期刊
PHOTOCHEMISTRY AND PHOTOBIOLOGY
卷 91, 期 6, 页码 1356-1367出版社
WILEY
DOI: 10.1111/php.12501
关键词
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资金
- Deutsche Forschungsgemeinschaft [SFB 987]
- Spanish Government (Ministerio de Ciencia y Tecnologia) [BIO2006-01323, BIO2009-11131]
- Andalusian Government [P07-CVI-02813]
- European Union (European Regional Development Fund [ERDF])
- Spanish Ministerio de Educacion, Cultura y Deporte
Proteins from the cryptochrome/photolyase family utilize UV-A, blue or even red light to achieve such diverse functions as repair of DNA lesions by photolyases and signaling by cryptochromes. DASH-type cryptochromes retained the ability to repair cyclobutane pyrimidine dimers (CPDs) in single-stranded DNA regions invitro. However, most organisms possess conventional CPD photolyases responsible for repair of these lesions invivo. Recent work showed that the DASH-type cryptochrome CryD plays a regulatory role in diverse light-dependent processes in Fusarium fujikuroi. Here, we report our invitro studies on heterologously expressed FfCryD. The purified protein contains N-5,N-10-methenyltetrahydrofolate and flavin adenine dinucleotide as cofactors. Photoreduction and DNA photorepair experiments confirmed that FfCryD is active in light-driven electron transfer processes. However, the protein showed comparable affinities for CPD-comprising and undamaged DNA probes. Surprisingly, after purification, full-length FfCryD as well as a truncated version containing only the PHR domain bound RNA which influenced their behavior invitro. Moreover, binding of FfCryD to RNA indicates a putative role in RNAmetabolism or in posttranscriptional control of gene expression.
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