ArticleNature communications2026
The photolyase/cryptochrome of Aspergillus nidulans senses oxidative stress and shuttles from nuclei to mitochondria.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Basidiomycete fruiting body morphology correlates with the convergent loss of photolyase-related proteins.iScience · 2026Article
- Integrated Transcriptomic and Metabolomic Analyses Reveal Acyl-CoA Dehydrogenase-Mediated Primordium Formation and Metabolite Synthesis inJournal of fungi (Basel, Switzerland) · 2026Article
- Role of photolyase in stress tolerance and virulence of plant-pathogenic bacteriumApplied and environmental microbiology · 2026Article
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7 authors.
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Abstract
Cryptochromes are photoreceptors with functions in the entrainment of circadian clocks or as proposed magnetoreceptors in birds or as light-independent regulators of stress responses in plants. Here, we show that the fungal cryptochrome-like photolyase CryA from Aspergillus nidulans is induced by light and oxidative stress and establishes negative-feedback loops for light- and stress-activated genes. The negative-feedback loops depend on CryA interaction with phytochrome and the HOG (high osmolarity glycerol) pathway transcription factor AtfA in nuclei. CryA translocated in less than one minute from nuclei to mitochondria in the presence of hydrogen peroxide suggesting mitochondrial functions and possibly mitochondrial-nuclear communication. The shuttle to mitochondria depended on the N-terminal extension and a cysteine therein, which probably induces conformational changes of CryA upon oxidation. Therefore, we propose CryA as a sensor for oxidative stress. Such an N-terminal extension is also present in other photolyases and some cryptochromes, suggesting evolutionary conservation of the mechanism.
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