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Gene Review

PHR1  -  photolyase 1

Arabidopsis thaliana

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Disease relevance of PHR1

  • The PHR1 protein complements a photolyase-deficient mutant of Escherichia coli and thus confers photoreactivation activity [1].
  • Recent biochemical studies demonstrate that the Cryptochrome-Drosophila, Arabidopsis, Synechocystis, Human (Cry-DASH) subfamily of cryptochromes have photolyase activity exclusively for single-stranded cyclobutane pyrimidine dimer (CPD)-containing DNA substrate [Selby C, Sancar A (2006) Proc Natl Acad Sci USA 103:17696-17700] [2].

High impact information on PHR1

  • Increases in recombination are accompanied by a strong induction of photolyase and Rad51 gene expression [3].
  • Despite the sequence homology to microbial DNA photolyases, CRY1 was found to have no detectable photolyase activity [4].
  • One of the mutants, phr1 (phosphate starvation response 1), displayed reduced response of AtIPS1::GUS to Pi starvation, and also had a broad range of Pi starvation responses impaired, including the responsiveness of various other Pi starvation-induced genes and metabolic responses, such as the increase in anthocyanin accumulation [5].
  • We conclude that PHR1 represents a genuine plant photolyase gene and that the plant genes with homology to type I photolyases (the cryptochrome family of blue light photoreceptors) do not contribute to photoreactivation repair, at least in the case of Arabidopsis [1].
  • Instead, the PHR1 gene encodes an amino acid sequence with significant homology to the recently characterized type II photolyases identified in a number of prokaryotic and animal systems [1].

Chemical compound and disease context of PHR1


Biological context of PHR1


Associations of PHR1 with chemical compounds


Other interactions of PHR1

  • PHR1 is a single-copy gene and is not expressed in dark-grown etiolated seedlings: the message is light inducible, which is similar to the expression profile for photoreactivation activity in plants [1].
  • We describe the isolation and characterization of two new classes of mutants of Arabidopsis, termed uvr2 and uvr3, that are defective in the photoreactivation of CPDs and 6-4 products, respectively [8].
  • Cryptochromes 1 and 2 are photolyase-like receptors that regulate hypocotyl growth and flowering time; phototropin mediates phototropism in response to blue light [15].

Analytical, diagnostic and therapeutic context of PHR1


  1. An enzyme similar to animal type II photolyases mediates photoreactivation in Arabidopsis. Ahmad, M., Jarillo, J.A., Klimczak, L.J., Landry, L.G., Peng, T., Last, R.L., Cashmore, A.R. Plant Cell (1997) [Pubmed]
  2. Crystal structure of cryptochrome 3 from Arabidopsis thaliana and its implications for photolyase activity. Huang, Y., Baxter, R., Smith, B.S., Partch, C.L., Colbert, C.L., Deisenhofer, J. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  3. Elevated UV-B radiation reduces genome stability in plants. Ries, G., Heller, W., Puchta, H., Sandermann, H., Seidlitz, H.K., Hohn, B. Nature (2000) [Pubmed]
  4. Association of flavin adenine dinucleotide with the Arabidopsis blue light receptor CRY1. Lin, C., Robertson, D.E., Ahmad, M., Raibekas, A.A., Jorns, M.S., Dutton, P.L., Cashmore, A.R. Science (1995) [Pubmed]
  5. A conserved MYB transcription factor involved in phosphate starvation signaling both in vascular plants and in unicellular algae. Rubio, V., Linhares, F., Solano, R., Martín, A.C., Iglesias, J., Leyva, A., Paz-Ares, J. Genes Dev. (2001) [Pubmed]
  6. Light-induced electron transfer in Arabidopsis cryptochrome-1 correlates with in vivo function. Zeugner, A., Byrdin, M., Bouly, J.P., Bakrim, N., Giovani, B., Brettel, K., Ahmad, M. J. Biol. Chem. (2005) [Pubmed]
  7. An Arabidopsis photolyase mutant is hypersensitive to ultraviolet-B radiation. Landry, L.G., Stapleton, A.E., Lim, J., Hoffman, P., Hays, J.B., Walbot, V., Last, R.L. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  8. Photorepair mutants of Arabidopsis. Jiang, C.Z., Yee, J., Mitchell, D.L., Britt, A.B. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  9. Genome-wide analysis of the Arabidopsis leaf transcriptome reveals interaction of phosphate and sugar metabolism. M??ller, R., Morant, M., Jarmer, H., Nilsson, L., Nielsen, T.H. Plant Physiol. (2007) [Pubmed]
  10. Molecular cloning of Arabidopsis photolyase gene (PHR1) and characterization of its promoter region. Sakamoto, A., Tanaka, A., Watanabe, H., Tano, S. DNA Seq. (1998) [Pubmed]
  11. Repair of UV damage in plants by nucleotide excision repair: Arabidopsis UVH1 DNA repair gene is a homolog of Saccharomyces cerevisiae Rad1. Liu, Z., Hossain, G.S., Islas-Osuna, M.A., Mitchell, D.L., Mount, D.W. Plant J. (2000) [Pubmed]
  12. Class II DNA photolyase from Arabidopsis thaliana contains FAD as a cofactor. Kleiner, O., Butenandt, J., Carell, T., Batschauer, A. Eur. J. Biochem. (1999) [Pubmed]
  13. Human blue-light photoreceptor hCRY2 specifically interacts with protein serine/threonine phosphatase 5 and modulates its activity. Zhao, S., Sancar, A. Photochem. Photobiol. (1997) [Pubmed]
  14. Characterization of Arabidopsis photolyase enzymes and analysis of their role in protection from ultraviolet-B radiation. Waterworth, W.M., Jiang, Q., West, C.E., Nikaido, M., Bray, C.M. J. Exp. Bot. (2002) [Pubmed]
  15. Plant blue-light receptors. Lin, C. Trends Plant Sci. (2000) [Pubmed]
  16. Characteristic structure and environment in FAD cofactor of (6-4) photolyase along function revealed by resonance Raman spectroscopy. Li, J., Uchida, T., Ohta, T., Todo, T., Kitagawa, T. The journal of physical chemistry. B, Condensed matter, materials, surfaces, interfaces & biophysical. (2006) [Pubmed]
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