$ Tpz1^{TPP} $1 SUMOylation reveals evolutionary conservation of SUMO‐dependent Stn1 telomere association
Abstract Elongation of the telomeric overhang by telomerase is counteracted by synthesis of the complementary strand by the CST complex, CTC1(Cdc13)/Stn1/Ten1. Interaction of budding yeast Stn1 with overhang‐binding Cdc13 is increased by Cdc13 SUMOylation. Human and fission yeast CST instead interac...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Garg, Mansi [verfasserIn] Gurung, Resham L [verfasserIn] Mansoubi, Sahar [verfasserIn] Ahmed, Jubed O [verfasserIn] Davé, Anoushka [verfasserIn] Watts, Felicity Z [verfasserIn] Bianchi, Alessandro [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2014 |
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| Schlagwörter: |
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| Anmerkung: |
© The Authors. Published under the terms of the CC BY 4.0 License 2014 |
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| Übergeordnetes Werk: |
Enthalten in: EMBO Reports - Nature Publishing Group UK, 2023, 15(2014), 8 vom: 12. Juni, Seite 871-877 |
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| Übergeordnetes Werk: |
volume:15 ; year:2014 ; number:8 ; day:12 ; month:06 ; pages:871-877 |
| Links: |
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| DOI / URN: |
10.15252/embr.201438919 |
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| Katalog-ID: |
SPR057903220 |
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| 100 | 1 | |a Garg, Mansi |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a $ Tpz1^{TPP} $1 SUMOylation reveals evolutionary conservation of SUMO‐dependent Stn1 telomere association |
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| 520 | |a Abstract Elongation of the telomeric overhang by telomerase is counteracted by synthesis of the complementary strand by the CST complex, CTC1(Cdc13)/Stn1/Ten1. Interaction of budding yeast Stn1 with overhang‐binding Cdc13 is increased by Cdc13 SUMOylation. Human and fission yeast CST instead interact with overhang‐binding TPP1/POT1. We show that the fission yeast TPP1 ortholog, Tpz1, is SUMOylated. Tpz1 SUMOylation restricts telomere elongation and promotes Stn1/Ten1 telomere association, and a SUMO‐Tpz1 fusion protein has increased affinity for Stn1. Our data suggest that SUMO inhibits telomerase through stimulation of Stn1/Ten1 action by Tpz1, highlighting the evolutionary conservation of the regulation of CST function by SUMOylation. | ||
| 520 | |a Synopsis This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. Tpz1 SUMOylation increases its affinity for Stn1. Fission yeast telomere protein Tpz1, the TPP1 ortholog, is SUMOylated at lysine 242.Tpz1 SUMOylation limits telomere elongation and the association of telomerase with telomeres.As SUMOylation of budding yeast Cdc13, Tpz1 SUMOylation is required for efficient recruitment of Stn1/Ten1 to telomeres.SUMO‐mediated recruitment of Stn1 is proposed to be a conserved feature within the CST complex. | ||
| 520 | |a Graphical Abstract This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. Tpz1 SUMOylation increases its affinity for Stn1. | ||
| 650 | 4 | |a CST |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Stn1 |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a telomeres |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a Tpz1 |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a SUMO |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Gurung, Resham L |e verfasserin |4 aut | |
| 700 | 1 | |a Mansoubi, Sahar |e verfasserin |4 aut | |
| 700 | 1 | |a Ahmed, Jubed O |e verfasserin |4 aut | |
| 700 | 1 | |a Davé, Anoushka |e verfasserin |4 aut | |
| 700 | 1 | |a Watts, Felicity Z |e verfasserin |4 aut | |
| 700 | 1 | |a Bianchi, Alessandro |e verfasserin |4 aut | |
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10.15252/embr.201438919 doi (DE-627)SPR057903220 (SPR)embr.201438919-e DE-627 ger DE-627 rakwb eng Garg, Mansi verfasserin aut $ Tpz1^{TPP} $1 SUMOylation reveals evolutionary conservation of SUMO‐dependent Stn1 telomere association 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Authors. Published under the terms of the CC BY 4.0 License 2014 Abstract Elongation of the telomeric overhang by telomerase is counteracted by synthesis of the complementary strand by the CST complex, CTC1(Cdc13)/Stn1/Ten1. Interaction of budding yeast Stn1 with overhang‐binding Cdc13 is increased by Cdc13 SUMOylation. Human and fission yeast CST instead interact with overhang‐binding TPP1/POT1. We show that the fission yeast TPP1 ortholog, Tpz1, is SUMOylated. Tpz1 SUMOylation restricts telomere elongation and promotes Stn1/Ten1 telomere association, and a SUMO‐Tpz1 fusion protein has increased affinity for Stn1. Our data suggest that SUMO inhibits telomerase through stimulation of Stn1/Ten1 action by Tpz1, highlighting the evolutionary conservation of the regulation of CST function by SUMOylation. Synopsis This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. Tpz1 SUMOylation increases its affinity for Stn1. Fission yeast telomere protein Tpz1, the TPP1 ortholog, is SUMOylated at lysine 242.Tpz1 SUMOylation limits telomere elongation and the association of telomerase with telomeres.As SUMOylation of budding yeast Cdc13, Tpz1 SUMOylation is required for efficient recruitment of Stn1/Ten1 to telomeres.SUMO‐mediated recruitment of Stn1 is proposed to be a conserved feature within the CST complex. Graphical Abstract This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. Tpz1 SUMOylation increases its affinity for Stn1. CST (dpeaa)DE-He213 Stn1 (dpeaa)DE-He213 telomeres (dpeaa)DE-He213 Tpz1 (dpeaa)DE-He213 SUMO (dpeaa)DE-He213 Gurung, Resham L verfasserin aut Mansoubi, Sahar verfasserin aut Ahmed, Jubed O verfasserin aut Davé, Anoushka verfasserin aut Watts, Felicity Z verfasserin aut Bianchi, Alessandro verfasserin aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 15(2014), 8 vom: 12. Juni, Seite 871-877 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:15 year:2014 number:8 day:12 month:06 pages:871-877 https://dx.doi.org/10.15252/embr.201438919 X:SPRINGER Resolving-System kostenfrei Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 15 2014 8 12 06 871-877 |
| spelling |
10.15252/embr.201438919 doi (DE-627)SPR057903220 (SPR)embr.201438919-e DE-627 ger DE-627 rakwb eng Garg, Mansi verfasserin aut $ Tpz1^{TPP} $1 SUMOylation reveals evolutionary conservation of SUMO‐dependent Stn1 telomere association 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Authors. Published under the terms of the CC BY 4.0 License 2014 Abstract Elongation of the telomeric overhang by telomerase is counteracted by synthesis of the complementary strand by the CST complex, CTC1(Cdc13)/Stn1/Ten1. Interaction of budding yeast Stn1 with overhang‐binding Cdc13 is increased by Cdc13 SUMOylation. Human and fission yeast CST instead interact with overhang‐binding TPP1/POT1. We show that the fission yeast TPP1 ortholog, Tpz1, is SUMOylated. Tpz1 SUMOylation restricts telomere elongation and promotes Stn1/Ten1 telomere association, and a SUMO‐Tpz1 fusion protein has increased affinity for Stn1. Our data suggest that SUMO inhibits telomerase through stimulation of Stn1/Ten1 action by Tpz1, highlighting the evolutionary conservation of the regulation of CST function by SUMOylation. Synopsis This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. Tpz1 SUMOylation increases its affinity for Stn1. Fission yeast telomere protein Tpz1, the TPP1 ortholog, is SUMOylated at lysine 242.Tpz1 SUMOylation limits telomere elongation and the association of telomerase with telomeres.As SUMOylation of budding yeast Cdc13, Tpz1 SUMOylation is required for efficient recruitment of Stn1/Ten1 to telomeres.SUMO‐mediated recruitment of Stn1 is proposed to be a conserved feature within the CST complex. Graphical Abstract This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. Tpz1 SUMOylation increases its affinity for Stn1. CST (dpeaa)DE-He213 Stn1 (dpeaa)DE-He213 telomeres (dpeaa)DE-He213 Tpz1 (dpeaa)DE-He213 SUMO (dpeaa)DE-He213 Gurung, Resham L verfasserin aut Mansoubi, Sahar verfasserin aut Ahmed, Jubed O verfasserin aut Davé, Anoushka verfasserin aut Watts, Felicity Z verfasserin aut Bianchi, Alessandro verfasserin aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 15(2014), 8 vom: 12. Juni, Seite 871-877 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:15 year:2014 number:8 day:12 month:06 pages:871-877 https://dx.doi.org/10.15252/embr.201438919 X:SPRINGER Resolving-System kostenfrei Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 15 2014 8 12 06 871-877 |
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10.15252/embr.201438919 doi (DE-627)SPR057903220 (SPR)embr.201438919-e DE-627 ger DE-627 rakwb eng Garg, Mansi verfasserin aut $ Tpz1^{TPP} $1 SUMOylation reveals evolutionary conservation of SUMO‐dependent Stn1 telomere association 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Authors. Published under the terms of the CC BY 4.0 License 2014 Abstract Elongation of the telomeric overhang by telomerase is counteracted by synthesis of the complementary strand by the CST complex, CTC1(Cdc13)/Stn1/Ten1. Interaction of budding yeast Stn1 with overhang‐binding Cdc13 is increased by Cdc13 SUMOylation. Human and fission yeast CST instead interact with overhang‐binding TPP1/POT1. We show that the fission yeast TPP1 ortholog, Tpz1, is SUMOylated. Tpz1 SUMOylation restricts telomere elongation and promotes Stn1/Ten1 telomere association, and a SUMO‐Tpz1 fusion protein has increased affinity for Stn1. Our data suggest that SUMO inhibits telomerase through stimulation of Stn1/Ten1 action by Tpz1, highlighting the evolutionary conservation of the regulation of CST function by SUMOylation. Synopsis This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. Tpz1 SUMOylation increases its affinity for Stn1. Fission yeast telomere protein Tpz1, the TPP1 ortholog, is SUMOylated at lysine 242.Tpz1 SUMOylation limits telomere elongation and the association of telomerase with telomeres.As SUMOylation of budding yeast Cdc13, Tpz1 SUMOylation is required for efficient recruitment of Stn1/Ten1 to telomeres.SUMO‐mediated recruitment of Stn1 is proposed to be a conserved feature within the CST complex. Graphical Abstract This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. Tpz1 SUMOylation increases its affinity for Stn1. CST (dpeaa)DE-He213 Stn1 (dpeaa)DE-He213 telomeres (dpeaa)DE-He213 Tpz1 (dpeaa)DE-He213 SUMO (dpeaa)DE-He213 Gurung, Resham L verfasserin aut Mansoubi, Sahar verfasserin aut Ahmed, Jubed O verfasserin aut Davé, Anoushka verfasserin aut Watts, Felicity Z verfasserin aut Bianchi, Alessandro verfasserin aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 15(2014), 8 vom: 12. Juni, Seite 871-877 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:15 year:2014 number:8 day:12 month:06 pages:871-877 https://dx.doi.org/10.15252/embr.201438919 X:SPRINGER Resolving-System kostenfrei Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 15 2014 8 12 06 871-877 |
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10.15252/embr.201438919 doi (DE-627)SPR057903220 (SPR)embr.201438919-e DE-627 ger DE-627 rakwb eng Garg, Mansi verfasserin aut $ Tpz1^{TPP} $1 SUMOylation reveals evolutionary conservation of SUMO‐dependent Stn1 telomere association 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Authors. Published under the terms of the CC BY 4.0 License 2014 Abstract Elongation of the telomeric overhang by telomerase is counteracted by synthesis of the complementary strand by the CST complex, CTC1(Cdc13)/Stn1/Ten1. Interaction of budding yeast Stn1 with overhang‐binding Cdc13 is increased by Cdc13 SUMOylation. Human and fission yeast CST instead interact with overhang‐binding TPP1/POT1. We show that the fission yeast TPP1 ortholog, Tpz1, is SUMOylated. Tpz1 SUMOylation restricts telomere elongation and promotes Stn1/Ten1 telomere association, and a SUMO‐Tpz1 fusion protein has increased affinity for Stn1. Our data suggest that SUMO inhibits telomerase through stimulation of Stn1/Ten1 action by Tpz1, highlighting the evolutionary conservation of the regulation of CST function by SUMOylation. Synopsis This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. Tpz1 SUMOylation increases its affinity for Stn1. Fission yeast telomere protein Tpz1, the TPP1 ortholog, is SUMOylated at lysine 242.Tpz1 SUMOylation limits telomere elongation and the association of telomerase with telomeres.As SUMOylation of budding yeast Cdc13, Tpz1 SUMOylation is required for efficient recruitment of Stn1/Ten1 to telomeres.SUMO‐mediated recruitment of Stn1 is proposed to be a conserved feature within the CST complex. Graphical Abstract This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. Tpz1 SUMOylation increases its affinity for Stn1. CST (dpeaa)DE-He213 Stn1 (dpeaa)DE-He213 telomeres (dpeaa)DE-He213 Tpz1 (dpeaa)DE-He213 SUMO (dpeaa)DE-He213 Gurung, Resham L verfasserin aut Mansoubi, Sahar verfasserin aut Ahmed, Jubed O verfasserin aut Davé, Anoushka verfasserin aut Watts, Felicity Z verfasserin aut Bianchi, Alessandro verfasserin aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 15(2014), 8 vom: 12. Juni, Seite 871-877 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:15 year:2014 number:8 day:12 month:06 pages:871-877 https://dx.doi.org/10.15252/embr.201438919 X:SPRINGER Resolving-System kostenfrei Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 15 2014 8 12 06 871-877 |
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10.15252/embr.201438919 doi (DE-627)SPR057903220 (SPR)embr.201438919-e DE-627 ger DE-627 rakwb eng Garg, Mansi verfasserin aut $ Tpz1^{TPP} $1 SUMOylation reveals evolutionary conservation of SUMO‐dependent Stn1 telomere association 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Authors. Published under the terms of the CC BY 4.0 License 2014 Abstract Elongation of the telomeric overhang by telomerase is counteracted by synthesis of the complementary strand by the CST complex, CTC1(Cdc13)/Stn1/Ten1. Interaction of budding yeast Stn1 with overhang‐binding Cdc13 is increased by Cdc13 SUMOylation. Human and fission yeast CST instead interact with overhang‐binding TPP1/POT1. We show that the fission yeast TPP1 ortholog, Tpz1, is SUMOylated. Tpz1 SUMOylation restricts telomere elongation and promotes Stn1/Ten1 telomere association, and a SUMO‐Tpz1 fusion protein has increased affinity for Stn1. Our data suggest that SUMO inhibits telomerase through stimulation of Stn1/Ten1 action by Tpz1, highlighting the evolutionary conservation of the regulation of CST function by SUMOylation. Synopsis This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. Tpz1 SUMOylation increases its affinity for Stn1. Fission yeast telomere protein Tpz1, the TPP1 ortholog, is SUMOylated at lysine 242.Tpz1 SUMOylation limits telomere elongation and the association of telomerase with telomeres.As SUMOylation of budding yeast Cdc13, Tpz1 SUMOylation is required for efficient recruitment of Stn1/Ten1 to telomeres.SUMO‐mediated recruitment of Stn1 is proposed to be a conserved feature within the CST complex. Graphical Abstract This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. Tpz1 SUMOylation increases its affinity for Stn1. CST (dpeaa)DE-He213 Stn1 (dpeaa)DE-He213 telomeres (dpeaa)DE-He213 Tpz1 (dpeaa)DE-He213 SUMO (dpeaa)DE-He213 Gurung, Resham L verfasserin aut Mansoubi, Sahar verfasserin aut Ahmed, Jubed O verfasserin aut Davé, Anoushka verfasserin aut Watts, Felicity Z verfasserin aut Bianchi, Alessandro verfasserin aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 15(2014), 8 vom: 12. Juni, Seite 871-877 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:15 year:2014 number:8 day:12 month:06 pages:871-877 https://dx.doi.org/10.15252/embr.201438919 X:SPRINGER Resolving-System kostenfrei Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 15 2014 8 12 06 871-877 |
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Enthalten in EMBO Reports 15(2014), 8 vom: 12. Juni, Seite 871-877 volume:15 year:2014 number:8 day:12 month:06 pages:871-877 |
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Enthalten in EMBO Reports 15(2014), 8 vom: 12. Juni, Seite 871-877 volume:15 year:2014 number:8 day:12 month:06 pages:871-877 |
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Garg, Mansi @@aut@@ Gurung, Resham L @@aut@@ Mansoubi, Sahar @@aut@@ Ahmed, Jubed O @@aut@@ Davé, Anoushka @@aut@@ Watts, Felicity Z @@aut@@ Bianchi, Alessandro @@aut@@ |
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Published under the terms of the CC BY 4.0 License 2014</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Elongation of the telomeric overhang by telomerase is counteracted by synthesis of the complementary strand by the CST complex, CTC1(Cdc13)/Stn1/Ten1. Interaction of budding yeast Stn1 with overhang‐binding Cdc13 is increased by Cdc13 SUMOylation. Human and fission yeast CST instead interact with overhang‐binding TPP1/POT1. We show that the fission yeast TPP1 ortholog, Tpz1, is SUMOylated. Tpz1 SUMOylation restricts telomere elongation and promotes Stn1/Ten1 telomere association, and a SUMO‐Tpz1 fusion protein has increased affinity for Stn1. Our data suggest that SUMO inhibits telomerase through stimulation of Stn1/Ten1 action by Tpz1, highlighting the evolutionary conservation of the regulation of CST function by SUMOylation.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Synopsis This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. Tpz1 SUMOylation increases its affinity for Stn1. Fission yeast telomere protein Tpz1, the TPP1 ortholog, is SUMOylated at lysine 242.Tpz1 SUMOylation limits telomere elongation and the association of telomerase with telomeres.As SUMOylation of budding yeast Cdc13, Tpz1 SUMOylation is required for efficient recruitment of Stn1/Ten1 to telomeres.SUMO‐mediated recruitment of Stn1 is proposed to be a conserved feature within the CST complex.</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Graphical Abstract This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. 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Garg, Mansi |
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Garg, Mansi misc CST misc Stn1 misc telomeres misc Tpz1 misc SUMO $ Tpz1^{TPP} $1 SUMOylation reveals evolutionary conservation of SUMO‐dependent Stn1 telomere association |
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$ Tpz1^{TPP} $1 SUMOylation reveals evolutionary conservation of SUMO‐dependent Stn1 telomere association CST (dpeaa)DE-He213 Stn1 (dpeaa)DE-He213 telomeres (dpeaa)DE-He213 Tpz1 (dpeaa)DE-He213 SUMO (dpeaa)DE-He213 |
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$ Tpz1^{TPP} $1 SUMOylation reveals evolutionary conservation of SUMO‐dependent Stn1 telomere association |
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$ Tpz1^{TPP} $1 SUMOylation reveals evolutionary conservation of SUMO‐dependent Stn1 telomere association |
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Garg, Mansi Gurung, Resham L Mansoubi, Sahar Ahmed, Jubed O Davé, Anoushka Watts, Felicity Z Bianchi, Alessandro |
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$ tpz1^{tpp} $1 sumoylation reveals evolutionary conservation of sumo‐dependent stn1 telomere association |
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$ Tpz1^{TPP} $1 SUMOylation reveals evolutionary conservation of SUMO‐dependent Stn1 telomere association |
| abstract |
Abstract Elongation of the telomeric overhang by telomerase is counteracted by synthesis of the complementary strand by the CST complex, CTC1(Cdc13)/Stn1/Ten1. Interaction of budding yeast Stn1 with overhang‐binding Cdc13 is increased by Cdc13 SUMOylation. Human and fission yeast CST instead interact with overhang‐binding TPP1/POT1. We show that the fission yeast TPP1 ortholog, Tpz1, is SUMOylated. Tpz1 SUMOylation restricts telomere elongation and promotes Stn1/Ten1 telomere association, and a SUMO‐Tpz1 fusion protein has increased affinity for Stn1. Our data suggest that SUMO inhibits telomerase through stimulation of Stn1/Ten1 action by Tpz1, highlighting the evolutionary conservation of the regulation of CST function by SUMOylation. Synopsis This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. Tpz1 SUMOylation increases its affinity for Stn1. Fission yeast telomere protein Tpz1, the TPP1 ortholog, is SUMOylated at lysine 242.Tpz1 SUMOylation limits telomere elongation and the association of telomerase with telomeres.As SUMOylation of budding yeast Cdc13, Tpz1 SUMOylation is required for efficient recruitment of Stn1/Ten1 to telomeres.SUMO‐mediated recruitment of Stn1 is proposed to be a conserved feature within the CST complex. Graphical Abstract This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. Tpz1 SUMOylation increases its affinity for Stn1. © The Authors. Published under the terms of the CC BY 4.0 License 2014 |
| abstractGer |
Abstract Elongation of the telomeric overhang by telomerase is counteracted by synthesis of the complementary strand by the CST complex, CTC1(Cdc13)/Stn1/Ten1. Interaction of budding yeast Stn1 with overhang‐binding Cdc13 is increased by Cdc13 SUMOylation. Human and fission yeast CST instead interact with overhang‐binding TPP1/POT1. We show that the fission yeast TPP1 ortholog, Tpz1, is SUMOylated. Tpz1 SUMOylation restricts telomere elongation and promotes Stn1/Ten1 telomere association, and a SUMO‐Tpz1 fusion protein has increased affinity for Stn1. Our data suggest that SUMO inhibits telomerase through stimulation of Stn1/Ten1 action by Tpz1, highlighting the evolutionary conservation of the regulation of CST function by SUMOylation. Synopsis This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. Tpz1 SUMOylation increases its affinity for Stn1. Fission yeast telomere protein Tpz1, the TPP1 ortholog, is SUMOylated at lysine 242.Tpz1 SUMOylation limits telomere elongation and the association of telomerase with telomeres.As SUMOylation of budding yeast Cdc13, Tpz1 SUMOylation is required for efficient recruitment of Stn1/Ten1 to telomeres.SUMO‐mediated recruitment of Stn1 is proposed to be a conserved feature within the CST complex. Graphical Abstract This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. Tpz1 SUMOylation increases its affinity for Stn1. © The Authors. Published under the terms of the CC BY 4.0 License 2014 |
| abstract_unstemmed |
Abstract Elongation of the telomeric overhang by telomerase is counteracted by synthesis of the complementary strand by the CST complex, CTC1(Cdc13)/Stn1/Ten1. Interaction of budding yeast Stn1 with overhang‐binding Cdc13 is increased by Cdc13 SUMOylation. Human and fission yeast CST instead interact with overhang‐binding TPP1/POT1. We show that the fission yeast TPP1 ortholog, Tpz1, is SUMOylated. Tpz1 SUMOylation restricts telomere elongation and promotes Stn1/Ten1 telomere association, and a SUMO‐Tpz1 fusion protein has increased affinity for Stn1. Our data suggest that SUMO inhibits telomerase through stimulation of Stn1/Ten1 action by Tpz1, highlighting the evolutionary conservation of the regulation of CST function by SUMOylation. Synopsis This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. Tpz1 SUMOylation increases its affinity for Stn1. Fission yeast telomere protein Tpz1, the TPP1 ortholog, is SUMOylated at lysine 242.Tpz1 SUMOylation limits telomere elongation and the association of telomerase with telomeres.As SUMOylation of budding yeast Cdc13, Tpz1 SUMOylation is required for efficient recruitment of Stn1/Ten1 to telomeres.SUMO‐mediated recruitment of Stn1 is proposed to be a conserved feature within the CST complex. Graphical Abstract This study shows that Tpz1 SUMOylation in fission yeast is required for Stn1/Ten1 recruitment to telomeres and, thus, prevention of telomere elongation. Tpz1 SUMOylation increases its affinity for Stn1. © The Authors. Published under the terms of the CC BY 4.0 License 2014 |
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$ Tpz1^{TPP} $1 SUMOylation reveals evolutionary conservation of SUMO‐dependent Stn1 telomere association |
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https://dx.doi.org/10.15252/embr.201438919 |
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Gurung, Resham L Mansoubi, Sahar Ahmed, Jubed O Davé, Anoushka Watts, Felicity Z Bianchi, Alessandro |
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10.15252/embr.201438919 |
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2024-10-19T04:52:23.264Z |
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|
| score |
7.3997 |