Characterization of two members of the cryptochrome/photolyase family from Ostreococcus tauri provides insights into the origin and evolution of cryptochromes

• DOI: 10.1111/j.1365-3040.2010.02168.x
• Publication Date: 2010-04-29T06:54:04Z
• Authors: MARC HEIJDE; GÉRALD ZABULON; FLORENCE CORELLOU; TOMOKO ISHIKAWA; JOHANNA BRAZARD; ANWAR USMAN; FRÉDÉRIC SANCHEZ; PASCAL PLAZA; MONIQUE MARTIN; ANGELA FALCIATORE; TAKESHI TODO; FRANÇOIS‐YVES BOUGET; CHRIS BOWLER
• Keywords: Photolyase; Protein family

Cryptochromes (Crys) are blue light receptors believed to have evolved from the DNA photolyase protein family, implying that control and protection share a common ancient origin. In this paper, we report identification of five genes Cry/photolyase family (CPF) in two green algae Ostreococcus genus. Phylogenetic analyses were used confidently assign three these sequences cyclobutane pyrimidine dimer (CPD) photolyases, one them DASH-type Cry, third CPF gene has high homology with recently described diatom CPF1 displays bifunctional activity. Both purified OtCPF1 OtCPF2 proteins show non-covalent binding flavin adenine dinucleotide (FAD), additionally 5,10-methenyl-tetrahydrofolate (MTHF) for OtCPF2. Expression revealed all members tauri regulated by light. Furthermore, display activity is able interact CLOCK:BMAL heterodimer, transcription factors regulating circadian clock function other organisms. Finally, provide evidence involvement maintenance clock. This work improves our understanding evolutionary transition between photolyases Crys.