ArticleNucleic acids research2000
The 26S proteasome negatively regulates the level of overall genomic nucleotide excision repair.
Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- DNA damage-induced proteasome phosphorylation controls substrate recognition and facilitates DNA repair.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Hof1 plays a checkpoint-related role in MMS-induced DNA damage response inMolecular biology of the cell · 2020Article
- CD44 promotes multi-drug resistance by protecting P-glycoprotein from FBXO21-mediated ubiquitination.Oncotarget · 2015Article
- The ubiquitin-proteasome system in cancer, a major player in DNA repair. Part 1: post-translational regulation.Journal of cellular and molecular medicine · 2009Review
- Other proteins interacting with XP proteins.Advances in experimental medicine and biology · 2008Review
- Article
- Roles of Rad23 protein in yeast nucleotide excision repair.Nucleic acids research · 2004Article
- Degradation of retinoid X receptor alpha by TPA through proteasome pathway in gastric cancer cells.World journal of gastroenterology · 2003Article
- A novel regulation mechanism of DNA repair by damage-induced and RAD23-dependent stabilization of xeroderma pigmentosum group C protein.Genes & development · 2003Article
- Proteolysis of a nucleotide excision repair protein by the 26 S proteasome.Current genetics · 2002Article
- PA200, a nuclear proteasome activator involved in DNA repair.The EMBO journal · 2002Article
- Regulation of repair by the 26S proteasome.Journal of biomedicine & biotechnology · 2002Article
- The 19S complex of the proteasome regulates nucleotide excision repair in yeast.Genes & development · 2001Article
- Rad7 E3 Ubiquitin Ligase Attenuates Polyubiquitylation of Rpn10 and Dsk2 Following DNA Damage inAdvances in biological chemistryArticle
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Regulation of protein expression can be achieved through destruction of proteins by the 26S: proteasome. Cellular processes that are regulated by proteolysis include cell cycle progression, stress responses and differentiation. Several nucleotide excision repair proteins in yeast and humans, such as Rad23, Rad4 and XPB, have been shown to co-purify with Cim3 and Cim5, AAA ATPases of the 19S: proteasome regulatory subunit. However, it has not been determined if nucleotide excision repair is regulated through protein destruction. We measured nucleotide excision repair in yeast mutants that are defective in proteasome function and found that the repair of the transcribed and non-transcribed strands of an RNA polymerase II-transcribed reporter gene was increased in the absence of proteasome function. Additionally, overexpression of the Rad4 repair protein, which is bound to the repair/proteolytic factor Rad23, conferred higher rates of nucleotide excision repair. Based on our data we suggest that a protein (or proteins) involved in nucleotide excision repair or in regulation of repair is degraded by the 26S proteasome. We propose that decreased proteasome function enables increased DNA repair, due to the transient accumulation of a specific repair factor, perhaps Rad4.
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