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The PIAS homologue Siz2 regulates perinuclear telomere position and telomerase activity in budding yeast

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The PIAS homologue Siz2 regulates perinuclear telomere position and telomerase activity in budding yeast. / Ferreira, Helder Casimiro; Luke, Brian; Schober, Heiko; Kalck, Veronique; Lingner, Joachim; Gasser, Susan M.

In: Nature Cell Biology, Vol. 13, No. 7, 07.2011, p. 867-874.

Research output: Contribution to journalArticlepeer-review

Harvard

Ferreira, HC, Luke, B, Schober, H, Kalck, V, Lingner, J & Gasser, SM 2011, 'The PIAS homologue Siz2 regulates perinuclear telomere position and telomerase activity in budding yeast', Nature Cell Biology, vol. 13, no. 7, pp. 867-874. https://doi.org/10.1038/ncb2263

APA

Ferreira, H. C., Luke, B., Schober, H., Kalck, V., Lingner, J., & Gasser, S. M. (2011). The PIAS homologue Siz2 regulates perinuclear telomere position and telomerase activity in budding yeast. Nature Cell Biology, 13(7), 867-874. https://doi.org/10.1038/ncb2263

Vancouver

Ferreira HC, Luke B, Schober H, Kalck V, Lingner J, Gasser SM. The PIAS homologue Siz2 regulates perinuclear telomere position and telomerase activity in budding yeast. Nature Cell Biology. 2011 Jul;13(7):867-874. https://doi.org/10.1038/ncb2263

Author

Ferreira, Helder Casimiro ; Luke, Brian ; Schober, Heiko ; Kalck, Veronique ; Lingner, Joachim ; Gasser, Susan M. / The PIAS homologue Siz2 regulates perinuclear telomere position and telomerase activity in budding yeast. In: Nature Cell Biology. 2011 ; Vol. 13, No. 7. pp. 867-874.

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@article{fb77d77236b44f2184ae0cb4f8baa324,
title = "The PIAS homologue Siz2 regulates perinuclear telomere position and telomerase activity in budding yeast",
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(1,2). 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(3), normal telomere anchoring in siz2 Delta is restored by PIF1 deletion. By live-cell imaging of a critically short telomere, we show that telomeres shift a way 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.",
keywords = "SUMOYLATION, ENZYME, DOMAIN PROTEIN MPS3, NUCLEAR-PORE COMPLEX, DNA-REPAIR, S-PHASE, SUMO MODIFICATION, SACCHAROMYCES-CEREVISIAE, LENGTH, KU",
author = "Ferreira, {Helder Casimiro} and Brian Luke and Heiko Schober and Veronique Kalck and Joachim Lingner and Gasser, {Susan M.}",
year = "2011",
month = jul,
doi = "10.1038/ncb2263",
language = "English",
volume = "13",
pages = "867--874",
journal = "Nature Cell Biology",
issn = "1465-7392",
publisher = "Nature publishing group",
number = "7",

}

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TY - JOUR

T1 - The PIAS homologue Siz2 regulates perinuclear telomere position and telomerase activity in budding yeast

AU - Ferreira, Helder Casimiro

AU - Luke, Brian

AU - Schober, Heiko

AU - Kalck, Veronique

AU - Lingner, Joachim

AU - Gasser, Susan M.

PY - 2011/7

Y1 - 2011/7

N2 - 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(1,2). 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(3), normal telomere anchoring in siz2 Delta is restored by PIF1 deletion. By live-cell imaging of a critically short telomere, we show that telomeres shift a way 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.

AB - 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(1,2). 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(3), normal telomere anchoring in siz2 Delta is restored by PIF1 deletion. By live-cell imaging of a critically short telomere, we show that telomeres shift a way 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.

KW - SUMOYLATION

KW - ENZYME

KW - DOMAIN PROTEIN MPS3

KW - NUCLEAR-PORE COMPLEX

KW - DNA-REPAIR

KW - S-PHASE

KW - SUMO MODIFICATION

KW - SACCHAROMYCES-CEREVISIAE

KW - LENGTH

KW - KU

U2 - 10.1038/ncb2263

DO - 10.1038/ncb2263

M3 - Article

VL - 13

SP - 867

EP - 874

JO - Nature Cell Biology

JF - Nature Cell Biology

SN - 1465-7392

IS - 7

ER -

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