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Replication in Eukaryotes

Replication in Eukaryotes

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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

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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...

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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.
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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.

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Related Experiment Video

Updated: May 11, 2026

In vitro Reconstitution of the Active T. castaneum Telomerase

In vitro Reconstitution of the Active T. castaneum Telomerase

Published on: July 14, 2011

The POT1-TPP1 telomere complex is a telomerase processivity factor.

Feng Wang¹, Elaine R Podell, Arthur J Zaug

¹Department of Biological Chemistry, University of Michigan Medical School, MSRBIII 5301D, 1150 W. Medical Center Drive, Ann Arbor, Michigan 48109, USA.

|January 24, 2007

Summary

This summary is machine-generated.

The POT1-TPP1 protein complex binds telomeric DNA and enhances human telomerase activity. This finding suggests a dual role for POT1-TPP1 in regulating telomere length and stability.

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Last Updated: May 11, 2026

In vitro Reconstitution of the Active T. castaneum Telomerase

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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

Area of Science:

Molecular Biology
Genetics
Biochemistry

Background:

Telomeres protect chromosome ends from degradation and fusion.
POT1 (protection of telomeres) binds G-rich DNA overhangs at telomeres.
TPP1 is a POT1 binding partner proposed to be part of the shelterin complex.

Purpose of the Study:

To determine the structural relationship between TPP1 and POT1.
To investigate the effect of the POT1-TPP1 complex on telomerase activity.

Main Methods:

Crystal structure determination of a human TPP1 domain.
Biochemical assays to assess telomerase activity and processivity in the presence of POT1-TPP1 and telomeric DNA.

Main Results:

The crystal structure of TPP1 revealed an oligonucleotide/oligosaccharide-binding fold similar to a protozoan telomere end-binding protein beta-subunit, suggesting TPP1 is the POT1 beta-subunit.
The POT1-TPP1 complex, bound to telomeric DNA, significantly increased the activity and processivity of human telomerase.

Conclusions:

TPP1 is identified as the missing beta-subunit of human POT1.
The POT1-TPP1 complex acts as a processivity factor for telomerase, enhancing telomere extension, contrasting with the inhibitory role of other telomeric DNA end-binding proteins.