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Journal ArticleDOI

Est1 and Cdc13 as comediators of telomerase access.

Sara K. Evans, +1 more
- 01 Oct 1999 - 
- Vol. 286, Iss: 5437, pp 117-120
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TLDR
Fusion proteins consisting of mutant versions of Cdc13 or Est1 confer similar telomere elongation, indicating that close physical proximity can bypass telomerase-defective mutations in either protein.
Abstract
Cdc13 and Est1 are single-strand telomeric DNA binding proteins that contribute to telomere replication in the yeast Saccharomyces cerevisiae. Here it is shown that fusion of Cdc13 to the telomerase-associated Est1 protein results in greatly elongated telomeres. Fusion proteins consisting of mutant versions of Cdc13 or Est1 confer similar telomere elongation, indicating that close physical proximity can bypass telomerase-defective mutations in either protein. Fusing Cdc13 directly to the catalytic core of telomerase allows stable telomere maintenance in the absence of Est1, consistent with a role for Est1 in mediating telomerase access. Telomere length homeostasis therefore is maintained in part by restricting access of telomerase to chromosome termini, but this limiting situation can be overcome by directly tethering telomerase to the telomere.

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Citations
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Journal ArticleDOI

Telomere states and cell fates

TL;DR: Recent findings are integrated into a new, probabilistic view of the telomere to explain how and when it can signal not only its own fate but also that of a cell.
Journal ArticleDOI

X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution.

TL;DR: In this article, a review of the use of small angle X-ray scattering (SAXS) for modeling macromolecular folding, unfolding, aggregation, extended conformations, flexibly linked domains, shape, conformation, and assembly state in solution, albeit at the lower resolution range of about 50 A to 10 A resolution, is presented.
Journal ArticleDOI

Pot1, the Putative Telomere End-Binding Protein in Fission Yeast and Humans

TL;DR: It now appears that the protein that caps the ends of chromosomes is widely dispersed throughout the eukaryotic kingdom.
Journal ArticleDOI

Human Telomerase and Its Regulation

TL;DR: The currently known components of the telomerase complex are described and an update is provided on the molecular mechanisms of human telomere regulation to provide an update in antiaging and anticancer therapy.
Journal ArticleDOI

Regulation of Telomerase by Telomeric Proteins

TL;DR: The details of telomerase and its regulation by the telomere are discussed, including single-stranded DNA-binding proteins (POT1 in humans and Cdc13 in budding yeast), which have been proposed to contribute to the recruitment of telomersase and may also regulate the extent or frequency of elongation.
References
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Journal ArticleDOI

Reverse Transcriptase Motifs in the Catalytic Subunit of Telomerase

TL;DR: The reverse transcriptase protein fold, previously known to be involved in retroviral replication and retrotransposition, is essential for normal chromosome telomere replication in diverse eukaryotes.
Journal ArticleDOI

Control of telomere length by the human telomeric protein TRF1.

TL;DR: It is proposed that the binding of TRF1 controls telomere length in cis by inhibiting the action of telomerase at the ends of individual telomeres, and shown that the human telomeric-repeat binding factor TRF 1 is involved in this regulation.
Journal ArticleDOI

An alternative pathway for yeast telomere maintenance rescues est1− senescence

TL;DR: It is shown that a minor subpopulation of est1- survivors arise as a result of the amplification and acquisition of subtelomeric elements (and their deletion derivatives) by a large number of telomeres, indicating that even when the primary pathway for telomere replication is defective, an alternative backup pathway can restore telomerre function and keep the cell alive.
Journal ArticleDOI

A mutant with a defect in telomere elongation leads to senescence in yeast.

TL;DR: Using this assay, a mutant that displays a progressive decrease in telomere length as well as an increased frequency of chromosome loss is isolated, which defines a new gene, designated EST1 (for ever shorter telomeres).
Journal ArticleDOI

TLC1: Template RNA component of Saccharomyces cerevisiae telomerase

TL;DR: The discovery of TLC1 confirms the existence of telomerase in S. cerevisiae and may facilitate both the analysis of this enzyme and an understanding of telomere structure and function.
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