Evidence map›Paper›PMID 40790130›Full record

ArticleNature communications2025

Conservation of dark CPD photolyase function in blind cavefish.

Hongxiang Li, Carina Scheitle, Giuseppe Di Mauro, Silvia Fuselli, Susanne Fritsch-Decker, Takeshi Todo, Carsten Weiss, Daniela Vallone, Tilman Lamparter, Cristiano Bertolucci and 1 more

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
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.

Hongxiang LiInstitute of Biological and Chemical Systems - Biological Information Processing, Karlsruhe Institute of Technology, Eggenstein-Leopoldshafen, Germany.
Carina ScheitleInstitute of Biological and Chemical Systems - Biological Information Processing, Karlsruhe Institute of Technology, Eggenstein-Leopoldshafen, Germany.
Giuseppe Di MauroInternational Centre for Genetic Engineering and Biotechnology, Trieste, Italy.
Silvia FuselliDepartment of Life Science and Biotechnology, University of Ferrara, Ferrara, Italy.
Susanne Fritsch-DeckerInstitute of Biological and Chemical Systems - Biological Information Processing, Karlsruhe Institute of Technology, Eggenstein-Leopoldshafen, Germany.
Takeshi TodoRadioisotope Research Center, Institute for Radiation Science, Osaka University, Osaka, Japan.ORCID http://orcid.org/0000-0002-5778-0584
Carsten WeissInstitute of Biological and Chemical Systems - Biological Information Processing, Karlsruhe Institute of Technology, Eggenstein-Leopoldshafen, Germany.
Daniela ValloneInstitute of Biological and Chemical Systems - Biological Information Processing, Karlsruhe Institute of Technology, Eggenstein-Leopoldshafen, Germany.
Tilman LamparterBotanical Institute, Karlsruhe Institute of Technology, Karlsruhe, Germany.ORCID http://orcid.org/0000-0003-4327-9737
Cristiano BertolucciDepartment of Life Science and Biotechnology, University of Ferrara, Ferrara, Italy.ORCID http://orcid.org/0000-0003-0252-3107
Nicholas S FoulkesInstitute of Biological and Chemical Systems - Biological Information Processing, Karlsruhe Institute of Technology, Eggenstein-Leopoldshafen, Germany. nicholas.foulkes@kit.edu.ORCID http://orcid.org/0000-0002-1794-9891

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA damage is generated by various environmental stressors and so DNA repair systems must inevitably adapt to changing environments. Photolyases represent a highly conserved class of enzymes which repair UV-induced covalent crosslinks between adjacent pyrimidine bases (CPD and 6-4 photoproducts) via photoreactivation. In the blind cavefish Phreatichthys andruzzii which has evolved for millions of years completely isolated from UV radiation and visible light, we have documented multiple polymorphisms and loss of function mutations affecting both the 6-4phr and DASHphr photolyase genes while strangely, the CPDphr gene remains highly conserved. Using loss and gain of photolyase function medaka and mammalian cell lines, we reveal a novel function for CPDphr. Specifically, it enables the light-independent repair of CPD as well as 8-OHdG, an oxidatively modified form of guanosine which are both generated under oxidative stress in the absence of UV radiation. Thereby we document selective conservation of light-independent photolyase function in blind cavefish, enabling the repair of DNA damage encountered in an extreme subterranean environment.

Indexed as

Deoxyribodipyrimidine Photo-LyaseFishesFish ProteinsPyrimidine DimersAnimalsDNA DamageDNA RepairHumansMutationOryziasOxidative StressUltraviolet RaysDeoxyribodipyrimidine Photo-LyaseFish ProteinsPyrimidine Dimers

Identifiers

PMID40790130
PMCPMC12340131

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Registered trials

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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.