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  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1999-04-30
    Description: Cryptochromes are blue, ultraviolet-A photoreceptors. They were first characterized for Arabidopsis and are also found in ferns and algae; they appear to be ubiquitous in the plant kingdom. They are flavoproteins similar in sequence to photolyases, their presumptive evolutionary ancestors. Cryptochromes mediate a variety of light responses, including entrainment of circadian rhythms in Arabidopsis, Drosophila, and mammals. Sequence comparison indicates that the plant and animal cryptochrome families have distinct evolutionary histories, with the plant cryptochromes being of ancient evolutionary origin and the animal cryptochromes having evolved relatively recently. This process of repeated evolution may have coincided with the origin in animals of a modified circadian clock based on the PERIOD, TIMELESS, CLOCK, and CYCLE proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cashmore, A R -- Jarillo, J A -- Wu, Y J -- Liu, D -- GM38409/GM/NIGMS NIH HHS/ -- GM51956/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Apr 30;284(5415):760-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Plant Science Institute, Department of Biology, University of Pennsylvania, Philadelphia, PA 19104-6018, USA. cashmore@upenn.sas.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10221900" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Nucleus/metabolism ; Circadian Rhythm ; Cryptochromes ; Deoxyribodipyrimidine Photo-Lyase/chemistry/*metabolism ; *Drosophila Proteins ; Evolution, Molecular ; *Eye Proteins ; Flavoproteins/chemistry/*physiology ; Humans ; Light ; Photoreceptor Cells/chemistry/*physiology ; *Photoreceptor Cells, Invertebrate ; Photosynthetic Reaction Center Complex Proteins/metabolism ; Plants/metabolism ; Receptors, G-Protein-Coupled ; *Signal Transduction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 1995-08-18
    Description: The arabidopsis thaliana HY4 gene encodes CRY1, a 75-kilodalton flavoprotein mediating blue light-dependent regulation of seedling development. CRY1 is demonstrated here to noncovalently bind stoichiometric amounts of flavin adenine dinucleotide (FAD). The redox properties of FAD bound by CRY1 include an unexpected stability of the neutral radical flavosemiquinone (FADH.). The absorption properties of this flavosemiquinone provide a likely explanation for the additional sensitivity exhibited by CRY1-mediated responses in the green region of the visible spectrum. Despite the sequence homology to microbial DNA photolyases, CRY1 was found to have no detectable photolyase activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, C -- Robertson, D E -- Ahmad, M -- Raibekas, A A -- Jorns, M S -- Dutton, P L -- Cashmore, A R -- GM31704/GM/NIGMS NIH HHS/ -- GM38409/GM/NIGMS NIH HHS/ -- GM51956/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 Aug 18;269(5226):968-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Pennsylvania, Philadelphia, 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638620" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*metabolism ; Arabidopsis Proteins ; Cryptochromes ; Deoxyribodipyrimidine Photo-Lyase/metabolism ; *Drosophila Proteins ; *Eye Proteins ; Flavoproteins/chemistry/genetics/*metabolism ; Genes, Plant ; Light ; Oxidation-Reduction ; *Photoreceptor Cells, Invertebrate ; Plant Proteins/chemistry/genetics/*metabolism ; Quinones/metabolism ; Receptors, G-Protein-Coupled ; Spectrum Analysis ; Ultraviolet Rays
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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