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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.
Replication in Eukaryotes01:29

Replication in Eukaryotes

In eukaryotic cells, DNA replication is highly conserved and tightly regulated. Multiple linear chromosomes must be duplicated with high fidelity before cell division, so there are many proteins that fulfill specialized roles in the replication process. Replication occurs in three phases: initiation, elongation, and termination, and ends with two complete sets of chromosomes in the nucleus.
Many Proteins Orchestrate Replication at the Origin
Eukaryotic replication follows many of the same...
Replication in Eukaryotes02:31

Replication in Eukaryotes

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Replicative Cell Senescence02:15

Replicative Cell Senescence

Replicative cell senescence is a property of cells that allows them to divide a finite number of times throughout the organism's lifespan while preventing excessive proliferation. Replicative senescence is associated with the gradual loss of the telomere — short, repetitive DNA sequences found at the end of the chromosomes. Telomeres are bound by a group of proteins to form a protective cap on the ends of chromosomes. Embryonic stem cells express telomerase — an enzyme that adds the telomeric...
Homologous Recombination02:31

Homologous Recombination

The basic reaction of homologous recombination (HR) involves two chromatids that contain DNA sequences sharing a significant stretch of identity. One of these sequences uses a strand from another as a template to synthesize DNA in an enzyme-catalyzed reaction. The final product is a novel amalgamation of the two substrates. To ensure an accurate recombination of sequences, HR is restricted to the S and G2 phases of the cell cycle. At these stages, the DNA has been replicated already and the...

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Updated: Jul 11, 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

Interactions of TRF2 with model telomeric ends.

Sheik J Khan1, Giscard Yanez, Kenneth Seldeen

  • 1Department of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, P.O. Box 016129 (R629), Miami, FL 33101-6129, USA.

Biochemical and Biophysical Research Communications
|September 14, 2007
PubMed
Summary

TTAGGG repeat factor 2 (TRF2) binds telomeric DNA junctions, preventing degradation. TRF2 oligomerization via its linker region and TRFH domain is crucial for telomere T-loop formation and stability.

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Last Updated: Jul 11, 2026

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Telomeres protect eukaryotic chromosome ends and are vital for genomic stability.
  • TTAGGG repeat factor 2 (TRF2) is a key protein involved in telomere maintenance, proposed to form T-loops.
  • The precise mechanism of TRF2's interaction with telomeric DNA structures remains incompletely understood.

Purpose of the Study:

  • To investigate the specific interactions of TRF2 with telomeric DNA junctions.
  • To elucidate the role of different TRF2 domains in DNA binding and oligomerization.
  • To understand TRF2's contribution to T-loop formation.

Main Methods:

  • Electrophoretic mobility shift assays (EMSAs) to study DNA-protein interactions.
  • Atomic force microscopy (AFM) to visualize DNA-TRF2 complexes.
  • Exonuclease T cleavage assays to assess DNA protection.

Main Results:

  • TRF2 specifically binds to telomeric single-stranded/double-stranded DNA junctions.
  • TRF2 binding is influenced by the sequence of the G-strand overhang and junctional DNA.
  • TRF2 association inhibits exonuclease T-mediated DNA degradation.
  • The TRF2 linker region, previously uncharacterized, mediates DNA-specific oligomerization, independent of the DNA binding domain.
  • Both the TRFH domain and the linker region are involved in TRF2 oligomerization.

Conclusions:

  • TRF2 binds telomeric DNA junctions, protecting them from degradation.
  • TRF2 oligomerization, involving both the TRFH domain and the linker region, is essential for T-loop formation.
  • These findings provide mechanistic insights into TRF2's role in maintaining telomere integrity.