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  1. Article ; Online: DNA replication origins, ORC/DNA interaction, and assembly of pre-replication complex in eukaryotes.

    Sun, Jingya / Kong, Daochun

    Acta biochimica et biophysica Sinica

    2010  Volume 42, Issue 7, Page(s) 433–439

    Abstract: ... significant diversity in origin structure, assembly of pre-replication complex (pre-RC) and regulation ... how DNA replication origins are organized, how pre-RC is assembled and how DNA replication is ... Chromosomal DNA replication in eukaryotic cells is highly complicated and sophisticatedly regulated ...

    Abstract Chromosomal DNA replication in eukaryotic cells is highly complicated and sophisticatedly regulated. Owing to its large size, a typical eukaryotic genome contains hundreds to tens of thousands of initiation sites called DNA replication origins where DNA synthesis takes place. Multiple initiation sites remove the constraint of a genome size because only a certain amount of DNA can be replicated from a single origin in a limited time. The activation of these multiple origins must be coordinated so that each segment of chromosomal DNA is precisely duplicated only once per cell cycle. Although DNA replication is a vital process for cell growth and its mechanism is highly conserved, recent studies also reveal significant diversity in origin structure, assembly of pre-replication complex (pre-RC) and regulation of replication initiation along evolutionary lines. The DNA replication origins in the fission yeast Schizosaccharomyces pombe are found to contain a second essential element that is bound by Sap1 protein besides the essential origin recognition complex-binding site. Sap1 is recently demonstrated to be a novel replication initiation protein that plays an essential role in loading the initiation protein Cdc18 to origins and thus directly participates in pre-RC formation. In this review, we summarize the recent advance in understanding how DNA replication origins are organized, how pre-RC is assembled and how DNA replication is initiated and regulated in yeast and metazoans.
    MeSH term(s) Animals ; Cell Cycle ; DNA/metabolism ; DNA Replication ; Eukaryotic Cells/metabolism ; Models, Biological ; Origin Recognition Complex/genetics ; Origin Recognition Complex/metabolism ; Protein Binding ; Replication Origin
    Chemical Substances Origin Recognition Complex ; DNA (9007-49-2)
    Language English
    Publishing date 2010-07
    Publishing country China
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2175256-4
    ISSN 1745-7270 ; 0582-9879 ; 1672-9145
    ISSN (online) 1745-7270
    ISSN 0582-9879 ; 1672-9145
    DOI 10.1093/abbs/gmq048
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Dynamic association of ORCA with prereplicative complex components regulates DNA replication initiation.

    Shen, Zhen / Chakraborty, Arindam / Jain, Ankur / Giri, Sumanprava / Ha, Taekjip / Prasanth, Kannanganattu V / Prasanth, Supriya G

    Molecular and cellular biology

    2012  Volume 32, Issue 15, Page(s) 3107–3120

    Abstract: In eukaryotes, initiation of DNA replication requires the assembly of a multiprotein prereplicative ... complex (pre-RC) at the origins. We recently reported that a WD repeat-containing protein ... of its interacting partners on chromatin and facilitates DNA replication initiation. ...

    Abstract In eukaryotes, initiation of DNA replication requires the assembly of a multiprotein prereplicative complex (pre-RC) at the origins. We recently reported that a WD repeat-containing protein, origin recognition complex (ORC)-associated (ORCA/LRWD1), plays a crucial role in stabilizing ORC to chromatin. Here, we find that ORCA is required for the G(1)-to-S-phase transition in human cells. In addition to binding to ORC, ORCA associates with Cdt1 and its inhibitor, geminin. Single-molecule pulldown experiments demonstrate that each molecule of ORCA can bind to one molecule of ORC, one molecule of Cdt1, and two molecules of geminin. Further, ORCA directly interacts with the N terminus of Orc2, and the stability of ORCA is dependent on its association with Orc2. ORCA associates with Orc2 throughout the cell cycle, with Cdt1 during mitosis and G(1), and with geminin in post-G(1) cells. Overexpression of geminin results in the loss of interaction between ORCA and Cdt1, suggesting that increased levels of geminin in post-G(1) cells titrate Cdt1 away from ORCA. We propose that the dynamic association of ORCA with pre-RC components modulates the assembly of its interacting partners on chromatin and facilitates DNA replication initiation.
    MeSH term(s) Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Cell Cycle/genetics ; Cell Cycle Proteins/biosynthesis ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Cell Line, Tumor ; Cell Nucleus/genetics ; Cell Nucleus/metabolism ; Chromatin/metabolism ; DNA Replication/physiology ; DNA-Binding Proteins/metabolism ; G1 Phase Cell Cycle Checkpoints ; Geminin ; HeLa Cells ; Humans ; Mitosis ; Origin Recognition Complex/genetics ; Origin Recognition Complex/metabolism ; Protein Binding/genetics ; Sequestosome-1 Protein
    Chemical Substances Adaptor Proteins, Signal Transducing ; CDT1 protein, human ; Cell Cycle Proteins ; Chromatin ; DNA-Binding Proteins ; GMNN protein, human ; Geminin ; ORC2 protein, human ; Origin Recognition Complex ; SQSTM1 protein, human ; Sequestosome-1 Protein
    Language English
    Publishing date 2012-05-29
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 779397-2
    ISSN 1098-5549 ; 0270-7306
    ISSN (online) 1098-5549
    ISSN 0270-7306
    DOI 10.1128/MCB.00362-12
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1666: Show issues Location:
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  3. Article ; Online: Dynamic Association of ORCA with Prereplicative Complex Components Regulates DNA Replication Initiation

    Shen, Zhen / Chakraborty, Arindam / Jain, Ankur / Giri, Sumanprava / Ha, Taekjip / Prasanth, Kannanganattu V. / Prasanth, Supriya G.

    Molecular and Cellular Biology. 2012 Aug. 1, v. 32, no. 15 p.3107-3120

    2012  

    Abstract: In eukaryotes, initiation of DNA replication requires the assembly of a multiprotein prereplicative ... complex (pre-RC) at the origins. We recently reported that a WD repeat-containing protein ... of its interacting partners on chromatin and facilitates DNA replication initiation. ...

    Abstract In eukaryotes, initiation of DNA replication requires the assembly of a multiprotein prereplicative complex (pre-RC) at the origins. We recently reported that a WD repeat-containing protein, origin recognition complex (ORC)-associated (ORCA/LRWD1), plays a crucial role in stabilizing ORC to chromatin. Here, we find that ORCA is required for the G₁-to-S-phase transition in human cells. In addition to binding to ORC, ORCA associates with Cdt1 and its inhibitor, geminin. Single-molecule pulldown experiments demonstrate that each molecule of ORCA can bind to one molecule of ORC, one molecule of Cdt1, and two molecules of geminin. Further, ORCA directly interacts with the N terminus of Orc2, and the stability of ORCA is dependent on its association with Orc2. ORCA associates with Orc2 throughout the cell cycle, with Cdt1 during mitosis and G₁, and with geminin in post-G₁ cells. Overexpression of geminin results in the loss of interaction between ORCA and Cdt1, suggesting that increased levels of geminin in post-G₁ cells titrate Cdt1 away from ORCA. We propose that the dynamic association of ORCA with pre-RC components modulates the assembly of its interacting partners on chromatin and facilitates DNA replication initiation.
    Keywords DNA replication ; chromatin ; eukaryotic cells ; humans ; mitosis
    Language English
    Dates of publication 2012-0801
    Size p. 3107-3120.
    Publishing place Taylor & Francis
    Document type Article ; Online
    ZDB-ID 779397-2
    ISSN 1098-5549 ; 0270-7306
    ISSN (online) 1098-5549
    ISSN 0270-7306
    DOI 10.1128/MCB.00362-12
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    In stock of ZB MED Cologne/Königswinter

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  4. Article: Interactions and subcellular distribution of DNA replication initiation proteins in eukaryotic cells.

    Brand, Normen / Faul, Thomas / Grummt, Friedrich

    Molecular genetics and genomics : MGG

    2007  Volume 278, Issue 6, Page(s) 623–632

    Abstract: For initiation of eukaryotic DNA replication the origin recognition complex (ORC) associates ... interaction in pre-RC assembly, the interaction between Orc2 and Orc3, is not restricted to the nucleus ... replication complex (pre-RC). In S phase, the putative MCM helicase is assumed to move away from the ORC ...

    Abstract For initiation of eukaryotic DNA replication the origin recognition complex (ORC) associates with chromatin sites and constitutes a landing pad allowing Cdc6, Cdt1 and MCM proteins to accomplish the pre-replication complex (pre-RC). In S phase, the putative MCM helicase is assumed to move away from the ORC to trigger DNA unwinding. By using the fluorescence-based assays bioluminescence resonance energy transfer (BRET) and bimolecular fluorescence complementation (BiFC) we show in live mammalian cells that one key interaction in pre-RC assembly, the interaction between Orc2 and Orc3, is not restricted to the nucleus but also occurs in the cytoplasm. BRET assays also revealed a direct interaction between Orc2 and nuclear localization signal (NLS)-depleted Orc3. Further, we assessed the subcellular distribution of Orc2 and Orc3 in relation to MCM proteins Mcm3 and Mcm6 as well as to a key protein involved in elongation of DNA replication, proliferating nuclear cell antigen (PCNA). Our findings illustrate the spatial complexity of the elaborated process of DNA replication as well as that the BRET and BiFC techniques are novel tools that could contribute to our understanding of the processes at the very beginning of the duplication of the genome.
    MeSH term(s) Animals ; Biotechnology/methods ; Cell Nucleus/metabolism ; Cells, Cultured ; Cytoplasm/metabolism ; DNA Replication ; Eukaryotic Cells ; Humans ; Mice ; Origin Recognition Complex/metabolism ; Peptide Chain Elongation, Translational ; Replication Origin ; Spectrometry, Fluorescence/methods ; Transfection
    Chemical Substances ORC2 protein, human ; ORC3 protein, human ; Origin Recognition Complex
    Language English
    Publishing date 2007-12
    Publishing country Germany
    Document type Evaluation Studies ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2044817-X
    ISSN 1617-4623 ; 1617-4615
    ISSN (online) 1617-4623
    ISSN 1617-4615
    DOI 10.1007/s00438-007-0278-1
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1198: Show issues Location:
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  5. Article: Interactions and subcellular distribution of DNA replication initiation proteins in eukaryotic cells

    Brand, Normen / Faul, Thomas / Grummt, Friedrich

    Molecular genetics and genomics MGG. 2007 Dec., v. 278, no. 6

    2007  

    Abstract: For initiation of eukaryotic DNA replication the origin recognition complex (ORC) associates ... interaction in pre-RC assembly, the interaction between Orc2 and Orc3, is not restricted to the nucleus ... replication complex (pre-RC). In S phase, the putative MCM helicase is assumed to move away from the ORC ...

    Abstract For initiation of eukaryotic DNA replication the origin recognition complex (ORC) associates with chromatin sites and constitutes a landing pad allowing Cdc6, Cdt1 and MCM proteins to accomplish the pre-replication complex (pre-RC). In S phase, the putative MCM helicase is assumed to move away from the ORC to trigger DNA unwinding. By using the fluorescence-based assays bioluminescence resonance energy transfer (BRET) and bimolecular fluorescence complementation (BiFC) we show in live mammalian cells that one key interaction in pre-RC assembly, the interaction between Orc2 and Orc3, is not restricted to the nucleus but also occurs in the cytoplasm. BRET assays also revealed a direct interaction between Orc2 and nuclear localization signal (NLS)-depleted Orc3. Further, we assessed the subcellular distribution of Orc2 and Orc3 in relation to MCM proteins Mcm3 and Mcm6 as well as to a key protein involved in elongation of DNA replication, proliferating nuclear cell antigen (PCNA). Our findings illustrate the spatial complexity of the elaborated process of DNA replication as well as that the BRET and BiFC techniques are novel tools that could contribute to our understanding of the processes at the very beginning of the duplication of the genome.
    Keywords DNA replication
    Language English
    Dates of publication 2007-12
    Size p. 623-632.
    Publisher Springer-Verlag
    Publishing place Berlin/Heidelberg
    Document type Article
    ISSN 1617-4615
    DOI 10.1007/s00438-007-0278-1
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  6. Article: CDK phosphorylation inhibits the DNA-binding and ATP-hydrolysis activities of the Drosophila origin recognition complex.

    Remus, Dirk / Blanchette, Marco / Rio, Donald C / Botchan, Michael R

    The Journal of biological chemistry

    2005  Volume 280, Issue 48, Page(s) 39740–39751

    Abstract: ... following origin activation. The origin recognition complex (ORC) initiates the assembly of pre-RCs ... at origins of replication and Cdk phosphorylation of ORC is important for the prevention of re-initiation. Here we show ... molecular mechanisms by which Cdks may inhibit ORC function as part of re-replication control and show ...

    Abstract Faithful propagation of eukaryotic chromosomes usually requires that no DNA segment be replicated more than once during one cell cycle. Cyclin-dependent kinases (Cdks) are critical for the re-replication controls that inhibit the activities of components of the pre-replication complexes (pre-RCs) following origin activation. The origin recognition complex (ORC) initiates the assembly of pre-RCs at origins of replication and Cdk phosphorylation of ORC is important for the prevention of re-initiation. Here we show that Drosophila melanogaster ORC (DmORC) is phosphorylated in vivo and is a substrate for Cdks in vitro. Cdk phosphorylation of DmORC subunits DmOrc1p and DmOrc2p inhibits the intrinsic ATPase activity of DmORC without affecting ATP binding to DmOrc1p. Moreover, Cdk phosphorylation inhibits the ATP-dependent DNA-binding activity of DmORC in vitro, thus identifying a novel determinant for DmORC-DNA interaction. DmORC is a substrate for both Cdk2 x cyclin E and Cdk1 x cyclin B in vitro. Such phosphorylation of DmORC by Cdk2 x cyclin E, but not by Cdk1 x cyclin B, requires an "RXL" motif in DmOrc1p. We also identify casein kinase 2 (CK2) as a kinase activity in embryonic extracts targeting DmORC for modification. CK2 phosphorylation does not affect ATP hydrolysis by DmORC but modulates the ATP-dependent DNA-binding activity of DmORC. These results suggest molecular mechanisms by which Cdks may inhibit ORC function as part of re-replication control and show that DmORC activity may be modulated in response to phosphorylation by multiple kinases.
    MeSH term(s) Adenosine Triphosphatases/chemistry ; Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/chemistry ; Amino Acid Motifs ; Animals ; Cell Nucleus/metabolism ; Cell Proliferation ; Cross-Linking Reagents/pharmacology ; Cyclin B/metabolism ; Cyclin E/metabolism ; Cyclin-Dependent Kinases/metabolism ; DNA/chemistry ; DNA Replication ; Drosophila melanogaster ; Hydrolysis ; Immunoprecipitation ; Mass Spectrometry ; Models, Genetic ; Origin Recognition Complex ; Phosphorylation ; Protein Binding ; Protein Kinases/metabolism ; Purines/pharmacology ; Silver Staining ; Time Factors ; Triazoles/pharmacology
    Chemical Substances 4,5,6,7-tetrabromobenzotriazole ; 6-((3-chloro)anilino)-2-(isopropyl-2-hydroxyethylamino)-9-isopropylpurine ; Cross-Linking Reagents ; Cyclin B ; Cyclin E ; Origin Recognition Complex ; Purines ; Triazoles ; Adenosine Triphosphate (8L70Q75FXE) ; DNA (9007-49-2) ; Protein Kinases (EC 2.7.-) ; histone H1 kinase (EC 2.7.1.-) ; Cyclin-Dependent Kinases (EC 2.7.11.22) ; Adenosine Triphosphatases (EC 3.6.1.-)
    Language English
    Publishing date 2005-09-27
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M508515200
    Database MEDical Literature Analysis and Retrieval System OnLINE

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