PubMed · 12535521
Identification of a new cryptochrome class. Structure, function, and evolution.
Abstract
Cryptochrome flavoproteins, which share sequence homology with light-dependent DNA repair photolyases, function as photoreceptors in plants and circadian clock components in animals. Here, we coupled sequencing of an Arabidopsis cryptochrome gene with phylogenetic, structural, and functional analyses to identify a new cryptochrome class (cryptochrome DASH) in bacteria and plants, suggesting that cryptochromes evolved before the divergence of eukaryotes and prokaryotes. The cryptochrome crystallographic structure, reported here for Synechocystis cryptochrome DASH, reveals commonalities with photolyases in DNA binding and redox-dependent function, despite distinct active-site and interaction surface features. Whole genome transcriptional profiling together with experimental confirmation of DNA binding indicated that Synechocystis cryptochrome DASH functions as a transcriptional repressor.
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Ronald Brudler, Kenichi Hitomi, Hiromi Daiyasu, Hiroyuki Toh, Ken-ichi Kucho, Masahiro Ishiura, Minoru Kanehisa, Victoria A Roberts, Takeshi Todo, John A Tainer, Elizabeth D Getzoff. 2003. Identification of a new cryptochrome class. Structure, function, and evolution.. https://doi.org/10.1016/s1097-2765(03)00008-x
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