Identification of a new cryptochrome class: Structure, function, and evolution
Identification of a new cryptochrome class: Structure, function, and evolution
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DOI：
10.1016/s1097-2765(03)00008-x
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发表时间：
2003-01-01
期刊：
影响因子：
16
通讯作者：
Getzoff, ED
中科院分区：
文献类型：
--
作者：
Brudler, R;Hitomi, K;Getzoff, ED
隐花色素黄素蛋白与光依赖性DNA修复光解酶具有序列同源性，在植物中作为光感受器发挥作用，在动物中作为生物钟成分发挥作用。在这里，我们耦合拟南芥隐花色素基因的测序与系统发育，结构和功能分析，以确定一个新的隐花色素类（隐花色素DASH）在细菌和植物，这表明隐花色素进化之前的真核生物和原核生物的分歧。隐花色素晶体结构，这里报道的集胞藻隐花色素DASH，揭示了与光解酶的DNA结合和氧化还原依赖的功能，尽管不同的活性位点和相互作用的表面特征的共性。全基因组转录谱分析与DNA结合的实验确认表明，集胞藻隐色素DASH功能作为一个转录抑制因子。
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.