PROSITE documentation PDOC51645Photolyase/cryptochrome alpha/beta domain profile
The photolyase/cryptochrome family consists of flavoproteins that perform various functions using blue-light photons as an energie source. It is present in all three domains of life, that is, archaea, eubacteria, and eukaryotes, and hence has arisen very early during evolution to protect genomes against the genotoxic effects of ultraviolet light originating from the sun. The photolyase/cryptochrome family is divided into two major groups: photolyases and cryptochromes. Photolyases (see <PDOC00331> and <PDOC00832>) repair cytotoxic and mutagenic UV-induced photolesions in DNA in many species from bacteria to plants and animals by using a light-dependent repair mechanism. It involves light absorption, electron transfer from an excited reduced and deprotanated FADH(-) to the flipped-out photolesion, followed by the fragmentation of the photolesions. Cryptochromes are highly related proteins that generally no longer repair damaged DNA, but function as photoreceptors. Cryptochromes regulate growth and development in plants and the circadian clock in animals [1,2,3,4,5,6,7].
Both photolyases and cryptochromes have a bilobal architecture consisting of two domains: an N-terminal α/β domain that may contain a light-harvesting chromophore to additionally broaden their activity spectra and a C-terminal α-helical catalytic domain comprising the light-sensitive FAD cofactor. Diverse classes of antenna chromophores likes 5,10-methenyltetrahydrofolate (MTHF), 8-hydroxydeazaflavin, FMN or FAD have been identified in some photolyase/cryptochrome to broaden their activity spectra, whereas many others apparently lack any bound antenna chromophores.
The photolyase/cryptochrome α/β domain adopts a dinucleotide binding fold with a five-stranded parallel β sheet flanked on both sides by α helices (see <PDB:1NP7>) [1,5].
Some proteins known to contain a photolyase/cryptochrome α/β domain are listed below:
- CPD photolyases, known as pyrimidine photolyase, repair cyclobutane pyrimidine dimer (CPD).
- (6-4) photolyases, repair (6-4) pyrimidine-pyrimidone photoproducts (6- 4PP).
- cryptochromes-DASH (CRY-DASH), photolyases with high specificity for CPDs in single-stranded DNA.
- cryptochromes, act as blue-light photoreceptors and exert various physiological functions.
The profile we developed covers the entire photolyase/cryptochrome α/β domain.
Last update:May 2012 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Brudler R. Hitomi K. Daiyasu H. Toh H. Kucho K. Ishiura M. Kanehisa M. Roberts V.A. Todo T. Tainer J.A. Getzoff E.D. |
| Title | Identification of a new cryptochrome class. Structure, function, and evolution. | |
| Source | Mol. Cell 11:59-67(2003). | |
| PubMed ID | 12535521 |
| 2 | Authors | Pokorny R. Klar T. Hennecke U. Carell T. Batschauer A. |
| Title | Essen L.-O. Recognition and repair of UV lesions in loop structures of duplex DNA by DASH-type cryptochrome. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 105:21023-21027(2008). | |
| PubMed ID | 19074258 | |
| DOI | 10.1073/pnas.0805830106 |
| 3 | Authors | Mueller M. Carell T. |
| Title | Structural biology of DNA photolyases and cryptochromes. | |
| Source | Curr. Opin. Struct. Biol. 19:277-285(2009). | |
| PubMed ID | 19487120 | |
| DOI | 10.1016/j.sbi.2009.05.003 |
| 4 | Authors | Glas A.F. Maul M.J. Cryle M. Barends T.R. Schneider S. Kaya E. Schlichting I. Carell T. |
| Title | The archaeal cofactor F0 is a light-harvesting antenna chromophore in eukaryotes. | |
| Source | Proc. Natl. Acad. Sci. U.S.A. 106:11540-11545(2009). | |
| PubMed ID | 19570997 | |
| DOI | 10.1073/pnas.0812665106 |
| 5 | Authors | Kiontke S. Geisselbrecht Y. Pokorny R. Carell T. Batschauer A. |
| Title | Essen L.-O. Crystal structures of an archaeal class II DNA photolyase and its complex with UV-damaged duplex DNA. | |
| Source | EMBO J. 30:4437-4449(2011). | |
| PubMed ID | 21892138 | |
| DOI | 10.1038/emboj.2011.313 |
| 6 | Authors | Hitomi K. Arvai A.S. Yamamoto J. Hitomi C. Teranishi M. Hirouchi T. Yamamoto K. Iwai S. Tainer J.A. Hidema J. Getzoff E.D. |
| Title | Eukaryotic Class II Cyclobutane Pyrimidine Dimer Photolyase Structure Reveals Basis for Improved Ultraviolet Tolerance in Plants. | |
| Source | J. Biol. Chem. 287:12060-12069(2012). | |
| PubMed ID | 22170053 | |
| DOI | 10.1074/jbc.M111.244020 |
| 7 | Authors | Asimgil H. Kavakli I.H. |
| Title | Purification and characterization of five members of photolyase/cryptochrome family from Cyanidioschyzon merolae. | |
| Source | Plant Sci. 185:190-198(2012). | |
| PubMed ID | 22325881 | |
| DOI | 10.1016/j.plantsci.2011.10.005 |
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