Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Related Experiment Videos

A human telomerase-associated nuclease.

Rena Oulton¹, Lea Harrington

¹Department of Medical Biophysics, Ontario Cancer Institute/Advanced Medical Discovery Institute, University of Toronto, Toronto, Ontario M5G 2C1, Canada.

Molecular Biology of the Cell

|May 4, 2004

Summary

Human telomerase exhibits a novel nucleolytic activity, removing non-telomeric DNA from primer 3' ends. This conserved function aids in enzyme proofreading and processivity during DNA extension.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

A Chemical-Genetic Interaction Matrix Reveals Drug Mechanism and Genetic Architecture.

bioRxiv : the preprint server for biology·2026

Same author

Foundations and Strategic Vision of the Canadian Translational Geroscience Network.

The journals of gerontology. Series A, Biological sciences and medical sciences·2025

Same author

No correlative evidence of costs of infection or immunity on leucocyte telomere length in a wild population of Soay sheep.

Proceedings. Biological sciences·2024

Same author

Navigating the Landscape of Translational Geroscience in Canada: A Comprehensive Evaluation of Current Progress and Future Directions.

The journals of gerontology. Series A, Biological sciences and medical sciences·2024

Same author

A CRISPR base editing approach for the functional assessment of telomere biology disorder-related genes in human health and aging.

Biogerontology·2024

Same author

Aberrant expression and localization of the RAP1 shelterin protein contribute to age-related phenotypes.

PLoS genetics·2022

Area of Science:

Molecular Biology
Biochemistry
Genetics

Background:

Telomerase, a ribonucleoprotein enzyme, maintains telomere length by synthesizing DNA.
Ciliate and yeast telomerases possess nucleolytic activity for proofreading and processivity.
The existence and function of similar nucleolytic activity in human telomerase remain largely uncharacterized.

Purpose of the Study:

To investigate a previously uncharacterized nuclease activity associated with human telomerase.
To determine if this activity shares properties with known ciliate and yeast telomerase nucleases.
To explore the functional implications of this nucleolytic activity in human telomere maintenance.

Main Methods:

Utilized partially purified human telomerase from cell extracts and recombinant sources.
Assessed nuclease activity using single-stranded oligonucleotide substrates with varying DNA sequences.
Analyzed the influence of sequence context and chemical modifications at the DNA boundary on cleavage/extension.

Main Results:

Human telomerase demonstrated an ability to remove 3' nontelomeric nucleotides from a substrate with 5' telomeric DNA.
This cleavage was followed by the extension of the newly exposed telomeric sequence.
The cleavage/extension activity was sequence-dependent and affected by modifications at the DNA boundary.

Conclusions:

Human telomerase possesses an evolutionarily conserved nucleolytic activity, similar to yeast and ciliate counterparts.
This nuclease activity likely contributes to telomerase proofreading and/or processivity.
Telomerase-substrate interactions may occur at sites distal to the 3' primer end, influencing telomere maintenance.

Related Experiment Videos