Blue Light-Dependent in Vivo and in Vitro Phosphorylation of Arabidopsis Cryptochrome 1

Shalitin, Dror; Yu, Xuhong; Maymon, Maskit; Mockler, Todd C.; Lin, Chentao

doi:10.1105/tpc.013011

Cited by 169 publications

(214 citation statements)

References 49 publications

(48 reference statements)

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“…CRY2 is particularly important in retarding hypocotyl growth in response to low intensity blue light, whereas CRY1 has a prevalent role in response to higher blue light intensity . Furthermore, CRY1 phosphorylation kinetics and activation exhibits a positive correlation with blue light intensity in direct contrast to CRY2, which exhibits a negative correlation with blue light intensity (Shalitin et al, 2002(Shalitin et al, , 2003. Thus, although CRY1, but not CRY2, has been shown to mediate a response to higher irradiances, a role for CRY1 during changes in irradiance and the high light response has not been previously described.…”

Section: Discussionmentioning

confidence: 59%

Genome-Wide Gene Expression Analysis Reveals a Critical Role for CRYPTOCHROME1 in the Response of Arabidopsis to High Irradiance

et al. 2007

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Exposure to high irradiance results in dramatic changes in nuclear gene expression in plants. However, little is known about the mechanisms by which changes in irradiance are sensed and how the information is transduced to the nucleus to initiate the genetic response. To investigate whether the photoreceptors are involved in the response to high irradiance, we analyzed expression of EARLY LIGHT-INDUCIBLE PROTEIN1 (ELIP1), ELIP2, ASCORBATE PEROXIDASE2 (APX2), and LIGHT-HARVESTING CHLOROPHYLL A/B-BINDING PROTEIN2.4 (LHCB2.4) in the phytochrome A (phyA), phyB, cryptochrome1 (cry1), and cry2 photoreceptor mutants and long hypocotyl5 (hy5) and HY5 homolog (hyh) transcription factor mutants. Following exposure to high intensity white light for 3 h (1,000 mmol quanta m 22 s 21 ) expression of ELIP1/2 and APX2 was strongly induced and LHCB2.4 expression repressed in wild type. The cry1 and hy5 mutants showed specific misregulation of ELIP1/2, and we show that the induction of ELIP1/2 expression is mediated via CRY1 in a blue light intensity-dependent manner. Furthermore, using the Affymetrix Arabidopsis (Arabidopsis thaliana) 24 K Gene-Chip, we showed that 77 of the high lightresponsive genes are regulated via CRY1, and 26 of those genes were also HY5 dependent. As a consequence of the misregulation of these genes, the cry1 mutant displayed a high irradiance-sensitive phenotype with significant photoinactivation of photosystem II, indicated by reduced maximal fluorescence ratio. Thus, we describe a novel function of CRY1 in mediating plant responses to high irradiances that is essential to the induction of photoprotective mechanisms. This indicates that high irradiance can be sensed in a chloroplast-independent manner by a cytosolic/nucleic component.

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Section: Discussionmentioning

confidence: 59%

Genome-Wide Gene Expression Analysis Reveals a Critical Role for CRYPTOCHROME1 in the Response of Arabidopsis to High Irradiance

et al. 2007

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“…It was found that both AtCRY1 and AtCRY2 are phosphorylated in vivo upon blue light exposure (Shalitin et al 2002;. Later, it was shown that purified AtCRY1 bound ATP stoichiometrically and that both AtCRY1 (Bouly et al 2003;Shalitin et al 2003) and human CRY1 (Bouly et al 2003) were autophosphorylated in a FAD-and blue-light-dependent manner. In line with these biochemical findings, the crystal structure of the AtCRY1 PHR domain contained an ATP analog in the cavity leading to FAD where the pyrimidine dimer binds in photolyase (Brautigam et al 2004).…”

Section: Protein-protein Interactionsmentioning

confidence: 99%

Structure and Function of Animal Cryptochromes

Öztürk

Song²,

Özgür³

et al. 2007

Cold Spring Harbor Symposia on Quantitative Biology

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Cryptochrome (CRY) is a photolyase-like flavoprotein with no DNA-repair activity but with known or presumed blue-light receptor function. Animal CRYs have DNA-binding and autokinase activities, and their flavin cofactor is reduced by photoinduced electron transfer. In Drosophila, CRY is a major circadian photoreceptor, and in mammals, the two CRY proteins are core components of the molecular clock and potential circadian photoreceptors. In mammals, CRYs participate in cell cycle regulation and the cellular response to DNA damage by controlling the expression of some cell cycle genes and by directly interacting with checkpoint proteins. in response to blue light (Koornneef et al. 1980), was isolated and sequenced, it revealed high sequence homology with Escherichia coli photolyase, and hence, it was in retrospect, correctly speculated that HY4 encoded a blue light photoreceptor and not a signal transducer involved in blue light response (Ahmad and Cashmore 1993). Later, this protein was named cryptochrome 1 (Lin et al. 1995, and a second Arabidopsis protein that has high homology with CRY1 identified by genomics was named CRY2 . The role of CRY in Arabidopsis growth (CRY1) and differentiation (CRY2) was well established by 1995 (see Guo et al. 1998). However, as late as 1997, it was thought that CRY had no role in circadian photoreception in plants (Millar and Kay 1997).The first report implicating CRY in the circadian clock of any organism, plant or animal, came about from the study of DNA repair, in particular, the repair of UV damage in humans by photolyase. This issue had been controversial for nearly 25 years when Li et al. (1993) conducted an exhaustive study with a highly specific and sensitive assay, concluding that humans, like all placental mammals, lacked photolyase (Li et al. 1993). However, a 1995 release of a human expressed sequence tag (EST) list contained a "photolyase ortholog" entry (Adams et al. 1995). In light of this finding and the discovery of a photolyase in Drosophila and rattlesnake (Todo et al. 1993Kim et al. 1996) that repairs the minor UV-induced lesion, the (6-4) photoproduct, in contrast to the classic photolyase that repairs cyclobutane pyrimidine dimers (CPDs), the earlier conclusion regarding the lack of photolyase in humans needed reevaluation. This was done by Hsu et al. (1996) who, in addition to the "photolyase ortholog" in public databases, discovered a second human photolyase gene. Human cells expressing both genes and recombinant proteins encoded by both genes were tested for CPD and (6-4) photolyase activities and were found to lack both. Moreover, the proteins encoded by these genes, like most photolyases (Johnson et al. 1988) and Arabidopsis CRY (Lin et al. 1995; Malhorta et al. 1995), contained FAD (flavin-adenine dinucleotide) and a pterin cofactor. Therefore, it was concluded that these proteins were not repair enzymes but that, like Arabidopsis CRYs, they performed non-repair-related blue light functions and were named human CRY1 and 2 (Hsu et al. 1996). In humans ...

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“…The C-terminal domain is important for either localization or protein stability, and its expression in Arabidopsis results in constitutive growth (Lin and Todo, 2005). Plant CRYs are phosphorylated under illumination, and gene expression control ranges from protein interactions to direct chromatin interactions (Shalitin et al, 2002(Shalitin et al, , 2003Lin and Todo, 2005). In mice, CRYs can affect the activity, interaction, degradation, or nuclear trafficking of circadian clock components in lightindependent manner (Griffin et al, 1999;Lin and Todo, 2005).…”

mentioning

confidence: 99%

More Than a Repair Enzyme:Aspergillus nidulansPhotolyase-like CryA Is a Regulator of Sexual Development

Bayram

Biesemann

Krappmann

et al. 2008

MBoC

127

116

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Cryptochromes are blue-light receptors that have presumably evolved from the DNA photolyase protein family, and the genomes of many organisms contain genes for both types of molecules. Both protein structures resemble each other, which suggests that light control and light protection share a common ancient origin. In the genome of the filamentous fungus Aspergillus nidulans, however, only one cryptochrome/photolyase-encoding gene, termed cryA, was identified. Deletion of the cryA gene triggers sexual differentiation under inappropriate culture conditions and results in upregulation of transcripts encoding regulators of fruiting body formation. CryA is a protein whose N-and C-terminal synthetic green fluorescent protein fusions localize to the nucleus. CryA represses sexual development under UVA 350-370 nm light both on plates and in submerged culture. Strikingly, CryA exhibits photorepair activity as demonstrated by heterologous complementation of a DNA repair-deficient Escherichia coli strain as well as overexpression in an A. nidulans uvsB⌬ genetic background. This is in contrast to the single deletion cryA⌬ strain, which does not show increased sensitivity toward UV-induced damage. In A. nidulans, cryA encodes a novel type of cryptochrome/photolyase that exhibits a regulatory function during light-dependent development and DNA repair activity. This represents a paradigm for the evolutionary transition between photolyases and cryptochromes. INTRODUCTIONCryptochromes (CRYs) are blue-light receptors that regulate growth, development, and the circadian clock in higher eukaryotes and that are believed to have evolved from the DNA photolyase protein family (Daiyasu et al., 2004;Lin and Todo, 2005). Photolyases, in contrast, repair UV-induced DNA damage by using a mechanism referred to as photorepair. They absorb light in the blue spectrum and transfer an excited electron from the cofactor FAD to an enzyme-bound cyclobutane pyrimidine dimer (CPD), which is thereby cleaved (Sancar, 1990(Sancar, , 1994Sancar, 1994). Cryptochromes are characterized by an N-terminal photolyase-related (PHR) region without significant photorepair activity and by a C-terminal domain of varying length, which is absent in members of the CRY-DASH subfamily (Daiyasu et al., 2004). The exact function of the CRY-DASH proteins was elusive; however, recent data imply that they are actually photolyases that specifically repair CPDs in single-stranded DNA (Selby and Sancar, 2006). The PHR domain is the most conserved region of the CRY proteins and contains the cofactor FAD required for electron transfer reactions. In Xenopus and Drosophila, the PHR domain is physiologically active even in the absence of the C-terminal domain. The C-terminal domain is important for either localization or protein stability, and its expression in Arabidopsis results in constitutive growth (Lin and Todo, 2005). Plant CRYs are phosphorylated under illumination, and gene expression control ranges from protein interactions to direct chromatin interactions (Shalitin et al....

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Blue Light-Dependent in Vivo and in Vitro Phosphorylation of Arabidopsis Cryptochrome 1

Cited by 169 publications

References 49 publications

Genome-Wide Gene Expression Analysis Reveals a Critical Role for CRYPTOCHROME1 in the Response of Arabidopsis to High Irradiance

Genome-Wide Gene Expression Analysis Reveals a Critical Role for CRYPTOCHROME1 in the Response of Arabidopsis to High Irradiance

Structure and Function of Animal Cryptochromes

More Than a Repair Enzyme:Aspergillus nidulansPhotolyase-like CryA Is a Regulator of Sexual Development

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