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A Putative Blue‐Light Receptor From Drosophila melanogaster
Author(s) -
Okano Satoshi,
Kanno Shinichiro,
Takao Masashi,
Eker Andre P. M.,
Lsono Kunio,
Tsukahara Yasuo,
Yasui Akira
Publication year - 1999
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1999.tb05314.x
Subject(s) - photolyase , pyrimidine dimer , biology , drosophila melanogaster , dna repair , escherichia coli , gene , cryptochrome , dna , microbiology and biotechnology , genetics , recombinant dna , biochemistry , circadian clock
Abstract— A gene encoding a 62.5 kDa homolog of Drosophila melanogaster photolyase was isolated. Purified recombinant protein contained a flavin adenine dinucleotide chromophore. The recombinant protein did not show photolyase activity for either cyclobutane pyrimidine dimers or 6–4 photoproducts in vitro as well as in vivo in Escherichia coli host cells, suggesting that the protein is not a DNA repair enzyme but a blue‐light photoreceptor. Reverse transcription polymerase chain reaction analysis showed that the gene is more expressed in head than in body and that it is more expressed in antennae than in legs, wings and mouth appendages. In a phylogenetic tree of the photolyase family, the Drosophila photolyase homolog is located in a cluster containing 6–4 photolyases and mammalian photolyase homologs, which is only distantly related to the clade of higher plant blue‐light photoreceptors. The mammalian photolyase homologs are more closely related to Drosophila 6–4 photolyase than to the Drosophila photolyase homolog, suggesting different roles of the photolyase homologs.