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Telomeres and Telomerase

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 Telomerase

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.

Translesion DNA Polymerases

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...

Chromosome Replication

Chromosome Replication

Before a cell can divide, it must accurately replicate all of its chromosomes, including the DNA and its associated histone and non-histone proteins. This process begins at numerous origins of replication during the S phase of the cell cycle in each of a cell’s chromosomes simultaneously. Certain nucleotides can act as origins of replication, but these sequences are not well defined - especially in complex, multi-cellular, eukaryotic species. The length of DNA that spans an origin of...

Replication in Eukaryotes

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 Eukaryotes

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Related Experiment Video

Updated: May 26, 2026

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

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

Published on: August 30, 2024

Structural basis for Tetrahymena telomerase processivity factor Teb1 binding to single-stranded telomeric-repeat DNA.

Zhixiong Zeng¹, Bosun Min, Jing Huang

¹Howard Hughes Medical Institute, Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, MI 48109, USA.

Proceedings of the National Academy of Sciences of the United States of America

|December 7, 2011

Summary

The Teb1 protein subunit enhances telomerase repeat addition processivity (RAP) by specifically binding telomeric DNA. Its domains recruit telomerase and trap DNA products, ensuring efficient telomere synthesis.

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Droplet Digital TRAP (ddTRAP): Adaptation of the Telomere Repeat Amplification Protocol to Droplet Digital Polymerase Chain Reaction

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Published on: May 3, 2019

Area of Science:

Molecular Biology
Biochemistry
Structural Biology

Background:

Telomerase synthesizes telomeric DNA repeats using an RNA template.
Telomerase achieves repeat addition processivity (RAP) by retaining its single-stranded DNA product.
The Tetrahymena telomerase holoenzyme's RAP is dependent on the Teb1 subunit.

Purpose of the Study:

To elucidate the structural basis of telomeric-repeat DNA recognition by Teb1.
To understand the functional significance of Teb1's DNA-binding domains in telomerase activity.
To investigate the mechanism by which Teb1 contributes to RAP.

Main Methods:

Crystal structure determination of Teb1 DNA-binding domains.
Site-directed mutagenesis to identify key amino acids for DNA interaction.
Reconstitution of telomerase holoenzyme to assess RAP activity.

Main Results:

Teb1's central domains (Teb1A and Teb1B) exhibit high-affinity, selective binding to telomeric repeats, similar to POT1.
Teb1's C-terminal domain (Teb1C) shares features with RPA70C and is crucial for high RAP.
The Teb1C zinc ribbon is not essential for DNA binding but is required for high RAP, possibly aiding holoenzyme association.

Conclusions:

Teb1AB binding recruits telomerase holoenzyme to telomeres.
Teb1C-DNA interaction stabilizes the enzyme-product complex in a sliding-clamp-like manner, enhancing RAP.
Teb1 plays a dual role in telomerase function: recruitment and product trapping for processivity.