Journal
EMBO JOURNAL
Volume 27, Issue 17, Pages 2328-2339Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/emboj.2008.158
Keywords
CST complex; Stn1; telomerase; telomere capping; telomere length regulation
Categories
Funding
- Swiss National Science Foundation
- Swiss Cancer League (OncoSuisse)
- Canton of Geneva
- 'Fondation Recherche Medicale' ( Paris, France)
Ask authors/readers for more resources
The budding yeast Cdc13, Stn1 and Ten1 (CST) proteins are proposed to function as an RPA-like complex at telomeres that protects ('caps') chromosome ends and regulates their elongation by telomerase. We show that Stn1 has a critical function in both processes through the deployment of two separable domains. The N terminus of Stn1 interacts with Ten1 and carries out its essential capping function. The C terminus of Stn1 binds both Cdc13 and Pol12, and we present genetic data indicating that the Stn1-Cdc13 interaction is required to limit continuous telomerase action. Stn1 telomere association, similar to that of Cdc13, peaks during S phase. Significantly, the magnitude of Stn1 telomere binding is independent of telomere TG tract length, suggesting that the negative effect of Stn1 on telomerase action might be regulated by a modification of CST activity or structure in cis at individual telomeres. Genetic analysis suggests that the Tel1 kinase exerts an effect in parallel with the Stn1 C terminus to counteract its inhibition of telomerase. These data provide new insights into the coordination of telomere capping and telomerase regulation.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available