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Molecular and Cellular Biology, November 1999, p. 7630-7638, Vol. 19, No. 11
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
RPH1 and GIS1 Are
Damage-Responsive Repressors of PHR1
Yeun Kyu
Jang,
Ling
Wang, and
Gwendolyn B.
Sancar*
Department of Biochemistry and Biophysics,
School of Medicine, The University of North Carolina at Chapel Hill,
Chapel Hill, North Carolina 27599-7260
Received 2 June 1999/Returned for modification 20 July
1999/Accepted 9 August 1999
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
URSPHR1 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
URSPHR1. 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 AG4
(C4T) within URSPHR1 is the binding
site for Rph1p and Gis1p and suggests that at least one additional DNA
binding component is present in the PRP complex.
*
Corresponding author. Mailing address: Department of
Biochemistry and Biophysics, CB# 7260, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7260. Phone: (919) 966-2077. Fax:
(919) 966-2852. E-mail: GwendolynSancar{at}med.unc.edu.

Present address: Department of Molecular Biology, College of
Natural Science, Seoul National University, Seoul 151-742, South
Korea.
Molecular and Cellular Biology, November 1999, p. 7630-7638, Vol. 19, No. 11
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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