Cryptochromes and the Circadian Clock: The Story of a Very Complex Relationship in a Spinning World

Lopez, Loredana; Fasano, Carlo; Perrella, Giorgio; Facella, Paolo

doi:10.3390/genes12050672

Cited by 27 publications

(22 citation statements)

References 172 publications

(235 reference statements)

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“…Most of these genes are also under the control of the circadian clock. Recent reports suggest that CRYs play an important role in the entrainment of the circadian clock to the day/night cycle and the burst of gene expression during early dawn ( Balcerowicz et al, 2021 ; Lopez et al, 2021 ). While phototropins are the blue light receptors for the directed growth of plants toward the light, CRY1 has recently been shown to modulate the phototropic curvature of seedlings in blue light ( Boccaccini et al, 2020 ).…”

Section: Cryptochromes Regulate Arabidopsis Growth Development Metabo...mentioning

confidence: 99%

Signaling Mechanisms by Arabidopsis Cryptochromes

Ponnu

Hoecker

2022

Front. Plant Sci.

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Cryptochromes (CRYs) are blue light photoreceptors that regulate growth, development, and metabolism in plants. In Arabidopsis thaliana (Arabidopsis), CRY1 and CRY2 possess partially redundant and overlapping functions. Upon exposure to blue light, the monomeric inactive CRYs undergo phosphorylation and oligomerization, which are crucial to CRY function. Both the N- and C-terminal domains of CRYs participate in light-induced interaction with multiple signaling proteins. These include the COP1/SPA E3 ubiquitin ligase, several transcription factors, hormone signaling intermediates and proteins involved in chromatin-remodeling and RNA N6 adenosine methylation. In this review, we discuss the mechanisms of Arabidopsis CRY signaling in photomorphogenesis and the recent breakthroughs in Arabidopsis CRY research.

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Section: Cryptochromes Regulate Arabidopsis Growth Development Metabo...mentioning

confidence: 99%

Signaling Mechanisms by Arabidopsis Cryptochromes

Ponnu

Hoecker

2022

Front. Plant Sci.

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“…Cryptochromes (CRYs) are blue-light-sensing flavoproteins that participate in a diverse range of sensory functions across all kingdoms of life (Chaves et al, 2011;Conrad et al, 2014). In flies, these functions include, but are not limited to, blue-lightevoked depolarization of neurons (Fogle et al, 2015) and lightentrainment of circadian clocks (Lopez et al, 2021). CRYs belong to the same protein superfamily as DNA photolyases, which form a class of enzymes that are responsible for lightdependent DNA repair (Sancar, 2003).…”

Section: Introductionmentioning

confidence: 99%

Room-temperature serial synchrotron crystallography of Drosophila cryptochrome

Schneps¹,

Ganguly²,

Crane³

2022

Acta Cryst Sect D Struct Biol

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Fixed-target serial crystallography allows the high-throughput collection of diffraction data from small crystals at room temperature. This methodology is particularly useful for difficult samples that have sensitivity to radiation damage or intolerance to cryoprotection measures; fixed-target methods also have the added benefit of low sample consumption. Here, this method is applied to the structure determination of the circadian photoreceptor cryptochrome (CRY), previous structures of which have been determined at cryogenic temperature. In determining the structure, several data-filtering strategies were tested for combining observations from the hundreds of crystals that contributed to the final data set. Removing data sets based on the average correlation coefficient among equivalent reflection intensities between a given data set and all others was most effective at improving the data quality and maintaining overall completeness. CRYs are light sensors that undergo conformational photoactivation. Comparisons between the cryogenic and room-temperature CRY structures reveal regions of enhanced mobility at room temperature in loops that have functional importance within the CRY family of proteins. The B factors of the room-temperature structure correlate well with those predicted from molecular-dynamics simulations.

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“…Photolyases are important DNA repair enzymes that repair UV-induced lesions such as CPDs and 6-4 products in DNA ( Sancar 2003 ; Vechtomova et al 2020 ). Cryptochromes are homologs of photolyases that play key roles in regulating circadian clock, development, and growth of organisms ( Chaves et al 2011 ; Lopez et al 2021 ). These proteins form a large protein family called cryptochrome/photolyase family (CPF).…”

Section: Resultsmentioning

confidence: 99%

“…Meanwhile, a good result of oxygen accumulation was the formation of the ozone layer, which greatly attenuated the UV irradiation reached the surface of the Earth ( Cockell 1998 ). Thereafter, the importance of photolyases might be lowered, allowing some of them to evolve to their functionally diverse homologs, called cryptochromes ( Chaves et al 2011 ; Lopez et al 2021 ).…”

Section: Introductionmentioning

confidence: 99%

Identification of a Novel Class of Photolyases as Possible Ancestors of Their Family

Chen

Wen

et al. 2021

Molecular Biology and Evolution

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UV-irradiation induces the formation of cyclobutane pyrimidine dimers (CPDs) and 6-4 photoproducts in DNA. These two types of lesions can be directly photorepaired by CPD photolyases and 6-4 photolyases, respectively. Recently, a new class of 6-4 photolyases named iron-Sulphur Bacterial Cryptochromes and Photolyases (FeS-BCPs) were found, which were considered as the ancestors of all photolyases and their homologs — cryptochromes. However, a controversy exists regarding 6-4 photoproducts only constituting ∼10-30% of the total UV-induced lesions that primordial organisms would hardly survive without a CPD repair enzyme. By extensive phylogenetic analyses, we identified a novel class of proteins, all from eubacteria. They have relatively high similarity to class I/III CPD photolyases, especially in the putative substrate-binding and FAD-binding regions. However, these proteins are shorter, and they lack the "N-terminal α/β domain" of normal photolyases. Therefore, we named them Short Photolyase-Like (SPL). Nevertheless, similar to FeS-BCPs, some of SPLs also contain four conserved cysteines, which may also coordinate an iron-sulphur cluster as FeS-BCPs. A member from Rhodococcus fascians was cloned and expressed. It was demonstrated that the protein contains a FAD cofactor and an iron-sulphur cluster, and has CPD repair activity. It was speculated that this novel class of photolyases may be the real ancestors of the cryptochrome/photolyase family.

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Cryptochromes and the Circadian Clock: The Story of a Very Complex Relationship in a Spinning World

Cited by 27 publications

References 172 publications

Signaling Mechanisms by Arabidopsis Cryptochromes

Signaling Mechanisms by Arabidopsis Cryptochromes

Room-temperature serial synchrotron crystallography of Drosophila cryptochrome

Identification of a Novel Class of Photolyases as Possible Ancestors of Their Family

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