Characterization of two members of the cryptochrome/photolyase family from Ostreococcus tauri provides insights into the origin and evolution of cryptochromes
Abstract
Cryptochromes (Crys) are blue light receptors believed to have evolved from the DNA photolyase protein family, implying that light control and light protection share a common ancient origin. In this paper, we report the identification of five genes of the Cry/photolyase family (CPF) in two green algae of the Ostreococcus genus. Phylogenetic analyses were used to confidently assign three of these sequences to cyclobutane pyrimidine dimer (CPD) photolyases, one of them to a DASH‐type Cry, and a third CPF gene has high homology with the recently described diatom CPF1 that displays a bifunctional activity. Both purified OtCPF1 and OtCPF2 proteins show non‐covalent binding to flavin adenine dinucleotide (FAD), and additionally to 5,10‐methenyl‐tetrahydrofolate (MTHF) for OtCPF2. Expression analyses revealed that all five CPF members of Ostreococcus tauri are regulated by light. Furthermore, we show that OtCPF1 and OtCPF2 display photolyase activity and that OtCPF1 is able to interact with the CLOCK:BMAL heterodimer, transcription factors regulating circadian clock function in other organisms. Finally, we provide evidence for the involvement of OtCPF1 in the maintenance of the Ostreococcus circadian clock. This work improves our understanding of the evolutionary transition between photolyases and Crys.
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The LUCA lineage contained photolyase.
“Phylogenetic analyses indicate that photolyase was present in the lineage of the Last Universal Common Ancestor (LUCA) and that the observed paraphyletic distribution across the three domains is due to widespread gene loss (Heijde et al. 2010;Kanai et al. 1997).”
From Environmental Adaptation from the Origin of Life to the Last Universal Common Ancestor (2018) · cites this paper as Heijde et al. 2010
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The cryptochromes: blue light photoreceptors in plants and animals
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- Authors
- HEIJDE, M., ZABULON, G., CORELLOU, F., ISHIKAWA, T., BRAZARD, J., USMAN, A., SANCHEZ, F., PLAZA, P., MARTIN, M., FALCIATORE, A., TODO, T., BOUGET, F., & BOWLER, C.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- The University of Osaka (JP)
- Corresponding author
- BOWLER, CHRIS
- ORCID
- Venue
- Plant, Cell & Environment
- Publisher
- Wiley
- Published
- 2010-09-07
- Volume
- 33
- Issue
- 10
- Pages
- 1614-1626
- ISSN
- 0140-7791 (ISSN-L)
- 1365-3040
- OpenAlex
- W2105873119
- Cited by
- 130
- References
- 62
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 4 · 2023: 7 · 2022: 10 · 2021: 10 · 2020: 10 · 2019: 7 · 2018: 2 · 2017: 12 · 2016: 8 · 2015: 7 · 2014: 14 · 2013: 7 · 2012: 14
- FWCI
- 12.70
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Plant Cell & Environment (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Japan Society for the Promotion of Science (22310035)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Light effects on plants
- Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Circadian rhythm and melatonin
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Keywords
- cryptochrome, photolyase, Ostreococcus tauri, blue light receptor, light-regulated gene expression, circadian clock, green algae
- MeSH terms
- Chlorophyta, Deoxyribodipyrimidine Photo-Lyase, DNA Repair, Biological Evolution, Light, Phylogeny, Protein Binding, Repressor Proteins, Spectrometry, Fluorescence, Photoperiod, Gene Expression Regulation, Plant, DNA, Plant, Cryptochromes, Circadian Clocks
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