RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/9635193http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9635193http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9635193http://www.w3.org/2000/01/rdf-schema#comment"Telomeres are functionally distinct from ends generated by chromosome breakage, in that telomeres, unlike double-strand breaks, are insulated from recombination with other chromosomal termini [1]. We report that the Ku heterodimer and the Rad50/Mre11/Xrs2 complex, both of which are required for repair of double-strand breaks [2-5], have separate roles in normal telomere maintenance in yeast. Using epistasis analysis, we show that the Ku end-binding complex defined a third telomere-associated activity, required in parallel with telomerase [6] and Cdc13, a protein binding the single-strand portion of telomere DNA [7,8]. Furthermore, loss of Ku function altered the expression of telomere-located genes, indicative of a disruption of telomeric chromatin. These data suggest that the Ku complex and the Cdc13 protein function as terminus-binding factors, contributing distinct roles in chromosome end protection. In contrast, MRE11 and RAD50 were required for the telomerase-mediated pathway, rather than for telomeric end protection; we propose that this complex functions to prepare DNA ends for telomerase to replicate. These results suggest that as a part of normal telomere maintenance, telomeres are identified as double-strand breaks, with additional mechanisms required to prevent telomere recombination. Ku, Cdc13 and telomerase define three epistasis groups required in parallel for telomere maintenance."xsd:string
http://purl.uniprot.org/citations/9635193http://purl.org/dc/terms/identifier"doi:10.1016/s0960-9822(98)70253-2"xsd:string
http://purl.uniprot.org/citations/9635193http://purl.org/dc/terms/identifier"doi:10.1016/s0960-9822(98)70253-2"xsd:string
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/author"Lundblad V."xsd:string
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/author"Lundblad V."xsd:string
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/author"Evans S.K."xsd:string
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/author"Evans S.K."xsd:string
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/author"Salinger A.P."xsd:string
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/author"Salinger A.P."xsd:string
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/author"Haber J.E."xsd:string
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/author"Haber J.E."xsd:string
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/author"Nugent C.I."xsd:string
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/author"Nugent C.I."xsd:string
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/author"Bosco G."xsd:string
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/author"Bosco G."xsd:string
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/author"Moore J.K."xsd:string
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/author"Moore J.K."xsd:string
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/author"Ross L.O."xsd:string
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/author"Ross L.O."xsd:string
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/name"Curr. Biol."xsd:string
http://purl.uniprot.org/citations/9635193http://purl.uniprot.org/core/name"Curr. Biol."xsd:string