Unknown

Dataset Information

0

Tpz1TPP1 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 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.

SUBMITTER: Garg M 

PROVIDER: S-EPMC4197044 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

Tpz1TPP1 SUMOylation reveals evolutionary conservation of SUMO-dependent Stn1 telomere association.

Garg Mansi M   Gurung Resham L RL   Mansoubi Sahar S   Ahmed Jubed O JO   Davé Anoushka A   Watts Felicity Z FZ   Bianchi Alessandro A  

EMBO reports 20140612 8


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  ...[more]

Similar Datasets

| S-EPMC4000806 | biostudies-other
| S-SCDT-10_1038-S44319-023-00010-8 | biostudies-other
| S-EPMC5773548 | biostudies-literature
| S-EPMC145504 | biostudies-literature
| S-EPMC10897377 | biostudies-literature
| S-EPMC4643655 | biostudies-literature
| S-EPMC3334497 | biostudies-literature
| S-EPMC6053418 | biostudies-literature
| S-EPMC2529371 | biostudies-literature
| S-EPMC4086084 | biostudies-literature