PS51645

Photolyase/cryptochrome alpha/beta domain profile

PROSITE profiles entry
Member databasePROSITE profiles
PROSITE profiles typedomain
Short namePHR_CRY_ALPHA_BETA

Description

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 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
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[5]
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. Both photolyases and cryptochromes have a bilobal architecture consisting of two domains: an N-terminal alpha/beta domain that may contain a light- harvesting chromophore to additionally broaden their activity spectra and a C- terminal alpha-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 alpha/beta domain adopts a dinucleotide binding fold with a five-stranded parallel beta sheet flanked on both sides by alpha helices
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. Some proteins known to contain a photolyase/cryptochrome alpha/beta 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 alpha/beta domain.

References

1.Crystal structures of an archaeal class II DNA photolyase and its complex with UV-damaged duplex DNA. Kiontke S, Geisselbrecht Y, Pokorny R, Carell T, Batschauer A, Essen LO. EMBO J. 30, 4437-49, (2011). View articlePMID: 21892138

2.Identification of a new cryptochrome class. Structure, function, and evolution. Brudler R, Hitomi K, Daiyasu H, Toh H, Kucho K, Ishiura M, Kanehisa M, Roberts VA, Todo T, Tainer JA, Getzoff ED. Mol. Cell 11, 59-67, (2003). View articlePMID: 12535521

3.Structural biology of DNA photolyases and cryptochromes. Muller M, Carell T. Curr Opin Struct Biol 19, 277-85, (2009). PMID: 19487120

4.The archaeal cofactor F0 is a light-harvesting antenna chromophore in eukaryotes. Glas AF, Maul MJ, Cryle M, Barends TR, Schneider S, Kaya E, Schlichting I, Carell T. Proc. Natl. Acad. Sci. U.S.A. 106, 11540-5, (2009). View articlePMID: 19570997

5.Recognition and repair of UV lesions in loop structures of duplex DNA by DASH-type cryptochrome. Pokorny R, Klar T, Hennecke U, Carell T, Batschauer A, Essen LO. Proc. Natl. Acad. Sci. U.S.A. 105, 21023-7, (2008). View articlePMID: 19074258

6.Purification and characterization of five members of photolyase/cryptochrome family from Cyanidioschyzon merolae. Asimgil H, Kavakli IH. Plant Sci. 185-186, 190-8, (2012). View articlePMID: 22325881

7.Eukaryotic class II cyclobutane pyrimidine dimer photolyase structure reveals basis for improved ultraviolet tolerance in plants. Hitomi K, Arvai AS, Yamamoto J, Hitomi C, Teranishi M, Hirouchi T, Yamamoto K, Iwai S, Tainer JA, Hidema J, Getzoff ED. J. Biol. Chem. 287, 12060-9, (2012). View articlePMID: 22170053

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