D
IPR006050

DNA photolyase, N-terminal

InterPro entry
Short nameDNA_photolyase_N
Overlapping
homologous
superfamilies
 

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
[2, 5, 3, 4, 1, 7, 6]
.

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.

This entry represents the photolyase/cryptochrome α/β domain. It adopts a dinucleotide binding fold with a five-stranded parallel β sheet flanked on both sides by α helices
[2, 1]
.

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.Localization of transforming growth factor-beta1 and type II receptor in developing normal human prostate and carcinoma tissues. Gerdes MJ, Larsen M, McBride L, Dang TD, Lu B, Rowley DR. J. Histochem. Cytochem. 46, 379-88, (1998). PMID: 9487120

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

Cross References

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