Evidence map›Paper›PMID 25319828›Full record

ArticleGenes & development2014

Crystal structure of a Fanconi anemia-associated nuclease homolog bound to 5' flap DNA: basis of interstrand cross-link repair by FAN1.

Gwang Hyeon Gwon, Youngran Kim, Yaqi Liu, Adam T Watson, Aera Jo, Thomas J Etheridge, Fenghua Yuan, Yanbin Zhang, YoungChang Kim, Anthony M Carr and 1 more

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2014. 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
–field-weighted citation impact
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, 22 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

11 authors at 4 institutions in 3 countries.

Gwang Hyeon GwonDepartment of Life Science, Pohang University of Science and Technology, Pohang 790-784, South Korea;
Youngran KimDepartment of Life Science, Pohang University of Science and Technology, Pohang 790-784, South Korea;
Yaqi LiuDepartment of Life Science, Pohang University of Science and Technology, Pohang 790-784, South Korea;
Adam T WatsonGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Brighton, East Sussex BN1 9RQ, United Kingdom;
Aera JoDepartment of Life Science, Pohang University of Science and Technology, Pohang 790-784, South Korea;
Thomas J EtheridgeGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Brighton, East Sussex BN1 9RQ, United Kingdom;
Fenghua YuanDepartment of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, Florida 33136, USA;
Yanbin ZhangDepartment of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, Florida 33136, USA;
YoungChang KimBiosciences Division, Structural Biology Center, Argonne National Laboratory, Argonne, Illinois 60439, USA.
Anthony M CarrGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Brighton, East Sussex BN1 9RQ, United Kingdom;
Yunje ChoDepartment of Life Science, Pohang University of Science and Technology, Pohang 790-784, South Korea; yunje@postech.ac.kr.
Pohang University of Science and Technology · KRUniversity of Sussex · GBUniversity of Miami · USArgonne National Laboratory · US

Funding

Role of Fanconi Anemia Core Complex in the Incision of DNA Interstrand CrosslinksR01HL105631 · NHLBI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI ZHANG, YANBIN · 2011 to 2015
$1.8M
European Research Council 268788NHLBI NIH HHS HL105631NHLBI NIH HHS R01 HL105631
6 · The paper itself

Abstract

Fanconi anemia (FA) is an autosomal recessive genetic disorder caused by defects in any of 15 FA genes responsible for processing DNA interstrand cross-links (ICLs). The ultimate outcome of the FA pathway is resolution of cross-links, which requires structure-selective nucleases. FA-associated nuclease 1 (FAN1) is believed to be recruited to lesions by a monoubiquitinated FANCI-FANCD2 (ID) complex and participates in ICL repair. Here, we determined the crystal structure of Pseudomonas aeruginosa FAN1 (PaFAN1) lacking the UBZ (ubiquitin-binding zinc) domain in complex with 5' flap DNA. All four domains of the right-hand-shaped PaFAN1 are involved in DNA recognition, with each domain playing a specific role in bending DNA at the nick. The six-helix bundle that binds the junction connects to the catalytic viral replication and repair (VRR) nuclease (VRR nuc) domain, enabling FAN1 to incise the scissile phosphate a few bases distant from the junction. The six-helix bundle also inhibits the cleavage of intact Holliday junctions. PaFAN1 shares several conserved features with other flap structure-selective nucleases despite structural differences. A clamping motion of the domains around the wedge helix, which acts as a pivot, facilitates nucleolytic cleavage. The PaFAN1 structure provides insights into how archaeal Holliday junction resolvases evolved to incise 5' flap substrates and how FAN1 integrates with the FA complex to participate in ICL repair.

Indexed as

Models, MolecularCatalytic DomainCrystallizationExodeoxyribonucleasesFlap EndonucleasesHumansProtein BindingProtein Structure, TertiaryPseudomonas aeruginosaExodeoxyribonucleasesFlap Endonucleasescrystal structureFanconi anemia nuclease 1interstrand cross-link repair

Identifiers

PMID25319828
PMCPMC4201288
OpenAlexW2020122081

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LicenceCC BY-NC
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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.