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http://purl.uniprot.org/citations/10413469http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10413469http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10413469http://www.w3.org/2000/01/rdf-schema#comment"Previously we showed that the yeast proteins Spt16 (Cdc68) and Pob3 are physically associated, and interact physically and genetically with the catalytic subunit of DNA polymerase alpha, Pol1 [Wittmeyer and Formosa (1997) Mol. Cell. Biol. 17, 4178-4190]. Here we show that purified Spt16 and Pob3 form a stable, abundant, elongated heterodimer and provide evidence that this is the functional form of these proteins. Genetic interactions between mutations in SPT16 and POB3 support the importance of the Spt16-Pob3 interaction in vivo. Spt16, Pob3, and Pol1 proteins were all found to localize to the nucleus in S. cerevisiae. A portion of the total cellular Spt16-Pob3 was found to be chromatin-associated, consistent with the proposed roles in modulating chromatin function. Some of the Spt16-Pob3 complex was found to copurify with the yeast DNA polymerase alpha/primase complex, further supporting a connection between Spt16-Pob3 and DNA replication."xsd:string
http://purl.uniprot.org/citations/10413469http://purl.org/dc/terms/identifier"doi:10.1021/bi982851d"xsd:string
http://purl.uniprot.org/citations/10413469http://purl.org/dc/terms/identifier"doi:10.1021/bi982851d"xsd:string
http://purl.uniprot.org/citations/10413469http://purl.uniprot.org/core/author"Joss L."xsd:string
http://purl.uniprot.org/citations/10413469http://purl.uniprot.org/core/author"Joss L."xsd:string
http://purl.uniprot.org/citations/10413469http://purl.uniprot.org/core/author"Wittmeyer J."xsd:string
http://purl.uniprot.org/citations/10413469http://purl.uniprot.org/core/author"Wittmeyer J."xsd:string
http://purl.uniprot.org/citations/10413469http://purl.uniprot.org/core/author"Formosa T."xsd:string
http://purl.uniprot.org/citations/10413469http://purl.uniprot.org/core/author"Formosa T."xsd:string
http://purl.uniprot.org/citations/10413469http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10413469http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10413469http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/10413469http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/10413469http://purl.uniprot.org/core/pages"8961-8971"xsd:string
http://purl.uniprot.org/citations/10413469http://purl.uniprot.org/core/pages"8961-8971"xsd:string
http://purl.uniprot.org/citations/10413469http://purl.uniprot.org/core/title"Spt16 and Pob3 of Saccharomyces cerevisiae form an essential, abundant heterodimer that is nuclear, chromatin-associated, and copurifies with DNA polymerase alpha."xsd:string
http://purl.uniprot.org/citations/10413469http://purl.uniprot.org/core/title"Spt16 and Pob3 of Saccharomyces cerevisiae form an essential, abundant heterodimer that is nuclear, chromatin-associated, and copurifies with DNA polymerase alpha."xsd:string
http://purl.uniprot.org/citations/10413469http://purl.uniprot.org/core/volume"38"xsd:string
http://purl.uniprot.org/citations/10413469http://purl.uniprot.org/core/volume"38"xsd:string
http://purl.uniprot.org/citations/10413469http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10413469
http://purl.uniprot.org/citations/10413469http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10413469
http://purl.uniprot.org/citations/10413469http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10413469
http://purl.uniprot.org/citations/10413469http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10413469