Modulation of DNA Synthesis in Saccharomyces cerevisiae Nuclear Extract by DNA Polymerases and the Origin Recognition Complex
We have analyzed the modulation of DNA synthesis on a supercoiled plasmid DNA template by DNA polymerases (pol), minichromosome maintenance protein complex (Mcm), topoisomerases, and the origin recognition complex (ORC) using an in vitro assay system. Antisera specific against the four-subunit pol α...
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| Veröffentlicht in: | The Journal of biological chemistry 2005-02, Vol.280 (8), p.6285-6292 |
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| container_title | The Journal of biological chemistry |
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| creator | Mitkova, Atanaska V. Biswas-Fiss, Esther E. Biswas, Subhasis B. |
| description | We have analyzed the modulation of DNA synthesis on a supercoiled plasmid DNA template by DNA polymerases (pol), minichromosome maintenance protein complex (Mcm), topoisomerases, and the origin recognition complex (ORC) using an in vitro assay system. Antisera specific against the four-subunit pol α, the catalytic subunit of pol δ, and the Mcm467 complex each inhibited DNA synthesis. However, DNA synthesis in this system appeared to be independent of polϵ. Consequently, DNA synthesis in the in vitro system appeared to depend only on two polymerases, α and δ, as well as the Mcm467 DNA helicase. This system requires supercoiled plasmid DNA template and DNA synthesis absolutely required DNA topoisomerase I. In addition, we also report here a novel finding that purified recombinant six subunit ORC significantly stimulated the DNA synthesis on a supercoiled plasmid DNA template containing an autonomously replicating sequence, ARS1. |
| doi_str_mv | 10.1074/jbc.M410129200 |
| format | Article |
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Antisera specific against the four-subunit pol α, the catalytic subunit of pol δ, and the Mcm467 complex each inhibited DNA synthesis. However, DNA synthesis in this system appeared to be independent of polϵ. Consequently, DNA synthesis in the in vitro system appeared to depend only on two polymerases, α and δ, as well as the Mcm467 DNA helicase. This system requires supercoiled plasmid DNA template and DNA synthesis absolutely required DNA topoisomerase I. In addition, we also report here a novel finding that purified recombinant six subunit ORC significantly stimulated the DNA synthesis on a supercoiled plasmid DNA template containing an autonomously replicating sequence, ARS1.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M410129200</identifier><identifier>PMID: 15590683</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Cell-Free System ; DNA Polymerase I - physiology ; DNA Polymerase III - physiology ; DNA Replication ; DNA Topoisomerases - physiology ; DNA Topoisomerases, Type I - physiology ; DNA, Superhelical - biosynthesis ; DNA-Binding Proteins - physiology ; DNA-Directed DNA Polymerase - physiology ; Minichromosome Maintenance 1 Protein - physiology ; Origin Recognition Complex ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae Proteins - physiology ; Transcription Factors - physiology</subject><ispartof>The Journal of biological chemistry, 2005-02, Vol.280 (8), p.6285-6292</ispartof><rights>2005 © 2005 ASBMB. 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Antisera specific against the four-subunit pol α, the catalytic subunit of pol δ, and the Mcm467 complex each inhibited DNA synthesis. However, DNA synthesis in this system appeared to be independent of polϵ. Consequently, DNA synthesis in the in vitro system appeared to depend only on two polymerases, α and δ, as well as the Mcm467 DNA helicase. This system requires supercoiled plasmid DNA template and DNA synthesis absolutely required DNA topoisomerase I. In addition, we also report here a novel finding that purified recombinant six subunit ORC significantly stimulated the DNA synthesis on a supercoiled plasmid DNA template containing an autonomously replicating sequence, ARS1.</description><subject>Cell-Free System</subject><subject>DNA Polymerase I - physiology</subject><subject>DNA Polymerase III - physiology</subject><subject>DNA Replication</subject><subject>DNA Topoisomerases - physiology</subject><subject>DNA Topoisomerases, Type I - physiology</subject><subject>DNA, Superhelical - biosynthesis</subject><subject>DNA-Binding Proteins - physiology</subject><subject>DNA-Directed DNA Polymerase - physiology</subject><subject>Minichromosome Maintenance 1 Protein - physiology</subject><subject>Origin Recognition Complex</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae Proteins - physiology</subject><subject>Transcription Factors - physiology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1v1DAQxS0EotvClSOyOPSWre3YWedYLS1U6geiIHGznMlk4yqJFzspzaH_O253pZ4Qc5nL7715mkfIB86WnK3kyV0FyyvJGRelYOwVWXCm8yxX_NdrsmBM8KwUSh-QwxjvWBpZ8rfkgCtVskLnC_J45eups6PzA_UN_Xx9Sm_nYWwxukjdQG8tQGuD72fASAED3rvoLNLrCTq0gZ49jMHCSKv5WfzNd3OPwcZE26GmyYneBLdJVt8R_GZwz6fWvt92-PCOvGlsF_H9fh-Rn-dnP9Zfs8ubLxfr08sMpGRjhoUGpatypURZlEzKhmsJvALWyFJYxmUjrADJQJcWlAC0iIpJaKy2uq7yI3K8890G_3vCOJreRcCuswP6KZpiJaUSUv0X5CvNuRR5Apc7EIKPMWBjtsH1NsyGM_PUjEnNmJdmkuDj3nmqeqxf8H0VCfi0A1q3af-4gKZyHlrsjdDMaFMI_ZRP7yBM37p3GEwEhwNgnQQwmtq7fwX4C8CuqNc</recordid><startdate>20050225</startdate><enddate>20050225</enddate><creator>Mitkova, Atanaska V.</creator><creator>Biswas-Fiss, Esther E.</creator><creator>Biswas, Subhasis B.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>M7N</scope><scope>7X8</scope></search><sort><creationdate>20050225</creationdate><title>Modulation of DNA Synthesis in Saccharomyces cerevisiae Nuclear Extract by DNA Polymerases and the Origin Recognition Complex</title><author>Mitkova, Atanaska V. ; 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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Cell-Free System DNA Polymerase I - physiology DNA Polymerase III - physiology DNA Replication DNA Topoisomerases - physiology DNA Topoisomerases, Type I - physiology DNA, Superhelical - biosynthesis DNA-Binding Proteins - physiology DNA-Directed DNA Polymerase - physiology Minichromosome Maintenance 1 Protein - physiology Origin Recognition Complex Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae Proteins - physiology Transcription Factors - physiology |
| title | Modulation of DNA Synthesis in Saccharomyces cerevisiae Nuclear Extract by DNA Polymerases and the Origin Recognition Complex |
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