| Characterization of functional domains in human Claspin. | |
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MedLine Citation:
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PMID: 21478680 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Claspin is a mediator of the ATR-dependent DNA replication checkpoint in human cells and also promotes DNA replication fork progression and stability. Though Claspin has been shown to bind DNA and co-immunoprecipitate with other replication fork-associated proteins, the specific protein-protein and protein-DNA interactions that are important for Claspin function are not known. We therefore purified several domains of human Claspin and then tested for direct interactions of these fragments with several replication fork-associated proteins and with DNA. Our data show that the N terminus of Claspin binds to the replicative helicase co-factor Cdc45, the Timeless protein and a branched, replication fork-like DNA structure. In contrast, the C terminus of Claspin associates with DNA polymerase epsilon and Rad17-Replication Factor C (RFC). We conclude that multiple protein-DNA and protein-protein interactions may be important for Claspin function during DNA replication and DNA replication checkpoint signaling. |
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Authors:
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Ozdemirhan Serçin; Michael G Kemp |
Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural Date: 2011-05-15 |
Journal Detail:
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Title: Cell cycle (Georgetown, Tex.) Volume: 10 ISSN: 1551-4005 ISO Abbreviation: Cell Cycle Publication Date: 2011 May |
Date Detail:
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Created Date: 2011-05-24 Completed Date: 2011-09-28 Revised Date: 2012-09-19 |
Medline Journal Info:
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Nlm Unique ID: 101137841 Medline TA: Cell Cycle Country: United States |
Other Details:
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Languages: eng Pagination: 1599-606 Citation Subset: IM |
Affiliation:
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University of North Carolina School of Medicine, Chapel Hill, NC USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adaptor Proteins, Signal Transducing
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chemistry*,
metabolism Cell Cycle Proteins / chemistry, metabolism Cell Line, Tumor DNA / chemistry, metabolism DNA Polymerase II / chemistry, metabolism DNA Replication Humans Intracellular Signaling Peptides and Proteins / chemistry, metabolism Protein Binding Protein Interaction Domains and Motifs Replication Protein C / chemistry, metabolism Signal Transduction |
| Grant Support | |
ID/Acronym/Agency:
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GM32833/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Adaptor Proteins, Signal Transducing; 0/CDC45 protein, human; 0/CLSPN protein, human; 0/Cell Cycle Proteins; 0/Intracellular Signaling Peptides and Proteins; 0/Rad17 protein, human; 0/Replication Protein C; 0/TIMELESS protein, human; 9007-49-2/DNA; EC 2.7.7.-/DNA Polymerase II |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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