Show simple item record

dc.contributor.authorFroy, Oren
dc.contributor.authorChang, Dennis C.
dc.contributor.authorReppert, Steven M.
dc.date2022-08-11T08:10:50.000
dc.date.accessioned2022-08-23T17:22:01Z
dc.date.available2022-08-23T17:22:01Z
dc.date.issued2002-01-22
dc.date.submitted2016-10-31
dc.identifier.issn0960-9822
dc.identifier.pmid11818067
dc.identifier.urihttp://hdl.handle.net/20.500.14038/48655
dc.description<p>Dennis Chang is a PhD student in the Reppert Lab at UMass Medical School.</p>
dc.description.abstractCryptochromes (CRYs) are flavoproteins important for the molecular clocks of animals. The Drosophila cryptochrome (dCRY) is a circadian photoreceptor, whereas mouse cryptochromes (mCRY1 and mCRY2) are essential negative elements of circadian clock transcriptional feedback loops. It has been proposed that reduction/oxidation (redox) reactions are important for dCRY light responsiveness and mCRY1 transcriptional inhibition. 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.
dc.language.isoen_US
dc.publisherCell Press
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11818067&dopt=Abstract">Link to article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1016/S0960-9822(01)00656-X
dc.rightsCitation: Froy O, Chang DC, Reppert SM. Redox potential: differential roles in dCRY and mCRY1 functions. Curr Biol. 2002 Jan 22;12(2):147-52. PubMed PMID: 11818067.
dc.subjectNeuroscience and Neurobiology
dc.titleRedox potential: differential roles in dCRY and mCRY1 functions
dc.typeJournal Article
dc.source.journaltitleCurrent biology : CB
dc.source.volume12
dc.source.issue2
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/reppert_student_pubs/2
dc.identifier.contextkey9323705
html.description.abstract<p>Cryptochromes (CRYs) are flavoproteins important for the molecular clocks of animals. The Drosophila cryptochrome (dCRY) is a circadian photoreceptor, whereas mouse cryptochromes (mCRY1 and mCRY2) are essential negative elements of circadian clock transcriptional feedback loops. It has been proposed that reduction/oxidation (redox) reactions are important for dCRY light responsiveness and mCRY1 transcriptional inhibition. 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.</p>
dc.identifier.submissionpathreppert_student_pubs/2
dc.contributor.departmentReppert Lab
dc.contributor.departmentNeurobiology
dc.source.pages147-52
dc.contributor.studentDennis C. Chang


This item appears in the following Collection(s)

Show simple item record