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http://purl.uniprot.org/citations/14766746http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14766746http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14766746http://www.w3.org/2000/01/rdf-schema#comment"Models of DNA replication in yeast and Xenopus suggest that Mcm10p is required to generate the pre-initiation complex as well as progression of the replication fork during the elongation of DNA chains. In this report, we show that the Schizosaccharomyces pombe Mcm10p/Cdc23p binds to the S. pombe DNA polymerase (pol) alpha-primase complex in vitro by interacting specifically with the catalytic p180 subunit and stimulates DNA synthesis catalyzed by the pol alpha-primase complex with various primed DNA templates. We investigated the mechanism by which Mcm10p activates the polymerase activity of the pol alpha-primase complex by generating truncated derivatives of the full-length 593-amino acid Mcm10p. Their ability to stimulate pol alpha polymerase activity and bind to single-stranded DNA and to pol alpha were compared. Concomitant with increased deletion of the N-terminal region (from amino acids 95 to 415), Mcm10p derivatives lost their ability to stimulate pol alpha polymerase activity and bind to single-stranded DNA. Truncated derivatives of Mcm10p containing amino acids 1-416 retained the pol alpha binding activity, whereas the C terminus, amino acids 496-593, did not. These results demonstrate that both the single-stranded DNA binding and the pol alpha binding properties of Mcm10p play important roles in the activation. In accord with these findings, Mcm10p facilitated the binding of pol alpha-primase complex to primed DNA and formed a stable complex with pol alpha-primase on primed templates. A mutant that failed to activate or bind to DNA and pol alpha, was not observed in this complex. We suggest that the interaction of Mcm10p with the pol alpha-primase complex, its binding to single-stranded DNA, and its activation of the polymerase complex together contribute to its role in the elongation phase of DNA replication."xsd:string
http://purl.uniprot.org/citations/14766746http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m400142200"xsd:string
http://purl.uniprot.org/citations/14766746http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m400142200"xsd:string
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/author"Hurwitz J."xsd:string
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/author"Hurwitz J."xsd:string
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/author"Lee J.-K."xsd:string
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/author"Lee J.-K."xsd:string
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/author"Raychaudhuri S."xsd:string
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/author"Raychaudhuri S."xsd:string
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/author"Cho Y.-S."xsd:string
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/author"Cho Y.-S."xsd:string
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/author"Fien K."xsd:string
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/author"Fien K."xsd:string
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/author"Tappin I."xsd:string
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/author"Tappin I."xsd:string
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/pages"16144-16153"xsd:string
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/pages"16144-16153"xsd:string
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/title"Primer utilization by DNA polymerase alpha-primase is influenced by its interaction with Mcm10p."xsd:string
http://purl.uniprot.org/citations/14766746http://purl.uniprot.org/core/title"Primer utilization by DNA polymerase alpha-primase is influenced by its interaction with Mcm10p."xsd:string
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