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PMID:19074258
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Citation |
Pokorny, R, Klar, T, Hennecke, U, Carell, T, Batschauer, A and Essen, LO (2008) Recognition and repair of UV lesions in loop structures of duplex DNA by DASH-type cryptochrome. Proc. Natl. Acad. Sci. U.S.A. 105:21023-7 |
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Abstract |
DNA photolyases and cryptochromes (cry) form a family of flavoproteins that use light energy in the blue/UV-A region for the repair of UV-induced DNA lesions or for signaling, respectively. Very recently, it was shown that members of the DASH cryptochrome subclade repair specifically cyclobutane pyrimidine dimers (CPDs) in UV-damaged single-stranded DNA. Here, we report the crystal structure of Arabidopsis cryptochrome 3 with an in-situ-repaired CPD substrate in single-stranded DNA. The structure shows a binding mode similar to that of conventional DNA photolyases. Furthermore, CPD lesions in double-stranded DNA are bound and repaired with similar efficiency as in single-stranded DNA if the CPD lesion is present in a loop structure. Together, these data reveal that DASH cryptochromes catalyze light-driven DNA repair like conventional photolyases but lack an efficient flipping mechanism for interaction with CPD lesions within duplex DNA. |
Links |
PubMed PMC2634942 Online version:10.1073/pnas.0805830106 |
Keywords |
Arabidopsis/enzymology; Arabidopsis/genetics; Arabidopsis Proteins/chemistry; Arabidopsis Proteins/genetics; Arabidopsis Proteins/metabolism; Cryptochromes; Crystallography, X-Ray; DNA Damage/physiology; DNA Damage/radiation effects; DNA Repair/physiology; DNA Repair/radiation effects; DNA, Plant/chemistry; DNA, Plant/genetics; DNA, Plant/metabolism; DNA, Single-Stranded/chemistry; DNA, Single-Stranded/genetics; DNA, Single-Stranded/metabolism; Deoxyribodipyrimidine Photo-Lyase/chemistry; Deoxyribodipyrimidine Photo-Lyase/genetics; Deoxyribodipyrimidine Photo-Lyase/metabolism; Protein Structure, Secondary/physiology; Protein Structure, Tertiary/physiology; Pyrimidine Dimers/chemistry; Pyrimidine Dimers/metabolism; Ultraviolet Rays/adverse effects |
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