The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair

Steven Jon Russell, Simon H. Reed, Wenya Huang, Errol C. Friedberg, Stephen Albert Johnston

研究成果: Article同行評審

172 引文 斯高帕斯(Scopus)

摘要

The 26S proteasome degrades proteins targeted by the ubiquitin pathway, a function thought to explain its role in cellular processes. The proteasome interacts with the ubiquitin-like N terminus of Rad23, a nucleotide excision repair (NER) protein, in Saccharomyces cerevisiae. Deletion of the ubiquitin- like domain causes UV radiation sensitivity. Here, we show that the ubiquitin-like domain of Rad23 is required for optimal activity of an in vitro NER system. Inhibition of proteasomal ATPases diminishes NER activity in vitro and increases UV sensitivity in vivo. Surprisingly, blockage of protein degradation by the proteasome has no effect on the efficiency of NER. This establishes that the regulatory complex of the proteasome has a function independent of protein degradation.

原文English
頁(從 - 到)687-695
頁數9
期刊Molecular Cell
3
發行號6
DOIs
出版狀態Published - 1999 六月

All Science Journal Classification (ASJC) codes

  • 分子生物學
  • 細胞生物學

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