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  • 1
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    Est1p as a cell cycle-regulated activator of telomere-bound telomerase (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-10
    Description: In Saccharomyces cerevisiae, the telomerase components Est2p, TLC1 RNA, Est1p, and Est3p are thought to form a complex that acts late during chromosome replication (S phase) upon recruitment by Cdc13p, a telomeric DNA binding protein. Consistent with this model, we show that Est1p, Est2p, and Cdc13p are telomere-associated at this time. However, Est2p, but not Est1p, also binds telomeres before late S phase. The cdc13-2 allele has been proposed to be defective in recruitment, yet Est1p and Est2p telomere association persists in cdc13-2 cells. These findings suggest a model in which Est1p binds telomeres late in S phase and interacts with Cdc13p to convert inactive, telomere-bound Est2p to an active form.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taggart, Andrew K P -- Teng, Shu-Chun -- Zakian, Virginia A -- GM43265/GM/NIGMS NIH HHS/ -- T32 CA09528-16/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 9;297(5583):1023-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12169735" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; *Cell Cycle ; DNA, Fungal/genetics/metabolism ; DNA-Binding Proteins/genetics/metabolism ; Enzyme Activation ; G1 Phase ; Genes, Fungal ; Models, Biological ; Polymerase Chain Reaction ; Precipitin Tests ; RNA, Fungal/genetics/metabolism ; S Phase ; Saccharomyces cerevisiae/cytology/enzymology/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/genetics/*metabolism ; Telomerase/genetics/*metabolism ; Telomere/*metabolism ; *Telomere-Binding 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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  • 2
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    Pif1p helicase, a catalytic inhibitor of telomerase in yeast (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-05
    Description: Mutations in the yeast Saccharomyces cerevisiae PIF1 gene, which encodes a 5'-to-3' DNA helicase, cause telomere lengthening and a large increase in the formation rate of new telomeres. Here, we show that Pif1p acts by inhibiting telomerase rather than telomere-telomere recombination, and this inhibition requires the helicase activity of Pif1p. Overexpression of enzymatically active Pif1p causes telomere shortening. Thus, Pif1p is a catalytic inhibitor of telomerase-mediated telomere lengthening. Because Pif1p is associated with telomeric DNA in vivo, its effects on telomeres are likely direct. Pif1p-like helicases are found in diverse organisms, including humans. We propose that Pif1p-mediated inhibition of telomerase promotes genetic stability by suppressing telomerase-mediated healing of double-strand breaks.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, J -- Monson, E K -- Teng, S C -- Schulz, V P -- Zakian, V A -- GM26938/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Aug 4;289(5480):771-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, Princeton, NJ 08544-1014, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10926538" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Motifs ; Animals ; Catalysis ; Cell Line ; Chromosomes, Fungal/metabolism ; DNA Damage ; DNA Helicases/chemistry/genetics/*metabolism ; DNA Replication ; DNA, Fungal/metabolism ; Gene Expression ; Humans ; Mutagenesis, Site-Directed ; Point Mutation ; Recombinant Proteins/chemistry/metabolism ; Recombination, Genetic ; Saccharomyces cerevisiae/*enzymology/genetics ; *Saccharomyces cerevisiae Proteins ; Sequence Homology, Amino Acid ; Telomerase/*antagonists & inhibitors/metabolism ; Telomere/*metabolism
    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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  • 3
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    Expansion and length-dependent fragility of CTG repeats in yeast (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-28
    Description: Expansion of DNA trinucleotide repeats (TNRs) is the causative mutation in a growing number of human genetic diseases. Large expansions of a CTG tract were obtained and shown by genetic and physical assays to be length-dependent sites of chromosome breakage in Saccharomyces cerevisiae. Deletion of RAD27, which encodes a nuclease involved in Okazaki fragment processing, caused length-dependent destabilization of CTG tracts and a substantial increase in expansion frequency. The genetic assay described here can be used to evaluate other factors that induce TNR expansion or chromosome fragility in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freudenreich, C H -- Kantrow, S M -- Zakian, V A -- AG05740-02/AG/NIA NIH HHS/ -- GM26938/GM/NIGMS NIH HHS/ -- GM43265/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1998 Feb 6;279(5352):853-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9452383" target="_blank"〉PubMed〈/a〉
    Keywords: *Chromosome Breakage ; *Chromosome Fragility ; Chromosomes, Fungal/*metabolism ; DNA Damage ; DNA Repair ; DNA Replication ; DNA, Fungal/metabolism ; Electrophoresis, Gel, Pulsed-Field ; Exodeoxyribonuclease V ; Exodeoxyribonucleases/genetics ; Gene Deletion ; Genes, Fungal ; Humans ; Hydroxyurea/pharmacology ; Recombination, Genetic ; Saccharomyces cerevisiae/*genetics/metabolism ; Transformation, Genetic ; *Trinucleotide Repeat Expansion ; Trinucleotide Repeats/*genetics
    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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  • 4
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    Telomeres: beginning to understand the end (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-08
    Description: Telomeres are the protein-DNA structures at the ends of eukaryotic chromosomes. In yeast, and probably most other eukaryotes, telomeres are essential. They allow the cell to distinguish intact from broken chromosomes, protect chromosomes from degradation, and are substrates for novel replication mechanisms. Telomeres are usually replicated by telomerase, a telomere-specific reverse transcriptase, although telomerase-independent mechanisms of telomere maintenance exist. Telomere replication is both cell cycle- and developmentally regulated, and its control is likely to be complex. Because telomere loss causes the kinds of chromosomal changes associated with cancer and aging, an understanding of telomere biology has medical relevance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zakian, V A -- New York, N.Y. -- Science. 1995 Dec 8;270(5242):1601-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Princeton University, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502069" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Cycle ; Chromosomes/metabolism/physiology ; DNA/analysis/chemistry/metabolism ; DNA Replication ; DNA-Binding Proteins/metabolism ; Gene Expression Regulation ; Humans ; Molecular Sequence Data ; Telomerase/metabolism ; Telomere/chemistry/*physiology
    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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