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THE PLANT CELL, Vol 9, Issue 2 199-207, Copyright © 1997 by American Society of Plant Biologists
An Enzyme Similar to Animal Type II Photolyases Mediates Photoreactivation in Arabidopsis
M. Ahmad, J. A. Jarillo, L. J. Klimczak, L. G. Landry, T. Peng, R. L. Last and A. R. Cashmore
Plant Science Institute, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6018
The important issue of photoreactivation DNA repair in plants has become
even more interesting in recent years because a family of genes that are
highly homologous to photoreactivating DNA repair enzymes but that function
as blue light photoreceptors has been isolated. Here, we report the
isolation of a novel photolyase-like sequence from Arabidopsis designated
PHR1 (for photoreactivating enzyme). It shares little sequence similarity
with either type I photolyases or the cryptochrome family of blue light
photoreceptors. Instead, the PHR1 gene encodes an amino acid sequence with
significant homology to the recently characterized type II photolyases
identified in a number of prokaryotic and animal systems. PHR1 is a
single-copy gene and is not expressed in dark-grown etiolated seedlings:
the message is light inducible, which is similar to the expression profile
for photoreactivation activity in plants. The PHR1 protein complements a
photolyase-deficient mutant of Escherichia coli and thus confers
photoreactivation activity. In addition, an Arabidopsis mutant that is
entirely lacking in photolyase activity has been found to contain a lesion
within this Arabidopsis type II photolyase sequence. We conclude that PHR1
represents a genuine plant photolyase gene and that the plant genes with
homology to type I photolyases (the cryptochrome family of blue light
photoreceptors) do not contribute to photoreactivation repair, at least in
the case of Arabidopsis.
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