The PIAS homologue Siz2 regulates perinuclear telomere position and telomerase activity in budding yeast
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Helder C Ferreira
- Brian Luke
- Heiko Schober
- Veronique Kalck
- Joachim Lingner
- Susan M Gasser
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000292305700018&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1038/ncb2263
- eISSN
- 1476-4679
- Externe Identifier
- Clarivate Analytics Document Solution ID: 786KD
- PubMed Identifier: 21666682
- ISSN
- 1465-7392
- Ausgabe der Veröffentlichung
- 7
- Zeitschrift
- NATURE CELL BIOLOGY
- Paginierung
- 867 - U313
- Datum der Veröffentlichung
- 2011
- Status
- Published
- Titel
- The PIAS homologue Siz2 regulates perinuclear telomere position and telomerase activity in budding yeast
- Sub types
- Article
- Ausgabe der Zeitschrift
- 13
Datenquelle: Web of Science (Lite)
- Andere Metadatenquellen:
-
- Autoren
- Helder C Ferreira
- Brian Luke
- Heiko Schober
- Véronique Kalck
- Joachim Lingner
- Susan M Gasser
- DOI
- 10.1038/ncb2263
- eISSN
- 1476-4679
- ISSN
- 1465-7392
- Ausgabe der Veröffentlichung
- 7
- Zeitschrift
- Nature Cell Biology
- Sprache
- en
- Online publication date
- 2011
- Paginierung
- 867 - 874
- Datum der Veröffentlichung
- 2011
- Status
- Published
- Herausgeber
- Springer Science and Business Media LLC
- Herausgeber URL
- http://dx.doi.org/10.1038/ncb2263
- Datum der Datenerfassung
- 2023
- Titel
- The PIAS homologue Siz2 regulates perinuclear telomere position and telomerase activity in budding yeast
- Ausgabe der Zeitschrift
- 13
Datenquelle: Crossref
- Abstract
- Budding yeast telomeres are reversibly bound at the nuclear envelope through two partially redundant pathways that involve the Sir2/3/4 silencing complex and the Yku70/80 heterodimer. To better understand how this is regulated, we studied the role of SUMOylation in telomere anchoring. We find that the PIAS-like SUMO E3 ligase Siz2 sumoylates both Yku70/80 and Sir4 in vivo and promotes telomere anchoring to the nuclear envelope. Remarkably, loss of Siz2 also provokes telomere extension in a telomerase-dependent manner that is epistatic with loss of the helicase Pif1. Consistent with our previously documented role for telomerase in anchorage, normal telomere anchoring in siz2 Δ is restored by PIF1 deletion. By live-cell imaging of a critically short telomere, we show that telomeres shift away from the nuclear envelope when elongating. We propose that SUMO-dependent association with the nuclear periphery restrains bound telomerase, whereas active elongation correlates with telomere release.
- Addresses
- Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, 4058 Basel, Switzerland.
- Autoren
- Helder C Ferreira
- Brian Luke
- Heiko Schober
- Véronique Kalck
- Joachim Lingner
- Susan M Gasser
- DOI
- 10.1038/ncb2263
- eISSN
- 1476-4679
- Externe Identifier
- PubMed Identifier: 21666682
- Funding acknowledgements
- European Research Council: 232812
- European Commission FP7: FP7_200950
- European Commission FP7: FP7_232812
- Open access
- false
- ISSN
- 1465-7392
- Ausgabe der Veröffentlichung
- 7
- Zeitschrift
- Nature cell biology
- Schlüsselwörter
- Nuclear Envelope
- Telomere
- Saccharomyces cerevisiae
- DNA Helicases
- Telomerase
- DNA-Binding Proteins
- Saccharomyces cerevisiae Proteins
- Silent Information Regulator Proteins, Saccharomyces cerevisiae
- Recombinant Fusion Proteins
- Microscopy, Fluorescence
- Protein Processing, Post-Translational
- Mutation
- Time Factors
- Sumoylation
- Sprache
- eng
- Medium
- Electronic
- Online publication date
- 2011
- Paginierung
- 867 - 874
- Datum der Veröffentlichung
- 2011
- Status
- Published
- Datum der Datenerfassung
- 2011
- Titel
- The PIAS homologue Siz2 regulates perinuclear telomere position and telomerase activity in budding yeast.
- Sub types
- Research Support, Non-U.S. Gov't
- Journal Article
- Ausgabe der Zeitschrift
- 13
Datenquelle: Europe PubMed Central
- Abstract
- Budding yeast telomeres are reversibly bound at the nuclear envelope through two partially redundant pathways that involve the Sir2/3/4 silencing complex and the Yku70/80 heterodimer. To better understand how this is regulated, we studied the role of SUMOylation in telomere anchoring. We find that the PIAS-like SUMO E3 ligase Siz2 sumoylates both Yku70/80 and Sir4 in vivo and promotes telomere anchoring to the nuclear envelope. Remarkably, loss of Siz2 also provokes telomere extension in a telomerase-dependent manner that is epistatic with loss of the helicase Pif1. Consistent with our previously documented role for telomerase in anchorage, normal telomere anchoring in siz2 Δ is restored by PIF1 deletion. By live-cell imaging of a critically short telomere, we show that telomeres shift away from the nuclear envelope when elongating. We propose that SUMO-dependent association with the nuclear periphery restrains bound telomerase, whereas active elongation correlates with telomere release.
- Date of acceptance
- 2011
- Autoren
- Helder C Ferreira
- Brian Luke
- Heiko Schober
- Véronique Kalck
- Joachim Lingner
- Susan M Gasser
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/21666682
- DOI
- 10.1038/ncb2263
- eISSN
- 1476-4679
- Funding acknowledgements
- European Research Council: 232812
- Ausgabe der Veröffentlichung
- 7
- Zeitschrift
- Nat Cell Biol
- Schlüsselwörter
- DNA Helicases
- DNA-Binding Proteins
- Microscopy, Fluorescence
- Mutation
- Nuclear Envelope
- Protein Processing, Post-Translational
- Recombinant Fusion Proteins
- Saccharomyces cerevisiae
- Saccharomyces cerevisiae Proteins
- Silent Information Regulator Proteins, Saccharomyces cerevisiae
- Sumoylation
- Telomerase
- Telomere
- Time Factors
- Sprache
- eng
- Country
- England
- Paginierung
- 867 - 874
- PII
- ncb2263
- Datum der Veröffentlichung
- 2011
- Status
- Published online
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2011
- Titel
- The PIAS homologue Siz2 regulates perinuclear telomere position and telomerase activity in budding yeast.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 13
Datenquelle: PubMed
- Abstract
- Budding yeast telomeres are reversibly bound at the nuclear envelope through two partially redundant pathways that involve the Sir2/3/4 silencing complex and the Yku70/80 heterodimer. To better understand how this is regulated, we studied the role of SUMOylation in telomere anchoring. We find that the PIAS-like SUMO E3 ligase Siz2 sumoylates both Yku70/80 and Sir4 in vivo and promotes telomere anchoring to the nuclear envelope. Remarkably, loss of Siz2 also provokes telomere extension in a telomerase-dependent manner that is epistatic with loss of the helicase Pif1. Consistent with our previously documented role for telomerase in anchorage, normal telomere anchoring in siz2 \textgreekD is restored by PIF1 deletion. By live-cell imaging of a critically short telomere, we show that telomeres shift away from the nuclear envelope when elongating. We propose that SUMO-dependent association with the nuclear periphery restrains bound telomerase, whereas active elongation correlates with telomere release.
- Autoren
- Helder C Ferreira
- Brian Luke
- Heiko Schober
- Véronique Kalck
- Joachim Lingner
- Susan M Gasser
- DOI
- 10.1038/ncb2263
- Zeitschrift
- Nature cell biology
- Notes
- keywords: DNA Helicases/genetics/metabolism;DNA-Binding Proteins/genetics/metabolism;Microscopy, Fluorescence;Mutation;Nuclear Envelope/enzymology;Protein Processing, Post-Translational;Recombinant Fusion Proteins/metabolism;Saccharomyces cerevisiae Proteins/genetics/metabolism;Saccharomyces cerevisiae/enzymology/genetics;Silent Information Regulator Proteins, Saccharomyces cerevisiae/genetics/metabolism;Sumoylation;Telomerase/metabolism;Telomere/enzymology;Time Factors
- Artikelnummer
- 7
- Paginierung
- 867 - 874
- Datum der Veröffentlichung
- 2011
- Datum der Datenerfassung
- 2023
- Titel
- The PIAS homologue Siz2 regulates perinuclear telomere position and telomerase activity in budding yeast
- Sub types
- article
- Ausgabe der Zeitschrift
- 13
Datenquelle: Manual
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