Abstract
Drosophila, Arabidopsis, Synechocystis, human (DASH)-type cryptochromes (cry-DASHs) form one subclade of the cryptochrome/photolyase family (CPF). CPF members are flavoproteins that act as DNA-repair enzymes (DNA-photolyases), or as ultraviolet(UV)-A/blue light photoreceptors (cryptochromes). In mammals, cryptochromes are essential components of the circadian clock feed-back loop. Cry-DASHs are present in almost all major taxa and were initially considered as photoreceptors. Later studies demonstrated DNA-repair activity that was, however, restricted to UV-lesions in single-stranded DNA. Very recent studies, particularly on microbial organisms, substantiated photoreceptor functions of cry-DASHs suggesting that they could be transitions between photolyases and cryptochromes.
Highlights
cryptochrome/photolyase family (CPF) members are flavoproteins that act as DNA-repair enzymes (DNA-photolyases), or as ultraviolet(UV)-A/blue light photoreceptors
Cryptochrome/photolyase family (CPF) members are present in all major taxa from archaea to mammals (Mei and Dvornyk 2015) and can be divided into 10 subfamilies based on sequence similarity and function (Öztürk 2017)
Second cofactors were not identified for classical animals and plant cryptochromes, MTHF-binding cannot be excluded for the latter based on structural similarities with class III photolyase that accommodates MTHF via two Trp residues (Scheerer et al 2015) and differ in this aspect from class I photolyase and cry-DASH
Summary
Cryptochrome/photolyase family (CPF) members are present in all major taxa from archaea to mammals (Mei and Dvornyk 2015) and can be divided into 10 subfamilies based on sequence similarity and function (Öztürk 2017). CPF members are flavoproteins that act as DNA-repair enzymes (DNA-photolyases), or as ultraviolet(UV)-A/blue light photoreceptors (cryptochromes). CPF members act as light-driven DNA-repair enzymes (DNA-photolyases), or as photoreceptors (cryptochromes) by using the same spectral range
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