Evidence map›Paper›PMID 29590107›Full record

ArticlePLoS genetics2018

Novel function of HATs and HDACs in homologous recombination through acetylation of human RAD52 at double-strand break sites.

Takeshi Yasuda, Wataru Kagawa, Tomoo Ogi, Takamitsu A Kato, Takehiro Suzuki, Naoshi Dohmae, Kazuya Takizawa, Yuka Nakazawa, Matthew D Genet, Mika Saotome and 18 more

Abstract read
In one paragraph

Article in PLoS genetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Targeting RAD52 overcomes PARP inhibitor resistance in preclinicalbioRxiv : the preprint server for biology · 2025
    Article
  6. Review
  7. Roles of SIRT3 in aging and aging-related diseases.International journal of biological sciences · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. DNA Damage-Mediated Neurotoxicity in Parkinson's Disease.International journal of molecular sciences · 2023
    Review
  12. Review
  13. Review
  14. Fueling genome maintenance: On the versatile roles of NADThe Journal of biological chemistry · 2022
    Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. 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

28 authors.

Takeshi YasudaResearch Center for Radiation Emergency Medicine, National Institute of Radiological Sciences (NIRS), Anagawa, Inage-ku, Chiba, Japan.ORCID 0000-0001-6812-3048
Wataru KagawaProgram in Chemistry and Life Science, Department of Interdisciplinary Science and Engineering, School of Science and Engineering, Meisei University, Hodokubo, Hino-shi, Tokyo, Japan.
Tomoo OgiDepartment of Genetics, Research Institute of Environmental Medicine, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Japan.ORCID 0000-0002-5492-9072
Takamitsu A KatoDepartment of Environmental and Radiological Health Sciences, Colorado State University, Fort Collins, CO, United States of America.
Takehiro SuzukiBiomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Hirosawa, Wako, Saitama, Japan.
Naoshi DohmaeBiomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Hirosawa, Wako, Saitama, Japan.
Kazuya TakizawaResearch Center for Radiation Emergency Medicine, National Institute of Radiological Sciences (NIRS), Anagawa, Inage-ku, Chiba, Japan.
Yuka NakazawaDepartment of Genetics, Research Institute of Environmental Medicine, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Japan.
Matthew D GenetDepartment of Environmental and Radiological Health Sciences, Colorado State University, Fort Collins, CO, United States of America.
Mika SaotomeProgram in Chemistry and Life Science, Department of Interdisciplinary Science and Engineering, School of Science and Engineering, Meisei University, Hodokubo, Hino-shi, Tokyo, Japan.
Michio HamaDepartment of Basic Medical Sciences for Radiation Damage, NIRS, National Institutes for Quantum and Radiation Sciences and Technology (QST), Anagawa, Inage-ku, Chiba, Japan.
Teruaki KonishiDepartment of Basic Medical Sciences for Radiation Damage, NIRS, National Institutes for Quantum and Radiation Sciences and Technology (QST), Anagawa, Inage-ku, Chiba, Japan.ORCID 0000-0002-2485-9659
Nakako Izumi NakajimaResearch Center for Charged Particle Therapy, NIRS, Anagawa, Inage-ku, Chiba, Japan.
Masaharu HazawaResearch Center for Radiation Emergency Medicine, National Institute of Radiological Sciences (NIRS), Anagawa, Inage-ku, Chiba, Japan.
Masanori TomitaRadiation Safety Research Center, Nuclear Technology Research Laboratory, Central Research Institute of Electric Power Industry, Iwado Kita, Komae-shi, Tokyo, Japan.
Manabu KoikeResearch Center for Radiation Protection, NIRS, 4-9-1 Anagawa, Inage-ku, Chiba, Japan.
Katsuko NoshiroResearch Center for Radiation Emergency Medicine, National Institute of Radiological Sciences (NIRS), Anagawa, Inage-ku, Chiba, Japan.
Kenichi TomiyamaResearch Center for Radiation Emergency Medicine, National Institute of Radiological Sciences (NIRS), Anagawa, Inage-ku, Chiba, Japan.
Chizuka ObaraResearch Center for Radiation Emergency Medicine, National Institute of Radiological Sciences (NIRS), Anagawa, Inage-ku, Chiba, Japan.
Takaya GotohResearch Center for Radiation Emergency Medicine, National Institute of Radiological Sciences (NIRS), Anagawa, Inage-ku, Chiba, Japan.
Ayako UiGenome regulation and Molecular pharmacogenomics, School of Bioscience and Biotechnology, Tokyo University of Technology, Katakuramachi, Hachioji City, Tokyo, Japan.
Akira FujimoriResearch Center for Charged Particle Therapy, NIRS, Anagawa, Inage-ku, Chiba, Japan.
Fumiaki NakayamaDepartment of Basic Medical Sciences for Radiation Damage, NIRS, National Institutes for Quantum and Radiation Sciences and Technology (QST), Anagawa, Inage-ku, Chiba, Japan.
Fumio HanaokaFaculty of Science, Gakushuin University, Mejiro, Toshima-ku, Tokyo, Japan.ORCID 0000-0002-0280-2475
Kaoru SugasawaBiosignal Research Center, and Graduate School of Science, Kobe University, Rokkodai-cho, Nada-ku, Kobe, Japan.
Ryuichi OkayasuInternational Open Laboratory (IOL), NIRS, Anagawa, Inage-ku, Chiba, Japan.
Penny A JeggoInternational Open Laboratory (IOL), NIRS, Anagawa, Inage-ku, Chiba, Japan.ORCID 0000-0002-8481-1462
Katsushi TajimaResearch Center for Radiation Emergency Medicine, National Institute of Radiological Sciences (NIRS), Anagawa, Inage-ku, Chiba, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The p300 and CBP histone acetyltransferases are recruited to DNA double-strand break (DSB) sites where they induce histone acetylation, thereby influencing the chromatin structure and DNA repair process. Whether p300/CBP at DSB sites also acetylate non-histone proteins, and how their acetylation affects DSB repair, remain unknown. Here we show that p300/CBP acetylate RAD52, a human homologous recombination (HR) DNA repair protein, at DSB sites. Using in vitro acetylated RAD52, we identified 13 potential acetylation sites in RAD52 by a mass spectrometry analysis. An immunofluorescence microscopy analysis revealed that RAD52 acetylation at DSBs sites is counteracted by SIRT2- and SIRT3-mediated deacetylation, and that non-acetylated RAD52 initially accumulates at DSB sites, but dissociates prematurely from them. In the absence of RAD52 acetylation, RAD51, which plays a central role in HR, also dissociates prematurely from DSB sites, and hence HR is impaired. Furthermore, inhibition of ataxia telangiectasia mutated (ATM) protein by siRNA or inhibitor treatment demonstrated that the acetylation of RAD52 at DSB sites is dependent on the ATM protein kinase activity, through the formation of RAD52, p300/CBP, SIRT2, and SIRT3 foci at DSB sites. Our findings clarify the importance of RAD52 acetylation in HR and its underlying mechanism.

Indexed as

DNA Breaks, Double-StrandedHomologous RecombinationAcetylationAtaxia Telangiectasia Mutated ProteinsHistone AcetyltransferasesHistone DeacetylasesHumansMicroscopy, FluorescenceRad52 DNA Repair and Recombination ProteinTwo-Hybrid System TechniquesAtaxia Telangiectasia Mutated ProteinsATM protein, humanHistone AcetyltransferasesHistone DeacetylasesRad52 DNA Repair and Recombination ProteinRAD52 protein, human

Identifiers

PMID29590107
PMCPMC5891081

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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.