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Related Concept Videos

Telomeres and Telomerase02:41

Telomeres and Telomerase

In eukaryotic DNA replication, a single-stranded DNA fragment remains at the end of a chromosome after the removal of the final primer. This section of DNA cannot be replicated in the same manner as the rest of the strand because there is no 3’ end to which the newly synthesized DNA can attach. This non-replicated fragment results in gradual loss of the chromosomal DNA during each cell duplication. Additionally, it can induce a DNA damage response by enzymes that recognize single-stranded DNA.
Telomeres and Telomerase02:41

Telomeres and Telomerase

In eukaryotic DNA replication, a single-stranded DNA fragment remains at the end of a chromosome after the removal of the final primer. This section of DNA cannot be replicated in the same manner as the rest of the strand because there is no 3’ end to which the newly synthesized DNA can attach. This non-replicated fragment results in gradual loss of the chromosomal DNA during each cell duplication. Additionally, it can induce a DNA damage response by enzymes that recognize single-stranded DNA.

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Related Experiment Video

Updated: Jun 18, 2026

Analyzing Telomeric Protein-DNA Interactions Using Single-Molecule Magnetic Tweezers
11:21

Analyzing Telomeric Protein-DNA Interactions Using Single-Molecule Magnetic Tweezers

Published on: August 30, 2024

A single-molecule assay for telomerase structure-function analysis.

John Y Wu1, Michael D Stone, Xiaowei Zhuang

  • 1Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.

Nucleic Acids Research
|November 19, 2009
PubMed
Summary
This summary is machine-generated.

Researchers developed a new single-molecule assay to analyze telomerase structure and activity. This method reveals an active telomerase conformation, advancing genome stability research.

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Semi-quantitative Detection of RNA-dependent RNA Polymerase Activity of Human Telomerase Reverse Transcriptase Protein

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Related Experiment Videos

Last Updated: Jun 18, 2026

Analyzing Telomeric Protein-DNA Interactions Using Single-Molecule Magnetic Tweezers
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Published on: August 30, 2024

Telomere Length and Telomerase Activity; A Yin and Yang of Cell Senescence
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Semi-quantitative Detection of RNA-dependent RNA Polymerase Activity of Human Telomerase Reverse Transcriptase Protein
08:26

Semi-quantitative Detection of RNA-dependent RNA Polymerase Activity of Human Telomerase Reverse Transcriptase Protein

Published on: June 12, 2018

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Telomerase ribonucleoprotein enzyme activity is crucial for genome stability and cell development.
  • Detailed structural models of active telomerase are lacking despite its biomedical importance.

Purpose of the Study:

  • To develop a single-molecule assay for direct structural analysis of catalytically active telomerase.
  • To characterize the structural organization of telomerase RNA within active holoenzymes.

Main Methods:

  • A novel single-molecule assay utilizing oligonucleotide hybridization.
  • Probing primer-extension activity with single nucleotide sensitivity.
  • Employing Förster Resonance Energy Transfer (FRET) signals to analyze enzyme conformation.

Main Results:

  • The assay precisely discriminates between inactive, active, and processive telomerase binding events.
  • Identified an active conformation of telomerase within a heterogeneous enzyme population.
  • Determined the global organization of telomerase RNA in catalytically active holoenzymes.

Conclusions:

  • The developed assay enables direct structural analysis of individual, active telomerase enzymes.
  • An active telomerase conformation has been identified, providing new structural insights.
  • This work contributes to understanding genome stability mechanisms at a molecular level.