Crystal structure of a prokaryotic (6-4) photolyase with an Fe-S cluster and a 6,7-dimethyl-8-ribityllumazine antenna chromophore

Zhang, Fan; Scheerer, Patrick; Oberpichler, Inga; Lamparter, Tilman; Krauß, Norbert

doi:10.1073/pnas.1302377110

Cited by 91 publications

(179 citation statements)

References 57 publications

(51 reference statements)

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“…A series of three tryptophans (Trp-306/359/382 in Escherichia coli photolyase) is typically involved in this electron transfer. This classical Trp triad (1) is conserved in all CPFs except CPD class II photolyases (8,9) and FeS-BCP (10,11). However, site-directed mutagenesis experiments showed that these residues are not necessary for in vivo function of E. coli photolyase (12) or plant Arabidopsis thaliana cryptochrome 2 (Arath-Cry2) (13).…”

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confidence: 99%

“…In this way, light capture is increased severalfold over that of FADH Ϫ alone, which has a low extinction coefficient in the visible range. The nature of the antenna chromophore and its position within the protein structure varies between photolyases: flavin mononucleotide (FMN) (17), 8-hydroxy-5-deazaflavin (18), FAD (19), and 6,7-dimethyl-8-ribityllumazine (10,11) bind to a homologous position inside the protein at the C-terminal edge of a ␤-sheet, whereas MTHF binds to a groove at the outside of the protein (20,21). Whether cryptochromes carry an antenna chromophore is still unclear: an action spectrum for degradation of recombinant Arath-Cry2 in living cells has a peak at 380 nm, providing strong evidence for a pterin antenna chromophore in Cry2 (22).…”

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confidence: 99%

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The Class III Cyclobutane Pyrimidine Dimer Photolyase Structure Reveals a New Antenna Chromophore Binding Site and Alternative Photoreduction Pathways

Scheerer

Zhang

Kalms

et al. 2015

Journal of Biological Chemistry

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Background: Photolyases use light energy to repair UV-damaged DNA. Results: The crystal structure of a "class III CPD" photolyase reveals a new binding pocket for an "5,10-methenyltetrahydrofolate" antenna chromophore. Conclusion: Related plant cryptochromes might use the same antenna chromophore binding pocket. Significance: The photolyase crystal structure allows a better understanding of the evolutionary transition of photolyases to plant cryptochromes.

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confidence: 99%

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The Class III Cyclobutane Pyrimidine Dimer Photolyase Structure Reveals a New Antenna Chromophore Binding Site and Alternative Photoreduction Pathways

Scheerer

Zhang

Kalms

et al. 2015

Journal of Biological Chemistry

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“…Animal type II CRY are closely related to eukaryotic (6 -4) photolyases whereas plant cryptochromes are homologous to CPD photolyases. In contrast, prokaryotic (6 -4) photolyases (11) and bacterial cryptochromes (12) form a distant subfamily.…”

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confidence: 99%

Essential Role of an Unusually Long-lived Tyrosyl Radical in the Response to Red Light of the Animal-like Cryptochrome aCRY

Oldemeyer

Franz

Wenzel

et al. 2016

Journal of Biological Chemistry

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Cryptochromes constitute a group of flavin-binding blue light receptors in bacteria, fungi, plants, and insects. Recently, the response of cryptochromes to light was extended to nearly the entire visible spectral region on the basis of the activity of the animal-like cryptochrome aCRY in the green alga Chlamydomonas reinhardtii. This finding was explained by the absorption of red light by the flavin neutral radical as the dark state of the receptor, which then forms the anionic fully reduced state. In this study, time-resolved UVvisible spectroscopy on the full-length aCRY revealed an unusually long-lived tyrosyl radical with a lifetime of 2.6 s, which is present already 1 s after red light illumination of the flavin radical. Mutational studies disclosed the tyrosine 373 close to the surface to form the long-lived radical and to be essential for photoreduction. This residue is conserved exclusively in the sequences of other putative aCRY proteins distinguishing them from conventional (6 -4) photolyases. Size exclusion chromatography showed the full-length aCRY to be a dimer in the dark at 0.5 mM injected concentration with the C-terminal extension as the dimerization site. Upon illumination, partial oligomerization was observed via disulfide bridge formation at cysteine 482 in close proximity to tyrosine 373. The lack of any light response in the C-terminal extension as evidenced by FTIR spectroscopy differentiates aCRY from plant and Drosophila cryptochromes. These findings imply that aCRY might have evolved a different signaling mechanism via a light-triggered redox cascade culminating in photooxidation of a yet unknown substrate or binding partner.Cryptochromes represent a group of diverse sensory photoreceptors present in all kingdoms of life (1, 2). Together with the UV-light-dependent DNA repair enzymes, the photolyases (3), they constitute the cryptochrome/photolyase family. Members of this family share a highly conserved photolyase homology region (PHR) 2 , which comprises ϳ500 amino acids and carries a non-covalently bound flavin adenine dinucleotide (FAD) as a chromophore. The C-terminal extension (CCT) present in many cryptochromes and photolyases is strongly variable in amino acid composition and length and has been shown to be crucial for signal transduction in the Arabidopsis cryptochrome AtCRY1 (4). The diverse subfamilies of cryptochromes comprise proteins acting as central blue light sensors in bacteria, fungi, plants, and insects (animal type I CRY) (1). Moreover, CRYs are also found as the light-independent, central part of the oscillator of the biological clock in mammals (animal type II CRY) (5) and as a mediator for light-dependent magnetosensitivity in flies (6). Opposed to these findings, DASH cryptochromes have been found to repair lesions in single-stranded DNA and double-stranded loop-structured DNA in vitro (7,8). Therefore, DASH cryptochromes are more similar in terms of functionality to photolyases than cryptochromes. Among the photolyases, two different types are separated dependin...

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“…However, microorganisms that thrive in polar ecosystems have developed a variety of strategies to tolerate stressful growth conditions [7]. DNA photolyases has been reported in bacteria, fungi, plants, invertebrates, and vertebrates, and may have played an important role in the evolution of the earliest organisms on primordial Earth [8][9][10]. Although photolyase contains two non-covalent cofactor, FADH2 and MTFH or 8-HDF.…”

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confidence: 99%

Cyclobutane pyrimidine dimers photolyase from extremophilic microalga: Remarkable UVB resistance and efficient DNA damage repair

Mou

et al. 2015

Mutation Research/Fundamental and Molecular Mechanisms of Mutag

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Crystal structure of a prokaryotic (6-4) photolyase with an Fe-S cluster and a 6,7-dimethyl-8-ribityllumazine antenna chromophore

Cited by 91 publications

References 57 publications

The Class III Cyclobutane Pyrimidine Dimer Photolyase Structure Reveals a New Antenna Chromophore Binding Site and Alternative Photoreduction Pathways

The Class III Cyclobutane Pyrimidine Dimer Photolyase Structure Reveals a New Antenna Chromophore Binding Site and Alternative Photoreduction Pathways

Essential Role of an Unusually Long-lived Tyrosyl Radical in the Response to Red Light of the Animal-like Cryptochrome aCRY

Cyclobutane pyrimidine dimers photolyase from extremophilic microalga: Remarkable UVB resistance and efficient DNA damage repair

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