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• W89380135 abstract "Cryptochromes (CRYs) are flavoproteins important for the molecular clocks of animals [1Cashmore A.R. Jarillo J.A. Wu Y.J. Liu D. Cryptochromes blue light receptors for plants and animals.Science. 1999; 284: 760-765Crossref PubMed Scopus (737) Google Scholar]. The Drosophila cryptochrome (dCRY) is a circadian photoreceptor [2Emery P. So W.V. Kaneko M. Hall J.C. Rosbash M. CRY, a Drosophila clock and light-regulated cryptochrome, is a major contributor to circadian rhythm resetting and photosensitivity.Cell. 1998; 95: 669-679Abstract Full Text Full Text PDF PubMed Scopus (659) Google Scholar, 3Stanewsky R. Kaneko M. Emery P. Beretta B. Wager-Smith K. Kay S.A. Rosbash M. Hall J.C. The cryb mutation identifies cryptochrome as a circadian photoreceptor in Drosophila.Cell. 1998; 95: 681-692Abstract Full Text Full Text PDF PubMed Scopus (737) Google Scholar, 4Egan E.S. Franklin T.M. Hilderbrand-Chae M.J. McNeil G.P. Roberts M.A. Schroeder A.J. Zhang X. Jackson F.R. An extraretinally expressed insect cryptochrome with similarity to the blue light photoreceptors of mammals and plants.J. Neurosci. 1999; 19: 3665-3673PubMed Google Scholar, 5Emery P. Stanewsky R. Helfrich-Forster C. Emery-Le M. Hall J.C. Rosbash M. Drosophila CRY is a deep brain circadian photoreceptor.Neuron. 2000; 26: 493-504Abstract Full Text Full Text PDF PubMed Scopus (308) Google Scholar], whereas mouse cryptochromes (mCRY1 and mCRY2) are essential negative elements of circadian clock transcriptional feedback loops [6van der Horst G.T.J. Muijtjens M. Kobayashi K. Takano R. Kanno S. Takao M. de Wit J. Verkerk A. Eker A.P. van Leenen D. et al.Mammalian Cry1 and Cry2 are essential for maintenance of circadian rhythms.Nature. 1999; 398: 627-630Crossref PubMed Scopus (1041) Google Scholar, 7Vitaterna M.H. Selby C.P. Todo T. Niwa H. Thompson C. Fruechte E.M. Hitomi K. Thresher R.J. Ishikawa T. Miyazaki J. et al.Differential regulation of mammalian period genes and circadian rhythmicity by cryptochromes 1 and 2.Proc. Natl. Acad. Sci. USA. 1999; 96: 12114-12119Crossref PubMed Scopus (527) Google Scholar, 8Kume K. Zylka M.J. Sriram S. Shearman L.P. Weaver D.R. Jin X. Maywood E.S. Hastings M.H. Reppert S.M. mCRY1 and mCRY2 are essential components of the negative limb of the circadian clock feedback loop.Cell. 1999; 98: 193-205Abstract Full Text Full Text PDF PubMed Scopus (1233) Google Scholar, 9Okamura H. Miyake S. Sumi Y. Yamaguchi S. Yasui A. Muijtjens M. Hoeijmakers J.H. van der Horst G.T. Photic induction of mPer1 and mPer2 in Cry-deficient mice lacking a biological clock.Science. 1999; 286: 2531-2534Crossref PubMed Scopus (326) Google Scholar]. It has been proposed that reduction/oxidation (redox) reactions are important for dCRY light responsiveness [10Lin F.J. Song W. Bernstein-Meyer E. Naidoo N. Sehgal A. Photic signaling by cryptochrome in the Drosophila circadian system.Mol. Cell. Biol. 2001; 21: 7287-7294Crossref PubMed Scopus (137) Google Scholar] and mCRY1 transcriptional inhibition [11Rutter J. Reick M. Wu L.C. McKnight S.L. Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors.Science. 2001; 293: 510-514Crossref PubMed Scopus (729) Google Scholar, 12Schibler U. Ripperger J.A. Brown S.A. Circadian rhythms. Chronobiology-reducing time.Science. 2001; 293: 437-438Crossref PubMed Scopus (25) Google Scholar, 13Merrow M. Roenneberg T. Circadian clocks running on redox.Cell. 2001; 106: 141-143Abstract Full Text Full Text PDF PubMed Scopus (39) Google Scholar]. We therefore evaluated the role of redox in light-dependent activation of dCRY and in mCRY1 transcriptional inhibition in Drosophila Schneider 2 cells. Using site-directed mutagenesis, three of the four conserved flavin binding residues in dCRY were found to be essential for light responses, whereas three of the four corresponding residues in mCRY1 did not abolish transcriptional responses. Two tryptophan residues in dCRY are critical for its function and are likely involved in an intramolecular redox reaction. The corresponding tryptophan residues do not play a redox-mediated role in mCRY1 function. The data provide a multistep redox model for the light-dependent activities of dCRY and suggest that such a model does not apply to mCRY1 transcriptional responses." @default.
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• W89380135 title "Redox Potential" @default.
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