ArticleScientific reports2019
Structural changes within the bifunctional cryptochrome/photolyase CraCRY upon blue light excitation.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 31 citations in OpenAlex.
- Conserved structural motifs in PAS, LOV, and CRY proteins regulate circadian rhythms and are therapeutic targets.FEBS letters · 2026Review
- Capturing structural intermediates in an animal-like cryptochrome photoreceptor by time-resolved crystallography.Science advances · 2025Article
- Full-Length Cryptochrome 1 in the Outer Segments of the Retinal Blue Cone Photoreceptors in Humans and Great Apes Suggests a Role Beyond Transcriptional Repression.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Dynamics and mechanism of DNA repair by a bifunctional cryptochrome.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- A structural decryption of cryptochromes.Frontiers in chemistry · 2024Review
- A marine cryptochrome with an inverse photo-oligomerization mechanism.Nature communications · 2023Article
- Direct experimental observation of blue-light-induced conformational change and intermolecular interactions of cryptochrome.Communications biology · 2022Article
- Animal behavior is central in shaping the realized diel light niche.Communications biology · 2022Article
- Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems.Chemical reviews · 2022Review
- Structural basis of the radical pair state in photolyases and cryptochromes.Chemical communications (Cambridge, England) · 2022Article
- The World of Algae Reveals a Broad Variety of Cryptochrome Properties and Functions.Frontiers in plant science · 2021Review
- A topologically distinct class of photolyases specific for UV lesions within single-stranded DNA.Nucleic acids research · 2020Article
- Common Functions of Disordered Proteins across Evolutionary Distant Organisms.International journal of molecular sciences · 2020Review
- Molecular Cloning and Expression of a Cryptochrome Gene CiCRY-DASH1 from the Antarctic microalga Chlamydomonas sp. ICE-L.Molecular biotechnology · 2020Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cryptochromes (CRYs) are an ubiquitously occurring class of photoreceptors, which are important for regulating the circadian rhythm of animals via a time-delayed transcription-translation feedback loop (TTFL). Due to their protein architecture and common FAD chromophore, they belong to the same superfamily as photolyases (PHLs), an enzyme class that repairs UV-induced DNA lesions upon blue light absorption. Apart from their different functions the only prominent structural difference between CRY and PHL is the highly variable C-terminal extension (CTE) of the former. The nature of the CTE is still unclear and highly speculated. In this study, we show by hydrogen/deuterium exchange and subsequent mass-spectrometric analysis that the CTE of the animal-like cryptochrome from the green algae Chlamydomonas reinhardtii (CraCRY) binds to the surface of the photolyase homology region, which flanks the DNA binding site. We also compared the fully oxidized and fully reduced states of the flavoprotein and designed a tool, so called light chamber, for automated HDX-MS measurements of photoreceptors in defined photostates. We could observe some striking differences between the two photostates and propose a model for light-dependent switching of this bifunctional cryptochrome.
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