Cloning, functional characterization, and near-ultraviolet radiation-enhanced expression of a photolyase gene (PHR1) from the phytopathogenic fungus Bipolaris oryzae.
Photolyase is a DNA repair enzyme that can absorb blue/ultraviolet A light as energy and split a pyrimidine dimer induced by ultraviolet radiation. We isolated and characterized PHR1, a gene encoding photolyase, from the phytopathogenic fungus Bipolaris oryzae. Sequence analysis showed that PHR1 encodes a putative protein that has 634 amino acids, a molecular mass of 72.6 kDa, and 51.3-55.5% sequence identity to other fungal photolyases. Complementation of the photoreactivation-deficient Escherichia coli mutant by PHR1 cDNA demonstrated that the PHR1 gene from B. oryzae encodes a functional photolyase. Real-time PCR analysis showed that the PHR1 transcripts were specifically enhanced by near-ultraviolet radiation (300-400 nm) and by sunlight.
Kihara
Junichi
J
Faculty of Life and Environmental Science, Shimane University, Matsue, Shimane, 690-8504, Japan.
Moriwaki
Akihiro
A
Matsuo
Nobuhito
N
Arase
Sakae
S
Honda
Yuichi
Y
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D004255:Deoxyribodipyrimidine Photo-Lyase / Q000235:genetics* / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics; D005656:Fungal Proteins / Q000235:genetics; D015966:Gene Expression Regulation, Fungal; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010802:Phylogeny; D016133:Polymerase Chain Reaction; D017386:Sequence Homology, Amino Acid; D014466:Ultraviolet Rays; D015854:Up-Regulation
D005656:Fungal Proteins; C437712:UVI-1 protein, Bipolaris oryzae; D004255:Deoxyribodipyrimidine Photo-Lyase