Rad23 links DNA repair to the ubiquitin/proteasome pathway
作者： Cherylene Schauber , Li Chen , Prasad Tongaonkar , Irving Vega , David Lambertson
DOI: 10.1038/35661
关键词:
摘要: Rad23 is an evolutionarily conserved protein that important for nucleotide excision repair1,2,3. A regulatory role has been proposed because rad23 mutants are sensitive to ultraviolet light but still capable of incising damaged DNA4,5. Here we show interacts with the 26S proteasome through amino-terminal ubiquitin-like domain (UbLR23). The carboxy terminus binds Rad4 DNA repair and creates a link between pathways. sensitivity caused by deletion UbLR23 may therefore arise from its inability interact proteasome. fusion proteins glutathione S-transferase (GST)–Rad23 Rad4–haemagglutinin (HA), subunits Cim3 Cim5, cofractionate consecutive chromatography steps. human (UbLHRB) also These results demonstrate domains (UbLs) represent new class proteasome-interacting motifs.
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