The finger subdomain of yeast telomerase cooperates with Pif1p to limit telomere elongation
| Autor: | Alessandra Pollice, Joachim Lingner, John F. Pulitzer, Yves Corda, Chiara Lanzuolo, Anne Sophie Berthiau, Klaus Förstemann, Pierre Luciano, Eric Gilson, Anne Eugster, Manon Bonneton, Vincent Géli, Emma Stegberg |
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| Přispěvatelé: | Unité mixte de recherche biologie moléculaire de la cellule, Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-École normale supérieure - Lyon (ENS Lyon), Laboratoire de Biologie Moléculaire de la Cellule (LBMC), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), École normale supérieure - Cachan (ENS Cachan), Università degli studi di Napoli Federico II, Centre National de la Recherche Scientifique (CNRS), Ecole Polytechnique Fédérale de Lausanne (EPFL), École normale supérieure de Lyon (ENS de Lyon)-Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS), École normale supérieure de Lyon (ENS de Lyon)-Université Claude Bernard Lyon 1 (UCBL), University of Naples Federico II = Università degli studi di Napoli Federico II |
| Předmět: |
Telomerase
Saccharomyces cerevisiae Proteins [SDV]Life Sciences [q-bio] Protein subunit Saccharomyces cerevisiae Biology S Phase Telomerase RNA component Structural Biology [INFO]Computer Science [cs] Telomerase reverse transcriptase Molecular Biology ComputingMilieux_MISCELLANEOUS DNA Helicases RNA Helicase RNA Fungal Telomere Molecular biology GENOMIQUE Reverse transcriptase Protein Structure Tertiary DNA-Binding Proteins PIF1P Mutation biology.protein |
| Zdroj: | Nature Structural and Molecular Biology Nature Structural and Molecular Biology, Nature Publishing Group, 2006, 13 (8), pp.734-739 HAL Nature Structural and Molecular Biology, 2006, 13 (8), pp.734-739 |
| ISSN: | 1545-9993 1545-9985 |
| Popis: | Telomere synthesis depends on telomerase, which contains an RNA subunit linked to a specialized reverse transcriptase subunit and several associated proteins. Here we report the characterization of four mutations in the yeast reverse transcriptase subunit Est2p that cause an overelongation of telomeres and an increase in the association of Est1p with telomeres during S phase. These 'up-mutations' are clustered in the finger subdomain of the reverse transcriptase. We show that the catalytic properties of the up-mutant telomerases are not improved in vitro. In vivo, the up-mutations neither bypass the activation step governed by Cdc13p nor do they uncouple telomerase from the Rap1p inhibition pathway. In the presence of the up-mutations, however, the ability of the Pif1p helicase to decrease telomere length and to inhibit the association of Est1p with telomeres is impaired. In addition, Pif1p associates in vivo with the telomerase RNA (TLC1) in a way that depends on the finger subdomain. We propose that, in addition to its catalytic role, the finger subdomain of Est2p facilitates the action of Pif1p at telomeres. |
| Databáze: | OpenAIRE |
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