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http://purl.uniprot.org/citations/8621497http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8621497http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8621497http://www.w3.org/2000/01/rdf-schema#comment"The B subunit of the DNA polymerase (pol) alpha-primase complex executes an essential role at the initial stage of DNA replication in Saccharomyces cerevisiae and is phosphorylated in a cell cycle-dependent manner. In this report, we show that the four subunits of the yeast DNA polymerase alpha-primase complex are assembled throughout the cell cycle, and physical association between newly synthesized pol alpha (p180) and unphosphorylated B subunit (p86) occurs very rapidly. Therefore, B subunit phosphorylation does not appear to modulate p180.p86 interaction. Conversely, by depletion experiments and by using a yeast mutant strain, which produces a low and constitutive level of the p180 polypeptide, we found that formation of the p180.p86 subcomplex is required for B subunit phosphorylation."xsd:string
http://purl.uniprot.org/citations/8621497http://purl.org/dc/terms/identifier"doi:10.1074/jbc.271.15.8661"xsd:string
http://purl.uniprot.org/citations/8621497http://purl.org/dc/terms/identifier"doi:10.1074/jbc.271.15.8661"xsd:string
http://purl.uniprot.org/citations/8621497http://purl.uniprot.org/core/author"Ferrari M."xsd:string
http://purl.uniprot.org/citations/8621497http://purl.uniprot.org/core/author"Ferrari M."xsd:string
http://purl.uniprot.org/citations/8621497http://purl.uniprot.org/core/author"Lucchini G."xsd:string
http://purl.uniprot.org/citations/8621497http://purl.uniprot.org/core/author"Lucchini G."xsd:string
http://purl.uniprot.org/citations/8621497http://purl.uniprot.org/core/author"Plevani P."xsd:string
http://purl.uniprot.org/citations/8621497http://purl.uniprot.org/core/author"Plevani P."xsd:string
http://purl.uniprot.org/citations/8621497http://purl.uniprot.org/core/author"Foiani M."xsd:string
http://purl.uniprot.org/citations/8621497http://purl.uniprot.org/core/author"Foiani M."xsd:string
http://purl.uniprot.org/citations/8621497http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8621497http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8621497http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8621497http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/8621497http://purl.uniprot.org/core/pages"8661-8666"xsd:string
http://purl.uniprot.org/citations/8621497http://purl.uniprot.org/core/pages"8661-8666"xsd:string
http://purl.uniprot.org/citations/8621497http://purl.uniprot.org/core/title"Phosphorylation of the DNA polymerase alpha-primase B subunit is dependent on its association with the p180 polypeptide."xsd:string
http://purl.uniprot.org/citations/8621497http://purl.uniprot.org/core/title"Phosphorylation of the DNA polymerase alpha-primase B subunit is dependent on its association with the p180 polypeptide."xsd:string
http://purl.uniprot.org/citations/8621497http://purl.uniprot.org/core/volume"271"xsd:string
http://purl.uniprot.org/citations/8621497http://purl.uniprot.org/core/volume"271"xsd:string
http://purl.uniprot.org/citations/8621497http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8621497
http://purl.uniprot.org/citations/8621497http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8621497