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Query: EC:4.1.99.3 (PRE)
 1,923 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cryptochromes are photosensory receptors mediating light regulation of growth and development in plants. Since the isolation of the Arabidopsis CRY1 gene in 1993, cryptochromes have been found in every multicellular eukaryote examined. Most plant cryptochromes have a chromophore-binding domain that shares similar structure with DNA photolyase, and a carboxyl terminal extension that contains a DQXVP-acidic-STAES (DAS) domain conserved from moss, to fern, to angiosperm. In Arabidopsis, cryptochromes are nuclear proteins that mediate light control of stem elongation, leaf expansion, photoperiodic flowering, and the circadian clock. Cryptochromes may act by interacting with proteins such as phytochromes, COP1, and clock proteins, or/and chromatin and DNA. Recent studies suggest that cryptochromes undergo a blue light-dependent phosphorylation that affects the conformation, intermolecular interactions, physiological activities, and protein abundance of the photoreceptors.
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PMID:Cryptochrome structure and signal transduction. 1450

Cryptochromes are blue light receptors that mediate various light-induced responses in plants and animals. They share sequence similarity to photolyases, flavoproteins that catalyze the repair of UV light-damaged DNA, but do not have photolyase activity. Arabidopsis cryptochromes work together with the red/far-red light receptor phytochromes to regulate various light responses, including the regulation of cell elongation and photoperiodic flowering, and are also found to act together with the blue light receptor phototropins to mediate blue light regulation of stomatal opening. The signaling mechanism of Arabidopsis cryptochromes is mediated through negative regulation of COP1 by direct CRY-COP1 interaction through CRY C-terminal domain. Arabidopsis CRY dimerized through its N-terminal domain and dimerization of CRY is required for light activation of the photoreceptor activity. Recently, significant progresses have been made in our understanding of cryptochrome functions in other dicots such as pea and tomato and lower plants including moss and fern. This review will focus on recent advances in functional and mechanism characterization of cryptochromes in plants. It is not intended to cover every aspect of the field; readers are referred to other review articles for historical perspectives and a more comprehensive understanding of this photoreceptor.
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PMID:Cryptochrome signaling in plants. 1700 22

Obligate photoautotrophs such as plants must capture energy from sunlight and are therefore exposed to the damaging collateral effects of ultraviolet (UV) irradiation, especially on DNA. Here we investigated the interconnection between light signaling and DNA repair, two concomitant pathways during photomorphogenesis, the developmental transition associated with the first light exposure. It is shown that combination of an enhanced sunscreen effect and photoreactivation confers a greater level of tolerance to damaging UV-C doses in the constitutive photomorphogenic de-etiolated1-1 (det1--1) Arabidopsis mutant. In darkness, expression of the PHR1 and UVR3 photolyase genes, responsible for photoreactivation, is maintained at a basal level through the positive action of HY5 and HYH photomorphogenesis-promoting transcription factors and the repressive effects of DET1 and COP1. Upon light exposure, HY5 and HYH activate PHR1 gene expression while the constitutively expressed nuclear-localized DET1 protein exerts a strong inhibitory effect. Altogether, the data presented indicate a dual role for DET1 in controlling expression of light-responsive and DNA repair genes, and describe more precisely the contribution of photomorphogenic regulators in the control of light-dependent DNA repair.
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PMID:det1-1-induced UV-C hyposensitivity through UVR3 and PHR1 photolyase gene over-expression. 2048 84

CRYPTOCHROMES (CRYs) are photolyase-like ultraviolet-A/blue light photoreceptors that mediate various light responses in plants. The signaling mechanism of Arabidopsis CRYs (CRY1 and CRY2) involves direct CRY-COP1 interaction. Here, we report that CRY1(G380R), which carries a Gly-to-Arg substitution of the highly conserved G380 in the photolyase-related (PHR) domain of Arabidopsis CRY1, shows constitutive CRY1 photoreceptor activity in Arabidopsis. Transgenic plants overexpressing CRY1(G380R) display a constitutively photomorphogenic (COP) phenotype in darkness, as well as a dramatic early flowering phenotype under short-day light conditions (SD). We further demonstrate that CRY1(G380R) expression driven by the native CRY1 promoter also results in a COP phenotype in darkness. Moreover, overexpression of either the Arabidopsis homolog CRY2(G377R) or the rice ortholog OsCRY1b(G388R) of CRY1(G380R) in Arabidopsis results in a COP phenotype in darkness. Cellular localization studies indicate that CRY1(G380R) co-localizes with COP1 in the same nuclear bodies (NBs) in vivo and inhibits the nuclear accumulation of COP1 in darkness. These results suggest that the conserved G380 may play a critical role in regulating the photoreceptor activity of plant CRYs and that CRY1(G380R) might constitutively phenocopy the photo-activated CRY1 in darkness and thus constitutively mediate CRY1 signaling.
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PMID:Substitution of a conserved glycine in the PHR domain of Arabidopsis cryptochrome 1 confers a constitutive light response. 2176 76