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  • 1
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    Regulated eukaryotic DNA replication origin firing with purified proteins (2015)
    Nature Publishing Group (NPG)
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    Publication Date: 2015-03-06
    Description: Eukaryotic cells initiate DNA replication from multiple origins, which must be tightly regulated to promote precise genome duplication in every cell cycle. To accomplish this, initiation is partitioned into two temporally discrete steps: a double hexameric minichromosome maintenance (MCM) complex is first loaded at replication origins during G1 phase, and then converted to the active CMG (Cdc45-MCM-GINS) helicase during S phase. Here we describe the reconstitution of budding yeast DNA replication initiation with 16 purified replication factors, made from 42 polypeptides. Origin-dependent initiation recapitulates regulation seen in vivo. Cyclin-dependent kinase (CDK) inhibits MCM loading by phosphorylating the origin recognition complex (ORC) and promotes CMG formation by phosphorylating Sld2 and Sld3. Dbf4-dependent kinase (DDK) promotes replication by phosphorylating MCM, and can act either before or after CDK. These experiments define the minimum complement of proteins, protein kinase substrates and co-factors required for regulated eukaryotic DNA replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yeeles, Joseph T P -- Deegan, Tom D -- Janska, Agnieszka -- Early, Anne -- Diffley, John F X -- Cancer Research UK/United Kingdom -- England -- Nature. 2015 Mar 26;519(7544):431-5. doi: 10.1038/nature14285. Epub 2015 Mar 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research UK London Research Institute, Clare Hall Laboratories, South Mimms EN6 3LD, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25739503" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Cycle Proteins/metabolism ; Cyclin-Dependent Kinases/metabolism ; *DNA Replication ; DNA-Binding Proteins/metabolism ; DNA-Directed DNA Polymerase/metabolism ; Minichromosome Maintenance Proteins/metabolism ; Multienzyme Complexes/metabolism ; Multiprotein Complexes/chemistry/metabolism ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/metabolism ; Replication Origin/genetics/*physiology ; Replication Protein A/metabolism ; Saccharomyces cerevisiae/enzymology/*genetics/*metabolism ; Saccharomyces cerevisiae Proteins/*isolation & purification/*metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 2
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    ATPase-dependent quality control of DNA replication origin licensing (2013)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2013-03-12
    Description: The regulated loading of the Mcm2-7 DNA helicase (comprising six related subunits, Mcm2 to Mcm7) into pre-replicative complexes at multiple replication origins ensures precise once per cell cycle replication in eukaryotic cells. The origin recognition complex (ORC), Cdc6 and Cdt1 load Mcm2-7 into a double hexamer bound around duplex DNA in an ATP-dependent reaction, but the molecular mechanism of this origin 'licensing' is still poorly understood. Here we show that both Mcm2-7 hexamers in Saccharomyces cerevisiae are recruited to origins by an essential, conserved carboxy-terminal domain of Mcm3 that interacts with and stimulates the ATPase activity of ORC-Cdc6. ATP hydrolysis can promote Mcm2-7 loading, but can also promote Mcm2-7 release if components are missing or if ORC has been inactivated by cyclin-dependent kinase phosphorylation. Our work provides new insights into how origins are licensed and reveals a novel ATPase-dependent mechanism contributing to precise once per cell cycle replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frigola, Jordi -- Remus, Dirk -- Mehanna, Amina -- Diffley, John F X -- Cancer Research UK/United Kingdom -- England -- Nature. 2013 Mar 21;495(7441):339-43. doi: 10.1038/nature11920. Epub 2013 Mar 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research UK London Research Institute, Clare Hall Laboratories, South Mimms EN6 3LD, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23474987" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/*metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Cell Cycle Proteins/metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; DNA Replication/*genetics ; DNA-Binding Proteins/metabolism ; Enzyme Activation ; Hydrolysis ; Minichromosome Maintenance Complex Component 3 ; Minichromosome Maintenance Complex Component 7 ; Nuclear Proteins/metabolism ; Protein Binding ; Replication Origin/*genetics ; Saccharomyces cerevisiae/cytology/enzymology/*genetics/*metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Sequence Alignment
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 3
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    Interaction of Dbf4, the Cdc7 protein kinase regulatory subunit, with yeast replication origins in vivo (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-26
    Description: DNA replication in the budding yeast Saccharomyces cerevisiae initiates from origins of specific DNA sequences during S phase. A screen based on two- and one-hybrid approaches demonstrates that the product of the DBF4 gene interacts with yeast replication origins in vivo. The Dbf4 protein interacts with and positively regulates the activity of the Cdc7 protein kinase, which is required for entry into S phase in the yeast mitotic cell cycle. The analysis described here suggests a model in which one function of Dbf4 may be to recruit the Cdc7 protein kinase to initiation complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dowell, S J -- Romanowski, P -- Diffley, J F -- New York, N.Y. -- Science. 1994 Aug 26;265(5176):1243-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Imperial Cancer Research Fund, Clare Hall Laboratories, South Mimms, Hertfordshire, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8066465" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Cell Cycle Proteins ; *DNA Replication ; DNA, Fungal/biosynthesis ; Enzyme Activation ; Fungal Proteins/genetics/*metabolism ; Models, Biological ; Molecular Sequence Data ; Point Mutation ; Protein Kinases/genetics/*metabolism ; *Protein-Serine-Threonine Kinases ; Replicon ; S Phase ; Saccharomyces cerevisiae/cytology/enzymology/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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