ArticlePlant physiology2004
The CPH1 gene of Chlamydomonas reinhardtii encodes two forms of cryptochrome whose levels are controlled by light-induced proteolysis.
Article in Plant physiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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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.
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Who cites it
32 citing papers in PubMed, 78 citations in OpenAlex.
- The Function and Photoregulatory Mechanisms of Cryptochromes From Moso Bamboo (Frontiers in plant science · 2022Article
- Transcriptomic and Proteomic Characterizations of the Molecular Response to Blue Light and Salicylic Acid inMarine drugs · 2021Article
- Diel transcriptional oscillations of light-sensitive regulatory elements in open-ocean eukaryotic plankton communities.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Plant Cryptochromes Illuminated: A Spectroscopic Perspective on the Mechanism.Frontiers in chemistry · 2021Review
- The World of Algae Reveals a Broad Variety of Cryptochrome Properties and Functions.Frontiers in plant science · 2021Review
- Review
- Mechanisms of Cryptochrome-Mediated Photoresponses in Plants.Annual review of plant biology · 2020Article
- Autophagic flux is required for the synthesis of triacylglycerols and ribosomal protein turnover in Chlamydomonas.Journal of experimental botany · 2018Article
- Algal light sensing and photoacclimation in aquatic environments.Plant, cell & environment · 2017Review
- An Animal-Like Cryptochrome Controls thePlant physiology · 2017Article
- A Plant Cryptochrome Controls Key Features of thePlant physiology · 2017Article
- CSL encodes a leucine-rich-repeat protein implicated in red/violet light signaling to the circadian clock in Chlamydomonas.PLoS genetics · 2017Article
- RNA-seq analysis of the transcriptional response to blue and red light in the extremophilic red alga, Cyanidioschyzon merolae.Functional & integrative genomics · 2016Article
- UV-B Perception and Acclimation in Chlamydomonas reinhardtii.The Plant cell · 2016Article
- Article
- Diversity of plant circadian clocks: Insights from studies of Chlamydomonas reinhardtii and Physcomitrella patens.Plant signaling & behavior · 2016Article
- Transcriptional analysis of Volvox photoreceptors suggests the existence of different cell-type specific light-signaling pathways.Current genetics · 2015Article
- Proton transfer to flavin stabilizes the signaling state of the blue light receptor plant cryptochrome.The Journal of biological chemistry · 2015Article
- Chlamydomonas reinhardtii strain CC-124 is highly sensitive to blue light in addition to green and red light in resetting its circadian clock, with the blue-light photoreceptor plant cryptochrome likely acting as negative modulator.Plant physiology and biochemistry : PPB · 2014Article
- Using natural selection to explore the adaptive potential of Chlamydomonas reinhardtii.PloS one · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Cryptochromes are proteins related to DNA photolyases and have been shown to function as blue-light photoreceptors and to play important roles in circadian rhythms in both plants and animals. The CPH1 gene from Chlamydomonas reinhardtii was originally predicted to encode a putative cryptochrome protein of 867 amino acids with a predicted molecular mass of 91 kD (Small et al., 1995). However, western blotting with antibodies specific to the CPH1 protein revealed the presence of two proteins that migrate at apparent molecular mass of approximately 126 and 143 kD. A reexamination of the assigned intron-exon boundaries has shown that the previously assigned intron 7 is in fact part of exon 7 which leads to a predicted protein of 1,007 amino acids corresponding to a size of 104.6 kD. The two forms of CPH1 that migrate slower on SDS-PAGE presumably result from unknown posttranslational modifications. In C. reinhardtii cells synchronized by light to dark cycles, the two slow migrating forms of CPH1 protein accumulate in the dark and disappear rapidly in the light. Both red and blue light are effective at inducing the degradation of the CPH1 proteins. Proteasomes are implicated because degradation is inhibited by MG132, a proteasome inhibitor. Studies with deletion mutants indicate that the C-terminal region is important for both the posttranslational modification and the protein's stability under both light and dark conditions.
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