Bish RA and Myers MP (2007) Werner helicase-interacting protein 1 binds polyubiquitin via its zinc finger domain. J Biol Chem 282(32):23184-93
Abstract: DNA repair is regulated on many levels by ubiquitination. In order to identify novel connections between DNA repair pathways and ubiquitin signaling, we used mass spectrometry to identify proteins which interact with lysine 6-linked polyubiquitin chains. From this proteomic screen, we identified the DNA repair protein Werner helicase interacting protein 1 (WRNIP1), along with nucleosome assembly protein 1 (NAP1), as novel ubiquitin-interacting proteins. We found that a small zinc finger domain at WRNIP1's N terminus is sufficient and necessary for non-covalent ubiquitin binding. This ubiquitin-binding zinc finger (UBZ) domain binds polyubiquitin, but not monoubiquitin, and appears to show no specificity for polyubiquitin chain linkage. A homologous zinc finger domain in RAD18 also binds polyubiquitin, suggesting a wider role for the UBZ domain in DNA repair. WRNIP1's ubiquitin-binding function, along with its previously established ATPase activity, suggests that WRNIP1 plays a role in the metabolism of ubiquitinated proteins. Supporting this model, deletion of MGS1, the yeast homolog of WRNIP1, slows the rate of ubiquitin turnover, rendering yeast resistant to cycloheximide. We also find that WRNIP1 is heavily modified with ubiquitin and SUMO, revealing complex layers in the involvement of ubiquitin pathway proteins in the regulation of DNA repair. WRNIP1's novel ubiquitin-binding ability sheds light on the role of UBZ domain-containing proteins in post-replication DNA repair.
|Status: Published||Type: Journal Article||PubMed ID: 17550899|
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