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  • 1
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    Uninterrupted MCM2-7 function required for DNA replication fork progression (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-06-02
    Description: Little is known about the DNA helicases required for the elongation phase of eukaryotic chromosome replication. Minichromosome maintenance (MCM) protein complexes have DNA helicase activity but have only been functionally implicated in initiating DNA replication. Using an improved method for constructing conditional degron mutants, we show that depletion of MCMs after initiation irreversibly blocks the progression of replication forks in Saccharomyces cerevisiae. Like the Escherichia coli dnaB and SV40 T antigen helicases, therefore, the MCM complex is loaded at origins before initiation and is essential for elongation. Restricting MCM loading to the G(1) phase ensures that initiation and elongation occur just once per cell cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Labib, K -- Tercero, J A -- Diffley, J F -- New York, N.Y. -- Science. 2000 Jun 2;288(5471):1643-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Imperial Cancer Research Fund Clare Hall Laboratories, South Mimms, Hertfordshire, EN6 3LD, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10834843" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Cycle Proteins/genetics/*metabolism ; Chromosomal Proteins, Non-Histone ; Chromosomes, Fungal/metabolism ; *DNA Replication ; DNA, Fungal/biosynthesis ; *DNA-Binding Proteins ; Fungal Proteins/genetics/*metabolism ; G1 Phase ; G2 Phase ; *Ligases ; Minichromosome Maintenance Complex Component 4 ; Minichromosome Maintenance Complex Component 6 ; Mitosis ; Mutation ; Recombinant Fusion Proteins/metabolism ; Replicon ; S Phase ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Temperature ; *Ubiquitin-Protein Ligases
    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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  • 2
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    Checkpoint-dependent inhibition of DNA replication initiation by Sld3 and Dbf4 phosphorylation (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-09-14
    Description: The initiation of eukaryotic DNA replication is regulated by three protein kinase classes: cyclin-dependent kinases (CDK), Dbf4-dependent kinase (DDK) and the DNA damage checkpoint kinases. CDK phosphorylation of two key initiation factors, Sld2 and Sld3, promotes essential interactions with Dpb11 (refs 2-4), whereas DDK acts by phosphorylating subunits of the Mcm2-7 helicase. CDK has an additional role in replication by preventing the re-loading of Mcm2-7 during the S, G2 and M phases, thus preventing origin re-firing and re-replication. During the G1 phase, both CDK and DDK are downregulated, which allows origin licensing and prevents premature replication initiation. Origin firing is also inhibited during the S phase when DNA damage or replication fork stalling activates the checkpoint kinases. Here we show that, analogous to the situation in the G1 phase, the Saccharomyces cerevisiae checkpoint kinase Rad53 inhibits both CDK- and DDK-dependent pathways, which acts redundantly to block further origin firing. Rad53 acts on DDK directly by phosphorylating Dbf4, whereas the CDK pathway is blocked by Rad53-mediated phosphorylation of the downstream CDK substrate, Sld3. This allows CDK to remain active during the S phase in the presence of DNA damage, which is crucial to prevent re-loading of Mcm2-7 onto origins that have already fired. Our results explain how checkpoints regulate origin firing and demonstrate that the slowing of S phase by the 'intra-S checkpoint' is primarily due to the inhibition of origin firing.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2948544/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2948544/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zegerman, Philip -- Diffley, John F X -- A3556/Cancer Research UK/United Kingdom -- Cancer Research UK/United Kingdom -- England -- Nature. 2010 Sep 23;467(7314):474-8. doi: 10.1038/nature09373. Epub 2010 Sep 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research UK London Research Institute, Clare Hall Laboratories, South Mimms, Hertfordshire EN6 3LD, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20835227" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Cycle Proteins/antagonists & inhibitors/genetics/*metabolism ; Checkpoint Kinase 2 ; Cyclin-Dependent Kinases/metabolism ; DNA Damage ; DNA Replication/*physiology ; DNA-Binding Proteins/antagonists & inhibitors/genetics/*metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics/metabolism ; Replication Origin/physiology ; S Phase/*physiology ; Saccharomyces cerevisiae/*cytology/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/antagonists & inhibitors/genetics/*metabolism ; Substrate Specificity
    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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    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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  • 4
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    Positive supercoiling of mitotic DNA drives decatenation by topoisomerase II in eukaryotes (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-03-12
    Description: DNA topoisomerase II completely removes DNA intertwining, or catenation, between sister chromatids before they are segregated during cell division. How this occurs throughout the genome is poorly understood. We demonstrate that in yeast, centromeric plasmids undergo a dramatic change in their topology as the cells pass through mitosis. This change is characterized by positive supercoiling of the DNA and requires mitotic spindles and the condensin factor Smc2. When mitotic positive supercoiling occurs on decatenated DNA, it is rapidly relaxed by topoisomerase II. However, when positive supercoiling takes place in catenated plasmid, topoisomerase II activity is directed toward decatenation of the molecules before relaxation. Thus, a topological change on DNA drives topoisomerase II to decatenate molecules during mitosis, potentially driving the full decatenation of the genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baxter, J -- Sen, N -- Martinez, V Lopez -- De Carandini, M E Monturus -- Schvartzman, J B -- Diffley, J F X -- Aragon, L -- MC_U120074328/Medical Research Council/United Kingdom -- Medical Research Council/United Kingdom -- Cancer Research UK/United Kingdom -- New York, N.Y. -- Science. 2011 Mar 11;331(6022):1328-32. doi: 10.1126/science.1201538.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council (MRC) Clinical Sciences Centre, Imperial College London, Hammersmith Hospital, London, UK. Jon.Baxter@sussex.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21393545" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Cycle ; Chromosome Segregation ; DNA Replication ; DNA Topoisomerases, Type II/*metabolism ; DNA, Catenated/*chemistry/metabolism ; DNA, Fungal/*chemistry/metabolism ; DNA, Superhelical/*chemistry/metabolism ; Dimerization ; *Mitosis ; Nucleic Acid Conformation ; Plasmids ; Saccharomyces cerevisiae ; Spindle Apparatus/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Identification of a heteromeric complex that promotes DNA replication origin firing in human cells (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-05-25
    Description: Treslin/TICRR (TopBP1-interacting, replication stimulating protein/TopBP1-interacting, checkpoint, and replication regulator), the human ortholog of the yeast Sld3 protein, is an essential DNA replication factor that is regulated by cyclin-dependent kinases and the DNA damage checkpoint. We identified MDM two binding protein (MTBP) as a factor that interacts with Treslin/TICRR throughout the cell cycle. We show that MTBP depletion by means of small interfering RNA inhibits DNA replication by preventing assembly of the CMG (Cdc45-MCM-GINS) holohelicase during origin firing. Although MTBP has been implicated in the function of the p53 tumor suppressor, we found MTBP is required for DNA replication irrespective of a cell's p53 status. We propose that MTBP acts with Treslin/TICRR to integrate signals from cell cycle and DNA damage response pathways to control the initiation of DNA replication in human cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boos, Dominik -- Yekezare, Mona -- Diffley, John F X -- Cancer Research UK/United Kingdom -- New York, N.Y. -- Science. 2013 May 24;340(6135):981-4. doi: 10.1126/science.1237448.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research UK London Research Institute (LRI), Clare Hall Laboratories, South Mimms, Herts., UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23704573" target="_blank"〉PubMed〈/a〉
    Keywords: Carrier Proteins/genetics/*metabolism ; Cell Cycle Proteins/*metabolism ; Chromatin/metabolism ; DNA Damage ; DNA Replication/genetics/*physiology ; DNA-Binding Proteins/metabolism ; G1 Phase Cell Cycle Checkpoints ; HeLa Cells ; Humans ; Proliferating Cell Nuclear Antigen/metabolism ; RNA Interference ; RNA, Small Interfering/genetics ; *Replication Origin
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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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
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  • 7
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    Similarity between the transcriptional silencer binding proteins ABF1 and RAP1 (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-11-24
    Description: The yeast ARS binding factor 1 (ABF1)--where ARS is an autonomously replicating sequence--and repressor/activator protein 1 (RAP1) have been implicated in DNA replication, transcriptional activation, and transcriptional silencing. The ABF1 gene was cloned and sequenced and shown to be essential for viability. The predicted amino acid sequence contains a novel sequence motif related to the zinc finger, and the ABF1 protein requires zinc and unmodified cysteine residues for sequence-specific DNA binding. Interestingly, ABF1 is extensively related to its counterpart, RAP1, and both proteins share a region of similarity with SAN1, a suppressor of certain SIR4 mutations, suggesting that this region may be involved in mediating SIR function at the silent mating type loci.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Diffley, J F -- Stillman, B -- AI20460/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1989 Nov 24;246(4933):1034-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, NY 11724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2511628" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA-Binding Proteins/*genetics ; Fungal Proteins/*genetics ; *Genes, Fungal ; Metalloproteins/genetics ; Molecular Sequence Data ; Restriction Mapping ; Saccharomyces cerevisiae/*genetics ; *Saccharomyces cerevisiae Proteins ; Sequence Homology, Nucleic Acid ; *Transcription Factors ; *Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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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
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  • 9
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    Stepwise assembly of initiation proteins at budding yeast replication origins in vitro (2000)
    National Academy of Sciences
    Details
    Publication Date: 2000-12-19
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 10
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    A close relative of the nuclear, chromosomal high-mobility group protein HMG1 in yeast mitochondria. (1991)
    National Academy of Sciences
    Details
    Publication Date: 1991-09-01
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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