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Vol. 15, No. 12, pp. 1528-1539, June 15, 2001
1 Laboratory of Molecular Pathology, Department of
Pathology, 2 Department of Medicine and Biochemistry,
University of Texas Southwestern Medical Center,
Dallas, Texas 75390-9072, USA
Previous studies suggest that the amino-terminal ubiquitin-like
(ubl) domain of Rad23 protein can recruit the proteasome for a
stimulatory role during nucleotide excision repair in the yeast Saccharomyces cerevisiae. In this report, we show that the 19S regulatory complex of the yeast proteasome can affect nucleotide excision repair independently of Rad23 protein. Strains with mutations in 19S regulatory subunits (but not 20S subunits) of the proteasome promote partial recovery of nucleotide excision repair in vivo in
rad23 deletion mutants, but not in other nucleotide excision repair-defective strains tested. In addition, a strain that expresses a
temperature-degradable ATPase subunit of the 19S regulatory complex
manifests a dramatically increased rate of nucleotide excision repair
in vivo. These data indicate that the 19S regulatory complex of the 26S
proteasome can negatively regulate the rate of nucleotide excision
repair in yeast and suggest that Rad23 protein not only recruits the
19S regulatory complex, but also can mediate functional interactions
between the 19S regulatory complex and the nucleotide excision repair
machinery. The 19S regulatory complex of the yeast proteasome functions
in nucleotide excision repair independent of proteolysis.
[Key Words: Rad23 protein; DNA repair; Saccharomyces cerevisiae; proteasome]
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