ArticleEukaryotic cell2004
The circadian RNA-binding protein CHLAMY 1 represents a novel type heteromer of RNA recognition motif and lysine homology domain-containing subunits.
Article in Eukaryotic cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 55 citations in OpenAlex.
- Multiomics studies reveal how ambient temperature changes govern cellular responses of Chlamydomonas.The Plant cell · 2026Article
- Roles for theJournal of biological rhythms · 2023Article
- Evolution of circadian clocks along the green lineage.Plant physiology · 2022Article
- The enigmatic clock of dinoflagellates, is it unique?Frontiers in microbiology · 2022Review
- Alternative Splice Variant Sheds Light on Temperature Acclimation in Algae.Plant physiology · 2018Article
- A Musashi Splice Variant and Its Interaction Partners Influence Temperature Acclimation inPlant physiology · 2018Article
- An Animal-Like Cryptochrome Controls thePlant physiology · 2017Article
- A Plant Cryptochrome Controls Key Features of thePlant physiology · 2017Article
- Diversity of plant circadian clocks: Insights from studies of Chlamydomonas reinhardtii and Physcomitrella patens.Plant signaling & behavior · 2016Article
- Circadian rhythms and post-transcriptional regulation in higher plants.Frontiers in plant science · 2015Review
- RNA around the clock - regulation at the RNA level in biological timing.Frontiers in plant science · 2015Review
- Cell-type specific light-mediated transcript regulation in the multicellular alga Volvox carteri.BMC genomics · 2014Article
- Modeling temperature entrainment of circadian clocks using the Arrhenius equation and a reconstructed model from Chlamydomonas reinhardtii.Journal of biological physics · 2012Article
- Predicting the physiological role of circadian metabolic regulation in the green alga Chlamydomonas reinhardtii.PloS one · 2011Article
- Spotlight on post-transcriptional control in the circadian system.Cellular and molecular life sciences : CMLS · 2011Review
- How the green alga Chlamydomonas reinhardtii keeps time.Protoplasma · 2010Review
- Multiple roles and interaction factors of an E-box element in Chlamydomonas reinhardtii.Plant physiology · 2010Article
- Analysis of flagellar phosphoproteins from Chlamydomonas reinhardtii.Eukaryotic cell · 2009Article
- Both subunits of the circadian RNA-binding protein CHLAMY1 can integrate temperature information.Plant physiology · 2008Article
- A heteromeric RNA-binding protein is involved in maintaining acrophase and period of the circadian clock.Plant physiology · 2006Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The RNA-binding protein CHLAMY 1 from Chlamydomonas reinhardtii binds specifically to UG> or =7 repeat sequences situated in the 3' untranslated regions of several mRNAs. Its binding activity is controlled by the circadian clock. The biochemical purification and characterization of CHLAMY 1 revealed a novel type of RNA-binding protein. It includes two different subunits (named C1 and C3), whose interaction appears necessary for RNA binding. One of them (C3) belongs to the proteins of the CELF (CUG-BP-ETR-3-like factors) family and thus bears three RNA recognition motif domains. The other is composed of three lysine homology domains and a protein-protein interaction domain (WW). The subunits C1 and C3 have theoretical molecular masses of 45 and 52 kDa, respectively, and are present in nearly equal amounts during the circadian cycle. At the beginning of the subjective night, both can be found in protein complexes of 100 to 160 kDa. However, during subjective day when binding activity of CHLAMY 1 is low, the C1 subunit in addition is present in a high-molecular-mass protein complex of more than 680 kDa. These data indicate posttranslational control of the circadian binding activity of CHLAMY 1. Notably, the C3 subunit shows significant homology to the rat CUG-binding protein 2. Anti-C3 antibodies can recognize the rat homologue, which can also be found in a protein complex in this vertebrate.
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