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http://purl.uniprot.org/citations/8194531http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8194531http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8194531http://www.w3.org/2000/01/rdf-schema#comment"The protein RAP1 is essential for the maintenance of the telomeres of Saccharomyces cerevisiae and binds in vitro to multiple sites found within the TG1-3 telomeric repeats. We show here that, in addition to its known binding activity for double-stranded DNA, RAP1 binds sequence-specifically to the GT-strands. This indicates that RAP1 is the protein that binds to the telomeric terminal GT-tails. Furthermore, we have found that RAP1 binds to and promotes the formation of G-tetrads, i.e. DNA quadruplexes, in GT-strand oligonucleotides at nanomolar concentrations. The formation of DNA quadruplexes appears to involve the intermolecular association of GT-strands. The minimal DNA-binding domain of RAP1 (DBD) binds only to double-stranded DNA, so that the novel DNA-binding activity we have found involves regions of the protein located outside of the DBD. The finding that a telomeric protein promotes the formation of G-tetrads argues for the use of DNA quadruplexes in telomere association."xsd:string
http://purl.uniprot.org/citations/8194531http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1994.tb06526.x"xsd:string
http://purl.uniprot.org/citations/8194531http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1994.tb06526.x"xsd:string
http://purl.uniprot.org/citations/8194531http://purl.uniprot.org/core/author"Rhodes D."xsd:string
http://purl.uniprot.org/citations/8194531http://purl.uniprot.org/core/author"Rhodes D."xsd:string
http://purl.uniprot.org/citations/8194531http://purl.uniprot.org/core/author"Giraldo R."xsd:string
http://purl.uniprot.org/citations/8194531http://purl.uniprot.org/core/author"Giraldo R."xsd:string
http://purl.uniprot.org/citations/8194531http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8194531http://purl.uniprot.org/core/date"1994"xsd:gYear
http://purl.uniprot.org/citations/8194531http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/8194531http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/8194531http://purl.uniprot.org/core/pages"2411-2420"xsd:string
http://purl.uniprot.org/citations/8194531http://purl.uniprot.org/core/pages"2411-2420"xsd:string
http://purl.uniprot.org/citations/8194531http://purl.uniprot.org/core/title"The yeast telomere-binding protein RAP1 binds to and promotes the formation of DNA quadruplexes in telomeric DNA."xsd:string
http://purl.uniprot.org/citations/8194531http://purl.uniprot.org/core/title"The yeast telomere-binding protein RAP1 binds to and promotes the formation of DNA quadruplexes in telomeric DNA."xsd:string
http://purl.uniprot.org/citations/8194531http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/8194531http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/8194531http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8194531
http://purl.uniprot.org/citations/8194531http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8194531
http://purl.uniprot.org/citations/8194531http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8194531
http://purl.uniprot.org/citations/8194531http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/8194531
http://purl.uniprot.org/uniprot/P11938http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/8194531
http://purl.uniprot.org/uniprot/P11938#attribution-9CFE927E81521FFB1D8D0836CBD7A7E0http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/8194531