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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.
Cooperative Binding of Transcription Regulators02:13

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...
Translesion DNA Polymerases02:10

Translesion DNA Polymerases

Translesion (TLS) polymerases rescue stalled DNA polymerases at sites of damaged bases by replacing the replicative polymerase and installing a nucleotide across the damaged site. Doing so, TLS allows additional time for the cell to repair the damage before resuming regular DNA replication.
TLS polymerases are found in all three domains of life - archaea, bacteria, and eukaryotes. Of the different classes of TLS polymerases, members of the Y family are fitted with specialized structures that...
DNA as a Genetic Template02:05

DNA as a Genetic Template

Two structural features of the DNA molecule provide a basis for the mechanisms of heredity: the four nucleotide bases and its double-stranded nature. The Watson-Crick model of double-helical DNA structure, proposed in 1952, drew heavily upon the X-ray crystallography work of researchers Rosalind Franklin and Maurice Wilkins. Watson, Crick, and Wilkins jointly received the Nobel Prize in Physiology or Medicine for their work in 1962. Franklin was, controversially, excluded from the prize for...
Replication in Eukaryotes02:31

Replication in Eukaryotes

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Related Experiment Video

Updated: May 28, 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

RNA/DNA hybrid binding affinity determines telomerase template-translocation efficiency.

Xiaodong Qi1, Mingyi Xie, Andrew F Brown

  • 1Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287, USA.

The EMBO Journal
|October 13, 2011
PubMed
Summary

Telomerase uses its active site to bind RNA/DNA hybrids, a crucial step for DNA synthesis and template translocation. This binding occurs after template realignment outside the active site, ensuring processive telomere replication.

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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

Related Experiment Videos

Last Updated: May 28, 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

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:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Telomerase synthesizes telomeric DNA repeats using an intrinsic RNA template.
  • Telomere maintenance is vital for genomic stability and involves complex enzymatic mechanisms.
  • The precise mechanism of telomerase RNA template translocation remains poorly understood.

Purpose of the Study:

  • To elucidate the role of active site binding in telomerase-mediated template translocation.
  • To investigate the interaction between telomerase and RNA/DNA hybrid substrates during DNA polymerization.
  • To understand the processivity mechanism of telomerase.

Main Methods:

  • Utilized a template-free human telomerase system.
  • Investigated telomerase processivity mutants.
  • Assessed the impact of extrinsic RNA/DNA hybrids on telomerase activity.

Main Results:

  • Demonstrated direct binding of RNA/DNA hybrid substrates by the telomerase active site for DNA polymerization.
  • Showed a correlation between template-translocation efficiency and RNA/DNA hybrid substrate affinity in processivity mutants.
  • Found that the active site is unoccupied during template translocation, with extrinsic hybrids reducing processivity.

Conclusions:

  • Active site binding of the realigned RNA/DNA hybrid is essential for telomerase template translocation.
  • Strand separation and template realignment occur outside the active site.
  • Telomerase possesses an ancient RNA/DNA hybrid binding ability crucial for its processivity and function.