
Putative human blue-light photoreceptors hCRY1 and hCRY2 are flavoproteins.
Recently, a human cDNA clone with high sequence homology to the photolyase/blue-light photoreceptor family was identified. The putative protein encoded by this gene exhibited a strikingly high (48% identity) degree of homology to the Drosophila melanogaster (6-4) photolyase [Todo et al. (1996) Science 272, 109-112]. We have now identified a second human gene whose amino acid sequence displays 73% identity to the first one and have named the two genes CRY1 and CRY2, respectively. The corresponding proteins hCRY1 and hCRY2 were purified and characterized as maltose-binding fusion proteins. Similar to other members of the photolyase/blue-light photoreceptor family, both proteins were found to contain FAD and a pterin cofactor. Like the plant blue-light photoreceptors, both hCRY1 and hCRY2 lacked photolyase activity on the cyclobutane pyrimidine dimer and the (6-4) photoproduct. We conclude that these newly discovered members of the photolyase/photoreceptor family are not photolyases and instead may function as blue-light photoreceptors in humans.
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Related Subject Headings
- Spectrophotometry
- Sequence Homology, Amino Acid
- Recombinant Proteins
- Receptors, G-Protein-Coupled
- Plasmids
- Photoreceptor Cells, Invertebrate
- Photoreceptor Cells
- Molecular Sequence Data
- Humans
- Flavoproteins
Citation

Published In
DOI
ISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Spectrophotometry
- Sequence Homology, Amino Acid
- Recombinant Proteins
- Receptors, G-Protein-Coupled
- Plasmids
- Photoreceptor Cells, Invertebrate
- Photoreceptor Cells
- Molecular Sequence Data
- Humans
- Flavoproteins