Evidence map›Paper›PMID 37843130›Full record

ArticleNucleic acids research2023

RAD51 paralogs synergize with RAD51 to protect reversed forks from cellular nucleases.

Chia-Lun Guh, Kai-Hang Lei, Yi-An Chen, Yi-Zhen Jiang, Hao-Yen Chang, Hungjiun Liaw, Hung-Wen Li, Hsin-Yung Yen, Peter Chi

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

12 citing papers in PubMed, 14 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

9 authors at 3 institutions in 1 country.

Chia-Lun GuhInstitute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan.
Kai-Hang LeiInstitute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan.
Yi-An ChenInstitute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
Yi-Zhen JiangInstitute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan.
Hao-Yen ChangInstitute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan.
Hungjiun LiawDepartment of Life Sciences, National Cheng Kung University, Tainan, Taiwan.ORCID 0000-0002-3481-709X
Hung-Wen LiDepartment of Chemistry, National Taiwan University, Taipei, Taiwan.ORCID 0000-0002-5614-3727
Hsin-Yung YenInstitute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan.
Peter ChiInstitute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan.ORCID 0000-0001-9229-8729
National Taiwan University · TWInstitute of Biological Chemistry, Academia Sinica · TWNational Cheng Kung University · TW

Funding

Academia SinicaNational Science and Technology Council NSTC 111-2326-B-002-019National Taiwan University
6 · The paper itself

Abstract

Fork reversal is a conserved mechanism to prevent stalled replication forks from collapsing. Formation and protection of reversed forks are two crucial steps in ensuring fork integrity and stability. Five RAD51 paralogs, namely, RAD51B, RAD51C, RAD51D, XRCC2 and XRCC3, which share sequence and structural similarity to the recombinase RAD51, play poorly defined mechanistic roles in these processes. Here, using purified BCDX2 (RAD51BCD-XRCC2) and CX3 (RAD51C-XRCC3) complexes and in vitro reconstituted biochemical systems, we mechanistically dissect their functions in forming and protecting reversed forks. We show that both RAD51 paralog complexes lack fork reversal activities. Whereas CX3 exhibits modest fork protection activity, BCDX2 significantly synergizes with RAD51 to protect DNA against attack by the nucleases MRE11 and EXO1. DNA protection is contingent upon the ability of RAD51 to form a functional nucleoprotein filament on DNA. Collectively, our results provide evidence for a hitherto unknown function of RAD51 paralogs in synergizing with RAD51 nucleoprotein filament to prevent degradation of stressed replication forks.

Indexed as

DNA ReplicationRad51 RecombinaseCell LineChromosomesDNAHumansNucleoproteinsDNANucleoproteinsRAD51 protein, humanRad51 Recombinase

Identifiers

PMID37843130
PMCPMC10681713
OpenAlexW4387661832

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.