Evidence map›Paper›PMID 37391417›Full record

ArticleNature communications2023

ssDNA accessibility of Rad51 is regulated by orchestrating multiple RPA dynamics.

Jiawei Ding, Xiangting Li, Jiangchuan Shen, Yiling Zhao, Shuchen Zhong, Luhua Lai, Hengyao Niu, Zhi Qi

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

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  16. Rtt105 stimulates Rad51-ssDNA assembly and orchestrates Rad51 and RPA actions to promote homologous recombination repair.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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

8 authors at 3 institutions in 2 countries.

Jiawei Ding *Center for Quantitative Biology, Peking-Tsinghua Center for Life Sciences, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing, China.
Xiangting Li *Department of Computational Medicine, University of California, Los Angeles, CA, USA.ORCID 0000-0001-5238-7364
Jiangchuan Shen *Department of Molecular and Cellular Biochemistry, Indiana University, Bloomington, IN, USA.ORCID 0000-0003-1699-564X
Yiling ZhaoCenter for Quantitative Biology, Peking-Tsinghua Center for Life Sciences, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing, China.
Shuchen ZhongBNLMS, College of Chemistry and Molecular Engineering, Peking University, Beijing, China.
Luhua LaiCenter for Quantitative Biology, Peking-Tsinghua Center for Life Sciences, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing, China.ORCID 0000-0002-8343-7587
Hengyao NiuDepartment of Molecular and Cellular Biochemistry, Indiana University, Bloomington, IN, USA. hniu@indiana.edu.ORCID 0000-0003-1768-0674
Zhi QiCenter for Quantitative Biology, Peking-Tsinghua Center for Life Sciences, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing, China. zhiqi7@pku.edu.cn.ORCID 0000-0002-1572-9721
Peking University · CNIndiana University Bloomington · USUniversity of California, Los Angeles · US

Funding

Mechanisms of DNA helicases and nucleases in genome maintenanceR35GM124765 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI NIU, HENGYAO · 2017 to 2021
$2.0M
NIGMS NIH HHS R35 GM124765
6 · The paper itself

Abstract

The eukaryotic single-stranded DNA (ssDNA)-binding protein Replication Protein A (RPA) plays a crucial role in various DNA metabolic pathways, including DNA replication and repair, by dynamically associating with ssDNA. While the binding of a single RPA molecule to ssDNA has been thoroughly studied, the accessibility of ssDNA is largely governed by the bimolecular behavior of RPA, the biophysical nature of which remains unclear. In this study, we develop a three-step low-complexity ssDNA Curtains method, which, when combined with biochemical assays and a Markov chain model in non-equilibrium physics, allow us to decipher the dynamics of multiple RPA binding to long ssDNA. Interestingly, our results suggest that Rad52, the mediator protein, can modulate the ssDNA accessibility of Rad51, which is nucleated on RPA coated ssDNA through dynamic ssDNA exposure between neighboring RPA molecules. We find that this process is controlled by the shifting between the protection mode and action mode of RPA ssDNA binding, where tighter RPA spacing and lower ssDNA accessibility are favored under RPA protection mode, which can be facilitated by the Rfa2 WH domain and inhibited by Rad52 RPA interaction.

Indexed as

DNA, Single-StrandedRad51 RecombinaseReplication Protein ADNA-Binding ProteinsDNA-Binding ProteinsDNA, Single-StrandedRad51 RecombinaseReplication Protein A

Identifiers

PMID37391417
PMCPMC10313831
OpenAlexW4382786361

What OpenQuestion holds

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LicenceCC BY
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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.