Structural changes within the bifunctional cryptochrome/photolyase CraCRY upon blue light excitation.

ABSTRACT: Cryptochromes (CRYs) are an ubiquitously occurring class of photoreceptors, which are important for regulating the circadian rhythm of animals via a time-delayed transcription-translation feedback loop (TTFL). Due to their protein architecture and common FAD chromophore, they belong to the same superfamily as photolyases (PHLs), an enzyme class that repairs UV-induced DNA lesions upon blue light absorption. Apart from their different functions the only prominent structural difference between CRY and PHL is the highly variable C-terminal extension (CTE) of the former. The nature of the CTE is still unclear and highly speculated. In this study, we show by hydrogen/deuterium exchange and subsequent mass-spectrometric analysis that the CTE of the animal-like cryptochrome from the green algae C

SUBMITTER: Franz-Badur S 

PROVIDER: S-EPMC6616342 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature