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Characterization of two members of the cryptochrome/photolyase family from Ostreococcus tauri provides insights into the origin and evolution of cryptochromes
Author(s) -
HEIJDE MARC,
ZABULON GÉRALD,
CORELLOU FLORENCE,
ISHIKAWA TOMOKO,
BRAZARD JOHANNA,
USMAN ANWAR,
SANCHEZ FRÉDÉRIC,
PLAZA PASCAL,
MARTIN MONIQUE,
FALCIATORE ANGELA,
TODO TAKESHI,
BOUGET FRANÇOISYVES,
BOWLER CHRIS
Publication year - 2010
Publication title -
plant, cell and environment
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.646
H-Index - 200
eISSN - 1365-3040
pISSN - 0140-7791
DOI - 10.1111/j.1365-3040.2010.02168.x
Subject(s) - cryptochrome , photolyase , biology , circadian clock , genetics , gene family , protein family , gene , dna repair , botany , gene expression
Cryptochromes (Crys) are blue light receptors believed to have evolved from the DNA photolyase protein family, implying that light control and light protection share a common ancient origin. In this paper, we report the identification of five genes of the Cry/photolyase family (CPF) in two green algae of the Ostreococcus genus. Phylogenetic analyses were used to confidently assign three of these sequences to cyclobutane pyrimidine dimer (CPD) photolyases, one of them to a DASH‐type Cry, and a third CPF gene has high homology with the recently described diatom CPF1 that displays a bifunctional activity. Both purified OtCPF1 and OtCPF2 proteins show non‐covalent binding to flavin adenine dinucleotide (FAD), and additionally to 5,10‐methenyl‐tetrahydrofolate (MTHF) for OtCPF2. Expression analyses revealed that all five CPF members of Ostreococcus tauri are regulated by light. Furthermore, we show that OtCPF1 and OtCPF2 display photolyase activity and that OtCPF1 is able to interact with the CLOCK:BMAL heterodimer, transcription factors regulating circadian clock function in other organisms. Finally, we provide evidence for the involvement of OtCPF1 in the maintenance of the Ostreococcus circadian clock. This work improves our understanding of the evolutionary transition between photolyases and Crys.