Nucleic Acids Research, Vol 25, Issue 4 764-768, Copyright © 1997 by Oxford University Press
T Todo, ST Kim, K Hitomi, E Otoshi, T Inui, H Morioka, H Kobayashi, E Ohtsuka, H Toh and M Ikenaga
Two types of enzyme utilizing light from the blue and near-UV spectral
range (320-520 nm) are known to have related primary structures: DNA
photolyase, which repairs UV-induced DNA damage in a light-dependent
manner, and the blue light photoreceptor of plants, which mediates
light-dependent regulation of seedling development. Cyclobutane pyrimidine
dimers (CPDs) and pyrimidine (6-4) pyrimidone photoproducts
[(6-4)photoproducts] are the two major photoproducts produced in DNA by UV
irradiation. Two types of photolyases have been identified, one specific
for CPDs (CPD photolyase) and another specific for (6- 4)photoproducts
[(6-4)photolyase]. (6-4)Photolyase activity was first found in Drosophila
melanogaster and to date this gene has been cloned only from this organism.
The deduced amino acid sequence of the cloned gene shows that
(6-4)photolyase is a member of the CPD photolyase/blue light photoreceptor
family. Both CPD photolyase and blue light photoreceptor are flavoproteins
and bound flavin adenine dinucleotides (FADs) are essential for their
catalytic activity. Here we report isolation of a Xenopus
laevis(6-4)photolyase gene and show that the (6- 4)photolyase binds non-
covalently to stoichiometric amounts of FAD. This is the first indication
of FAD as the chromophore of (6- 4)photolyase.
ARTICLES
Flavin adenine dinucleotide as a chromophore of the Xenopus (6- 4)photolyase
Radiation Biology Center, Kyoto University, Japan.
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