Cloning of a marsupial DNA photolyase gene and the lack of related nucleotide sequences in placental mammals

Photoreactivating enzyme, DNA photolyase, reduces lethal, mutagenic and carcinogenic effects of ultraviolet light (UV) by catalyzing near UV or visible light-dependent repair of cyclobutane pyrimidine dimers (CPDs) in DNA. The enzyme activity has been detected in a wide variety of organisms ranging from bacteria to nonplacental mammals. However, the evidence for photoreactivation in placental mammals, including humans, is controversial. As a first step to identify the presence and activity of the gene in mammalian species, we isolated a cDNA clone of this gene from a marsupial, the South American opossum Monodelphis domestica. Photolyase activity was expressed in Escherichia coli from the cDNA which is predicted to encode a polypeptide of 470 amino acid residues. The deduced amino acid sequence of this protein is strikingly similar to those of photolyases from two metazoans; the opossum photolyase shares 59% and 63% sequence identity with the Drosophila melanogaster and goldfish Carassius auratus enzymes, respectively. However, no closely related nucleotide sequence was detected in higher mammals and a homologous transcript was undetectable in a number of human tissues. These results strongly suggest that humans, as well as other placental mammals, lack the photolyase gene.