photolyase

光回復酵素、光修復酵素、フォトリアーゼ

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/05/17 06:21:41」(JST)

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FAD binding domain of DNA photolyase
A deazaflavin photolyase from Anacystis nidulans, illustrating the two light-harvesting cofactors: FADH- (yellow) and 8-HDF (cyan).
Identifiers
Symbol	FAD_binding_7
Pfam	PF03441
InterPro	IPR005101
PROSITE	PDOC00331
SCOP	1qnf
SUPERFAMILY	1qnf
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

Photolyases (EC 4.1.99.3) are DNA repair enzymes that repair damage caused by exposure to ultraviolet light. This enzyme mechanism requires visible light, preferentially from the violet/blue end of the spectrum, and is known as photoreactivation.

Photolyase is a phylogenetically old enzyme which is present and functional in many species, from the bacteria to the fungi to plants and to the animals. Photolyase is particularly important in repairing UV induced damage in plants. The photolyase mechanism is no longer working in humans and other placental mammals who instead rely on the less efficient nucleotide excision repair mechanism. It is however a component of a patent a sunscreen called Eryfotona developed to treat actinic keratosis

Photolyases bind complementary DNA strands and break certain types of pyrimidine dimers that arise when a pair of thymine or cytosine bases on the same strand of DNA become covalently linked. These dimers result in a 'bulge' of the DNA structure, referred to as a lesion. The more common covalent linkage involves the formation of a cyclobutane bridge. Photolyases have a high affinity for these lesions and reversibly bind and convert them back to the original bases.

A UV radiation induced uracil-uracil cyclobutane dimer (right) is the type of DNA damage which is repaired by DNA photolyase. Note: The above diagram is incorrectly labelled as thymine as the structures lack 5-methyl groups.

Photolyases are flavoproteins and contain two light-harvesting cofactors. All photolyases contain the two-electron-reduced FADH^-; they are divided into two main classes based on the second cofactor, which may be either the pterin methenyltetrahydrofolate (MTHF) in folate photolyases or the deazaflavin 8-hydroxy-7,8-didemethyl-5-deazariboflavin (8-HDF) in deazaflavin photolyases. Although only FAD is required for catalytic activity, the second cofactor significantly accelerates reaction rate in low-light conditions. The enzyme acts by electron transfer in which the reduced flavin FADH^- is activated by light energy and acts as an electron donor to break the pyrimidine dimer.

On the basis of sequence similarities DNA photolyases can be grouped into two classes. The first class contains enzymes from Gram-negative and Gram-positive bacteria, the halophilic archaebacteria Halobacterium halobium, fungi and plants. Proteins containing this domain also include Arabidopsis thaliana cryptochromes 1 and 2, which are blue light photoreceptors that mediate blue light-induced gene expression and modulation of circadian rhythms.

Some sunscreens include photolyase in their ingredients, claiming a reparative action on UV-damaged skin.

Human proteins containing this domain

CRY1; CRY2;

References

English Journal

• Relation between Dephasing Time and Energy Gap Fluctuations in Biomolecular Systems.

• Mallus MI1, Aghtar M1, Chandrasekaran S1, Lüdemann G2, Elstner M2, Kleinekathöfer U1.
• The journal of physical chemistry letters.J Phys Chem Lett.2016 Apr 7;7(7):1102-8. doi: 10.1021/acs.jpclett.6b00134. Epub 2016 Mar 10.
• Excitation energy and charge transfer are fundamental processes in biological systems. Because of their quantum nature, the effect of dephasing on these processes is of interest especially when trying to understand their efficiency. Moreover, recent experiments have shown quantum coherences in such
• PMID 26950038

• Single Hydrogen Bond Donation from Flavin N5 to Proximal Asparagine Ensures FAD Reduction in DNA Photolyase.

• Wijaya IM, Domratcheva T1, Iwata T, Getzoff ED2, Kandori H.
• Journal of the American Chemical Society.J Am Chem Soc.2016 Apr 6;138(13):4368-76. doi: 10.1021/jacs.5b10533. Epub 2016 Mar 22.
• The spread of the absorbance of the stable FADH(•) radical (300-700 nm) allows CPD photolyase to highly efficiently form FADH(-), making it functional for DNA repair. In this study, FTIR spectroscopy detected a strong hydrogen bond, from FAD N5-H to the carbonyl group of the Asn378 side chain, tha
• PMID 27002596

• The Trichoderma atroviride cryptochrome/photolyase genes regulate the expression of blr1-independent genes both in red and blue light.

• García-Esquivel M1, Esquivel-Naranjo EU1, Hernández-Oñate MA1, Ibarra-Laclette E2, Herrera-Estrella A3.
• Fungal biology.Fungal Biol.2016 Apr;120(4):500-12. doi: 10.1016/j.funbio.2016.01.007. Epub 2016 Jan 18.
• Quantitative transcriptome analysis led to the identification of 331 transcripts regulated by white light. Evaluation of the response to white light in mutants affected in the previously characterized blue-light receptor Blr1, demonstrated the existence of both Blr1-dependent and independent respons
• PMID 27020152

Japanese Journal

• Differential responses to high- and low-dose ultraviolet-B stress in tobacco Bright Yellow-2 cells

• Frontiers in plant science 6, 254, 2015-04
• NAID 120005647567

• （6-4）光回復酵素による2光子DNA修復の分子メカニズム

• 生物物理 55(3), 157-158, 2015
• NAID 130005072025

• FTIR study of CPD photolyase with substrate in single strand DNA

• BIOPHYSICS 11(0), 39-45, 2015
• NAID 130004940808

Related Pictures

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★リンクテーブル★

リンク元	「光修復酵素」「フォトリアーゼ」
拡張検索	「DNA photolyase」

「光修復酵素」

　　[★]

英

photolyase

関

光回復酵素、フォトリアーゼ

「フォトリアーゼ」

　　[★]

英

photolyase

関

光回復酵素、光修復酵素

「DNA photolyase」

　　[★]

DNA光回復酵素、DNA光修復酵素、DNAフォトリアーゼ

関

deoxyribodipyrimidine photo-lyase