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Structure and Function of Animal Cryptochromes
Author(s) -
Nuri Öztürk,
Sang-Hun Song,
Sezgin Özgür,
Christopher P. Selby,
Logan M Morrison,
Carrie L. Partch,
Dongping Zhong,
Aziz Sancar
Publication year - 2007
Publication title -
cold spring harbor symposia on quantitative biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.615
H-Index - 77
eISSN - 1943-4456
pISSN - 0091-7451
DOI - 10.1101/sqb.2007.72.015
Subject(s) - cryptochrome , flavoprotein , photolyase , circadian clock , dna repair , microbiology and biotechnology , biology , flavin group , dna , function (biology) , cofactor , gene , genetics , biochemistry , enzyme
Cryptochrome (CRY) is a photolyase-like flavoprotein with no DNA-repair activity but with known or presumed blue-light receptor function. Animal CRYs have DNA-binding and autokinase activities, and their flavin cofactor is reduced by photoinduced electron transfer. In Drosophila, CRY is a major circadian photoreceptor, and in mammals, the two CRY proteins are core components of the molecular clock and potential circadian photoreceptors. In mammals, CRYs participate in cell cycle regulation and the cellular response to DNA damage by controlling the expression of some cell cycle genes and by directly interacting with checkpoint proteins.

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