Current Genetics

, Volume 42, Issue 1, pp 9–20 | Cite as

Proteolysis of a nucleotide excision repair protein by the 26S proteasome

  • Lori Lommel
  • Tatiana Ortolan
  • Li Chen
  • Kiran Madura
  • Kevin S. Sweder
Research Article


The 26S proteasome degrades a broad spectrum of proteins and interacts with several nucleotide excision repair (NER) proteins, including the complex of Rad4 and Rad23 that binds preferentially to UV-damaged DNA. The rate of NER is increased in yeast strains with mutations in genes encoding subunits of the 26S proteasome, indicating that it could negatively regulate a repair process. The specific function of the 26S proteasome in DNA repair is unclear. It might degrade DNA repair proteins after repair is completed or act as a molecular chaperone to promote the assembly or disassembly of the repair complex. In this study, we show that Rad4 is ubiquitylated and that Rad23 can control this process. We also find that ubiquitylated Rad4 is degraded by the 26S proteasome. However, the interaction of Rad23 with Rad4 is not only to control degradation of Rad4, but also to assist in assembling the NER incision complex at UV-induced cyclobutane pyrimidine dimers. We speculate that, following the completion of DNA repair, specific repair proteins might be degraded by the proteasome to regulate repair.


Regulation Repair Ubiquitylation Degradation 


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Copyright information

© Springer-Verlag 2002

Authors and Affiliations

  • Lori Lommel
    • 1
  • Tatiana Ortolan
    • 2
  • Li Chen
    • 2
  • Kiran Madura
    • 2
  • Kevin S. Sweder
    • 1
  1. 1.Susan Lehman Cullman Laboratory for Cancer Research, Department of Chemical Biology, Ernest Mario School of Pharmacy, RutgersThe State University of New JerseyPiscatawayUSA
  2. 2.Department of Biochemistry, Robert Wood Johnson Medical SchoolUniversity of Medicine and Dentistry of New JerseyPiscatawayUSA

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