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Regulation of DNA repair can be achieved through ubiquitin-mediated degradation of transiently induced proteins. In  Saccharomyces cerevisiae , Rad4 is involved in damage recognition during nucleotide excision repair (NER) and, in conjunction with Rad23, recruits other proteins to the site of damage. We identified a synthetic interaction upon UV exposure between Rad4 and Cdc20, a protein that modulates the activity of the anaphase promoting complex (APC/C), a multisubunit E3 ubiquitin ligase complex. The moderately UV sensitive Δ rad4  strain became highly sensitive when  cdc20-1  was present, and was rescued by overexpression of  CDC20 . The double mutant is also deficient in elicting  RNR3-lacZ  transcription upon exposure to UV irradiation or 4-NQO compared with the Δ rad4  single mutant. We demonstrate that the Δ rad4 / cdc20-1  double mutant is defective in double strand break repair by way of a plasmid end-joining assay, indicating that Rad4 acts to ensure that damaged DNA is repaired via a Cdc20-mediated mechanism. This study is the first to present evidence that Cdc20 may play a role in the degradation of proteins involved in nucleotide excision repair.

A Synthetic Interaction betweenCDC20andRAD4inSaccharomyces cerevisiaeupon UV Irradiation