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Recognition and repair of UV lesions in loop structures of duplex DNA by DASH-type cryptochrome.


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.

SUBMITTER: Pokorny R 

PROVIDER: S-EPMC2634942 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature

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Recognition and repair of UV lesions in loop structures of duplex DNA by DASH-type cryptochrome.

Pokorny Richard R   Klar Tobias T   Hennecke Ulrich U   Carell Thomas T   Batschauer Alfred A   Essen Lars-Oliver LO  

Proceedings of the National Academy of Sciences of the United States of America 20081212 52


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 structur  ...[more]

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