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Photolyase family

An in-depth study of DNA repair systems (Aravind et al., 1999a) has concluded that few, if any, repair proteins occur with identical collinear domain arrangements in all three kingdoms of life. Approximately 10 enzyme families of adenosine triphosphatases (ATPases), photolyases, helicases, and nucleases were identified that are all likely to have been present in the cenancestor. These enzymatic domains are accompanied in DNA repair proteins by numerous regulatory domains. This indicates that the domain architectures of these proteins are labile, with incremental addition and/or subtraction of domains to conserved cores to be a common phenomenon except in the most closely related species. [Pg.218]

Todo T, Ryo H, Yamamoto K et al 1996 Similarity among the Drosophila (6-4)photolyase, a human photolyase homolog, and the DNA photolyase-blue-Kght photoreceptor family. Science 272 109-112... [Pg.66]

Certain flavoproteins act in a quite different role as light receptors. Cryptochromes are a family of flavoproteins, widely distributed in the eukaryotic phyla, that mediate the effects of blue light on plant development and the effects of light on mammalian circadian rhythms (oscillations in physiology and biochemistry, with a 24-hour period). The cryptochromes are homologs of another family of flavoproteins, the photolyases. Found in both prokaryotes and eukaryotes, photolyases use the energy of absorbed light to repair chemical defects inDNA. [Pg.516]

In direct repair the chemical modification that constitutes the lesions is reversed without removing and replacing nucleotides. There are four known direct repair enzymes photolyase, spore photoproduct lyase, methylguanine DNA methyltransferase, and AUcB family oxidative demethylases (1). [Pg.345]

The TREPR results clearly show that cryptochromes (exemplified for the DASH-type) readily form radical-pair species upon photoexcitation. Spin correlation of such radical-pair states (singlet vs triplet), which is a necessary condition for magnetoselectivity of radical-pair reactions, manifests itself as electron-spin polarization of EPR transitions, which can be directly detected by TREPR in real time. Such observations support the conservation of photo-induced radical-pair reactions and their relevance among proteins of the photolyase/cryptochrome family. The results are of high relevance for studies of magnetosensors based on radical-pair (photo-)chemistry in general [114], and for the assessment of the suitability of cryptochrome radical pairs in animal magnetoreception in particular [17, 115]. [Pg.59]

Cryptochrome/photolyase blue light photoreceptor family. The photoreceptors in this family are flavoproteins. They have a wide range of functions including circadian clock regulation, seed germination, and pigment accumulation. [Pg.135]

At this time, the photolyase/cryptochrome family has three members photolyase (cyclobutane pyrimidine dimer photolyase), (6-4) photolyase, and cryptochrome. A number of phylogenetic trees based on sequence comparisons of more than 100 members of the family across the three... [Pg.74]

Fig. 3. Phylogentic relationship among select members of the photolyase/ cryptochrome family. Sequences were aligned with Clustal W, and the tree was produced by the Neighbor-Joining method using MEGA 2.1. Bootstrap confidence values are shown (values for interior branches >95% are statistically significant). At, Arabidopsis thaliana Dm, Drosophila melangaster Ec, Escherichia coli Hs, Homo sapiens Vc, Vibrio cholerae. Fig. 3. Phylogentic relationship among select members of the photolyase/ cryptochrome family. Sequences were aligned with Clustal W, and the tree was produced by the Neighbor-Joining method using MEGA 2.1. Bootstrap confidence values are shown (values for interior branches >95% are statistically significant). At, Arabidopsis thaliana Dm, Drosophila melangaster Ec, Escherichia coli Hs, Homo sapiens Vc, Vibrio cholerae.
Sancar, A., Thompson, C. L., Thresher, R. J., Araujo, F., Mo, J., Ozgur, S., Vagas, E., Dawut, L., and Selby, C. P. (2000). Photolyase/cryptochrome family blue-light photoreceptors use light energy to repair DNA or set the circadian clock. CM Spring Harbor Symp. Quant. Biol. 65, 157—171. [Pg.99]

Todo, T. (1999). Functional diversity of the DNA photolyase/blue light receptor family. Mutat. Res. 236, 89-97. [Pg.100]

Worthington, E. N., Kavakli, I. H., Berrocal-Tito, G., Bondo, B. E., and Sancar, A. (2003). Purification and characterization of three members of the photolyase/ cryptochrome family blue-light photoreceptors from Vibrio chokrae. J. Biol. Chem. 278, 3914T-39154. [Pg.100]

There are a few lesions for the pyrimidine nucleotides, the most commonly-studied being the family of photoproducts. Perhaps the most common of the photoproducts is the cyclobutane pyrimidine dimer (40), and there are repair enzymes for this lesion. The mechanism of action of DNA photolyase in the repair of (40) has been investigated and in particular the role of the adenine in the FAD co-factor. Another... [Pg.161]


See other pages where Photolyase family is mentioned: [Pg.2686]    [Pg.2690]    [Pg.2686]    [Pg.2690]    [Pg.726]    [Pg.637]    [Pg.133]    [Pg.96]    [Pg.154]    [Pg.167]    [Pg.192]    [Pg.2579]    [Pg.2743]   
See also in sourсe #XX -- [ Pg.74 ]




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6-4 Photolyase photolyases

Photolyases

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