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- W148315338 abstract "This chapter focuses on the photolyase/cryptochrome blue-light photoreceptor family that encompasses a large group of proteins from all three biological kingdoms. These proteins absorb near-ultraviolet (UV)/blue light and use the light energy to repair far UV-induced DNA damage to reset the circadian clock. The photolyase/cryptochrome family has three members: photolyase (cyclobutane pyrimidine dimer photolyase), (6–4) photolyase, and cryptochrome. Both photolyase and cryptochrome also perform light-independent functions in DNA repair and in generating the molecular circadian clock, respectively. Photolyases are monomeric proteins of 450–550 amino acids and two noncovalently bound cofactors. Escherichia coli (E. coli) photolyase is made up of two well-defined domains: an N terminal α/β domain (residues 1–132) and a C-terminal α-helical domain. Cryptochromes regulate blue-light-dependent growth and development in plants; cryptochromes have now been identified in the nonphotosynthetic bacterium Vibrio cholerae (V. cholerae), which has no known photoresponses. Cryptochromes exhibit 20–40% sequence identities to photolyases." @default.
- W148315338 created "2016-06-24" @default.
- W148315338 creator A5016678671 @default.
- W148315338 date "2004-01-01" @default.
- W148315338 modified "2023-09-24" @default.
- W148315338 title "Photolyase and Cryptochrome Blue-Light Photoreceptors" @default.
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- W148315338 doi "https://doi.org/10.1016/s0065-3233(04)69003-6" @default.
- W148315338 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15588840" @default.
- W148315338 hasPublicationYear "2004" @default.
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