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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Arabidopsis / enzymology*
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Arabidopsis / genetics
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Arabidopsis Proteins / chemistry*
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Arabidopsis Proteins / genetics
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Arabidopsis Proteins / metabolism
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Cryptochromes
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Crystallography, X-Ray
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DNA Damage / physiology
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DNA Damage / radiation effects
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DNA Repair / physiology*
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DNA Repair / radiation effects
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DNA, Plant / chemistry*
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DNA, Plant / genetics
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DNA, Plant / metabolism
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DNA, Single-Stranded / chemistry*
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DNA, Single-Stranded / genetics
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DNA, Single-Stranded / metabolism
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Deoxyribodipyrimidine Photo-Lyase / chemistry*
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Deoxyribodipyrimidine Photo-Lyase / genetics
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Deoxyribodipyrimidine Photo-Lyase / metabolism
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Protein Structure, Secondary / physiology
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Protein Structure, Tertiary / physiology
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Pyrimidine Dimers / chemistry*
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Pyrimidine Dimers / metabolism
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Ultraviolet Rays / adverse effects
Substances
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Arabidopsis Proteins
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Cryptochromes
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DNA, Plant
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DNA, Single-Stranded
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Pyrimidine Dimers
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Cry3 protein, Arabidopsis
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Deoxyribodipyrimidine Photo-Lyase