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http://purl.uniprot.org/citations/15805471http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15805471http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15805471http://www.w3.org/2000/01/rdf-schema#comment"The human UV-damaged DNA-binding protein Ddb1 associates with cullin 4 ubiquitin ligases implicated in nucleotide excision repair (NER). These complexes also contain the signalosome (CSN), but NER-relevant ubiquitination targets have not yet been identified. We report that fission yeast Ddb1, Cullin 4 (Pcu4), and CSN subunits Csn1 and Csn2 are required for degradation of the ribonucleotide reductase (RNR) inhibitor protein Spd1. Ddb1-deficient cells have >20-fold increased spontaneous mutation rate. This is partly dependent on the error-prone translesion DNA polymerases. Spd1 deletion substantially reduced the mutation rate, suggesting that insufficient RNR activity accounts for approximately 50% of observed mutations. Epistasis analysis indicated that Ddb1 contributed to mutation avoidance and tolerance to DNA damage in a pathway distinct from NER. Finally, we show that Ddb1/Csn1/Cullin 4-mediated Spd1 degradation becomes essential when cells differentiate into meiosis. These results suggest that Ddb1, along with Cullin 4 and the signalosome, constitute a major pathway controlling genome stability, repair, and differentiation via RNR regulation."xsd:string
http://purl.uniprot.org/citations/15805471http://purl.org/dc/terms/identifier"doi:10.1101/gad.329905"xsd:string
http://purl.uniprot.org/citations/15805471http://purl.org/dc/terms/identifier"doi:10.1101/gad.329905"xsd:string
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/author"Liu C."xsd:string
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/author"Liu C."xsd:string
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/author"Nielsen O."xsd:string
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/author"Nielsen O."xsd:string
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/author"Fleck O."xsd:string
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/author"Fleck O."xsd:string
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/author"Carr A.M."xsd:string
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/author"Carr A.M."xsd:string
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/author"Holmberg C."xsd:string
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/author"Holmberg C."xsd:string
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/author"Hansen H.A."xsd:string
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/author"Hansen H.A."xsd:string
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/author"Slaaby R."xsd:string
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/author"Slaaby R."xsd:string
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/pages"853-862"xsd:string
http://purl.uniprot.org/citations/15805471http://purl.uniprot.org/core/pages"853-862"xsd:string