Structure of the photolyase-like domain of cryptochrome 1 from
            <i>Arabidopsis thaliana</i>

Brautigam, Chad A.; Smith, Barbara; Ma, Z.; Palnitkar, Maya; Tomchick, Diana R.; Machius, Mischa; Deisenhofer, Johann

doi:10.1073/pnas.0404851101

Cited by 275 publications

(409 citation statements)

References 37 publications

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“…The results obtained with AtCry1 and AtCry2 are shown in Figure 2. From the data we calculated that AtCry1 binds ATP with a Kd = 4.2 μM and stoichiometry of 0.9 ATP to 1.0 AtCry1 enzyme, values which are in reasonable agreement with those published previously (17,18). For AtCry2, we obtained Kd = 0.9 μM and stoichiometry of 0.6 ATP to 1.0 AtCry2.…”

Section: Atp Binding Of Cryptochromessupporting

confidence: 90%

“…It has been shown previously that AtCry1 binds ATP with 1-to-1 stoichiometry (17,18) and the crystallographic structure of AtCry1 immersed in AMP-PNP solution revealed that the nucleotide analog was inserted into the cavity leading to the FAD, in a manner similar to the binding of cyclobutane pyrimidine dimer to photolyase (17). We wished to know if ATP binding was a general property of the cryptochromes.…”

Section: Atp Binding Of Cryptochromesmentioning

confidence: 99%

“…First, the crystal structure of the photolyase homology region (PHR) of AtCry1 was solved (17). The structure is very similar to that of E.coli photolyase with the notable absence of the positively charged DNA binding groove in AtCry1.…”

mentioning

confidence: 99%

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Analysis of Autophosphorylating Kinase Activities of Arabidopsis and Human Cryptochromes

Özgür

Sancar

2006

Biochemistry

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Cryptochromes are FAD-based blue-light photoreceptors that regulate growth and development in plants and the circadian clock in animals. Arabidopsis thaliana and humans possess two cryptochromes. Recently, it was found that Arabidopsis cryptochrome 1 (AtCry1) binds ATP and exhibits autokinase activity that is simulated by blue light. Similarly, it was reported that human cryptochrome 1 (HsCry1) exhibited autophosphorylation activity under blue light. To test the generality of light stimulated kinase function of cryptochromes, we purified AtCry1, AtCry2, HsCry1 and HsCry2 and probed them for kinase activity under a variety of conditions. We find that AtCry1, which contains near stoichiometric amount of FAD and human HsCry1 and HsCry2, which contain only trace amounts of FAD have autokinase activity but AtCry2, which also contains stoichiometric amounts of FAD does not. Finally, we find that the kinase activity of AtCry1 is not significantly affected by light or the redox status of the flavin cofactor.

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Section: Atp Binding Of Cryptochromessupporting

confidence: 90%

Section: Atp Binding Of Cryptochromesmentioning

confidence: 99%

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Analysis of Autophosphorylating Kinase Activities of Arabidopsis and Human Cryptochromes

Özgür

Sancar

2006

Biochemistry

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“…Additionally, this hole is of the right dimensions and polarity to allow entry of a pyrimidine dimer to within van der Waals contact distance of the isoalloxazine ring of FAD. The structure of AtCRY1 PHR domain structure is very similar to that of photolyase in many aspects, including the substrate-binding cavity; however, AtCRY1 lacks the positively charged DNAbinding groove, and in fact, many of the amino acid residues lining this groove are negatively charged which may partly be responsible for the lack of DNA-repair activity by plant CRYs (Brautigam et al 2004). The other significant aspect of the AtCRY1 PHR crystal structure is the lack of MTHF or any other second chromophore.…”

Section: Structures Of Photolyase and Cryptochromementioning

confidence: 99%

“…In contrast, only the PHR domain of AtCRY1 has been crystallized (Brautigam et al 2004). The structures of photolyases are characterized by two modular domains ( Fig.…”

Section: Structures Of Photolyase and Cryptochromementioning

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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Plant Cryptochromes and Signaling

Cashmore

2005

Handbook of Photosensory Receptors

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Structure of the photolyase-like domain of cryptochrome 1 from Arabidopsis thaliana

Cited by 275 publications

References 37 publications

Analysis of Autophosphorylating Kinase Activities of Arabidopsis and Human Cryptochromes

Analysis of Autophosphorylating Kinase Activities of Arabidopsis and Human Cryptochromes

Structure and Function of Animal Cryptochromes

Plant Cryptochromes and Signaling

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