Identification of Protein Components of Yeast Telomerase
Abstract
Recent evidence suggests that Pif1p is a catalytic inhibitor of telomerase in Saccharomyces cerevisiae. Mean telomere length increases in strains with mutations of PIF1, and this is dependent on the RNA template, TLCl, of the telomerase reverse transcriptase. It is likely that Piflp acts as a helicase to inhibit telomerase, as point mutations that knock out helicase activity in vitro lead to increased telomere length in vivo. The effect of Pif1p on telomerase is most likely direct, as Piflp is associated with telomeric chromatin in vivo. Here I use chromatin immunoprecipitation (ChIP) to show that the catalytic subunit of telomerase, Est2p, is also telomere-associated in vivo. Telomere association appears to he constitutive in the cell cycle, although the intensity of the ChIP signal varies. I plan to ask how this pattern of Est2p telomere association is altered in PIFi mutant backgrounds.
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 01, 2001
- Accession Number
- ADA391249
Entities
People
- Andrew K. Taggart
- Shu-chun Teng
Organizations
- Princeton University