| Cdc13 and telomerase bind through different mechanisms at the lagging- and leading-strand telomeres. | |
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MedLine Citation:
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PMID: 20620955 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Lagging-strand and leading-strand synthesis of chromosomes generates two structurally distinct ends at the telomeres. Based on sequence bias of yeast telomeres that contain a 250-300 bp array of C(1-3)A/ TG(1-3) repeats, we developed a method allowing us to distinguish which of the two daughter telomeres chromosome end-binding proteins bind to at the end of S phase. The single-stranded DNA-binding protein Cdc13 and the telomerase subunits Est1 and Est2 can bind to the two daughter telomeres, but only their binding to the leading-strand telomere depends on the Mre11/Rad50/Xrs2 (MRX) complex involved in both telomeric 5' nucleolytic resection and telomerase recruitment at short telomeres. Consistently, the MRX complex is mainly found to bind to the leading-strand telomere. Our results indicate that Cdc13 can bind to the telomeric template for lagging-strand replication. Since mre11-deficient strains have markedly short telomeres, telomere elongation by telomerase is likely to occur mainly at the leading-strand telomere. |
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Authors:
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Virginie Faure; Stéphane Coulon; Julien Hardy; Vincent Géli |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Molecular cell Volume: 38 ISSN: 1097-4164 ISO Abbreviation: Mol. Cell Publication Date: 2010 Jun |
Date Detail:
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Created Date: 2010-07-12 Completed Date: 2010-08-10 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9802571 Medline TA: Mol Cell Country: United States |
Other Details:
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Languages: eng Pagination: 842-52 Citation Subset: IM |
Copyright Information:
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Copyright (c) 2010 Elsevier Inc. All rights reserved. |
Affiliation:
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CNRS, UPR3081, Ifr88, Genome Instability and Carcinogenesis Conventionné par l'Université d'Aix-Marseille 2, 13402 Marseille Cedex 20, France. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Endodeoxyribonucleases
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metabolism Exodeoxyribonucleases / metabolism Protein Binding Saccharomyces cerevisiae / metabolism*, ultrastructure Saccharomyces cerevisiae Proteins / metabolism* Telomerase / metabolism* Telomere / metabolism* Telomere-Binding Proteins / metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Cdc13 protein, S cerevisiae; 0/Saccharomyces cerevisiae Proteins; 0/Telomere-Binding Proteins; EC 2.7.7.49/EST1 protein, S cerevisiae; EC 2.7.7.49/EST2 protein, S cerevisiae; EC 2.7.7.49/Telomerase; EC 3.1.-/Endodeoxyribonucleases; EC 3.1.-/Exodeoxyribonucleases; EC 3.1.-/MRE11 protein, S cerevisiae |
| Comments/Corrections | |
Comment In:
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Mol Cell. 2010 Jun 25;38(6):777-9
[PMID:
20620949
]
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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