEHORN, MICHAEL G. · 2005 to 2005
$48k
NIGMS NIH HHS F32 GM074529NIGMS NIH HHS R01 GM098510
6 · The paper itself

Abstract

Homologous recombination (HR) is a template-driven repair pathway that mends DNA double-stranded breaks (DSBs), and thus helps to maintain genome stability. The RAD51 recombinase facilitates DNA joint formation during HR, but to accomplish this task, RAD51 must be loaded onto the single-stranded DNA. DSS1, a candidate gene for split hand/split foot syndrome, provides the ability to recognize RPA-coated ssDNA to the tumor suppressor BRCA2, which is complexed with RAD51. Together BRCA2-DSS1 displace RPA and load RAD51 onto the ssDNA. In addition, the BRCA2 interacting protein BCCIP normally colocalizes with chromatin bound BRCA2, and upon DSB induction, RAD51 colocalizes with BRCA2-BCCIP foci. Down-regulation of BCCIP reduces DSB repair and disrupts BRCA2 and RAD51 foci formation. While BCCIP is known to interact with BRCA2, the relationship between BCCIP and RAD51 is not known. In this study, we investigated the biochemical role of the β-isoform of BCCIP in relation to the RAD51 recombinase. We demonstrate that BCCIPβ binds DNA and physically and functionally interacts with RAD51 to stimulate its homologous DNA pairing activity. Notably, this stimulatory effect is not the result of RAD51 nucleoprotein filament stabilization; rather, we demonstrate that BCCIPβ induces a conformational change within the RAD51 filament that promotes release of ADP to help maintain an active presynaptic filament. Our findings reveal a functional role for BCCIPβ as a RAD51 accessory factor in HR.

Indexed as

Base PairingHomologous RecombinationAdenosine DiphosphateAdenosine TriphosphateCalcium-Binding ProteinsCell Cycle ProteinsDNA RepairHumansHydrolysisNuclear ProteinsProtein BindingProtein ConformationProtein IsoformsProtein MultimerizationRad51 RecombinaseAdenosine DiphosphateAdenosine TriphosphateBCCIP protein, humanCalcium-Binding ProteinsCell Cycle ProteinsNuclear ProteinsProtein IsoformsRad51 Recombinase

Identifiers

PMID27694622
PMCPMC5314795
OpenAlexW2524466066

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.