PUBLICATION
Identification of a New Cryptochrome Class: Structure, Function, and Evolution
- Authors
- Brudler, R., Hitomi, K., Daiyasu, H., Toh, H., Kucho, K., Ishiura, M., Kanehisa, M., Roberts, V.A., Todo, T., Tainer, J.A., and Getzoff, E.D.
- ID
- ZDB-PUB-040617-8
- Date
- 2003
- Source
- Molecular Cell 11(1): 59-67 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Arabidopsis/genetics
- Arabidopsis Proteins
- Bacterial Proteins/chemistry
- Bacterial Proteins/genetics
- Bacterial Proteins/metabolism
- Binding Sites
- Biological Clocks
- Cryptochromes
- Crystallography, X-Ray
- Cyanobacteria/chemistry
- Cyanobacteria/metabolism
- Deoxyribodipyrimidine Photo-Lyase/chemistry
- Deoxyribodipyrimidine Photo-Lyase/genetics
- Deoxyribodipyrimidine Photo-Lyase/metabolism
- Drosophila Proteins*
- Evolution, Molecular
- Eye Proteins*
- Flavoproteins*/chemistry
- Flavoproteins*/classification
- Flavoproteins*/genetics
- Flavoproteins*/metabolism
- Genes, Plant
- Humans
- Models, Molecular
- Molecular Sequence Data
- Oligonucleotide Array Sequence Analysis
- Photoreceptor Cells, Invertebrate*
- Phylogeny*
- Receptors, G-Protein-Coupled
- Sequence Alignment
- Sequence Analysis, DNA
- Substrate Specificity
- PubMed
- 12535521 Full text @ Mol. Cell
Citation
Brudler, R., Hitomi, K., Daiyasu, H., Toh, H., Kucho, K., Ishiura, M., Kanehisa, M., Roberts, V.A., Todo, T., Tainer, J.A., and Getzoff, E.D. (2003) Identification of a New Cryptochrome Class: Structure, Function, and Evolution. Molecular Cell. 11(1):59-67.
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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping