The 19S regulatory complex of the proteasome functions independently of proteolysis in nucleotide excision repair.
Mol Cell
; 3(6): 687-95, 1999 Jun.
Article
em En
| MEDLINE
| ID: mdl-10394357
ABSTRACT
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.
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Coleções:
01-internacional
Temas:
Geral
Base de dados:
MEDLINE
Assunto principal:
Peptídeo Hidrolases
/
Saccharomyces cerevisiae
/
Proteínas Fúngicas
/
Proteínas de Saccharomyces cerevisiae
/
Complexo de Endopeptidases do Proteassoma
/
Reparo do DNA
Idioma:
En
Revista:
Mol Cell
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
1999
Tipo de documento:
Article
País de afiliação:
Estados Unidos