Affiliation:
1. Department of Biochemistry and Biophysics, School of Medicine, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-7260
Abstract
ABSTRACT
The
Saccharomyces cerevisiae
DNA repair gene
PHR1
encodes a photolyase that catalyzes the light-dependent repair of pyrimidine dimers.
PHR1
expression is induced at the level of transcription by a variety of DNA-damaging agents. The primary regulator of the
PHR1
damage response is a 39-bp sequence called URS
PHR1
which is the binding site for a protein(s) that constitutes the damage-responsive repressor PRP. In this communication, we report the identification of two proteins, Rph1p and Gis1p, that regulate
PHR1
expression through URS
PHR1
. Both proteins contain two putative zinc fingers that are identical throughout the DNA binding region, and deletion of both
RPH1
and
GIS1
is required to fully derepress
PHR1
in the absence of damage. Derepression of
PHR1
increases the rate and extent of photoreactivation in vivo, demonstrating that the damage response of
PHR1
enhances cellular repair capacity. In vitro footprinting and binding competition studies indicate that the sequence AG
4
(C
4
T) within URS
PHR1
is the binding site for Rph1p and Gis1p and suggests that at least one additional DNA binding component is present in the PRP complex.
Publisher
American Society for Microbiology
Subject
Cell Biology,Molecular Biology
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