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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

Overview
DNA Helicases00:55

DNA Helicases

DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...
Chromosome Replication02:31

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...

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Related Experiment Video

Updated: May 13, 2026

In vitro Reconstitution of the Active T. castaneum Telomerase
09:25

In vitro Reconstitution of the Active T. castaneum Telomerase

Published on: July 14, 2011

Structure of active dimeric human telomerase.

Anselm Sauerwald1, Sara Sandin, Gaël Cristofari

  • 1Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.

Nature Structural & Molecular Biology
|March 12, 2013
PubMed
Summary
This summary is machine-generated.

Human telomerase, crucial for DNA replication, functions as a dimer. This study reveals the active full-length human telomerase dimer structure, showing two catalytic protein subunits (TERT) are essential for its function.

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Last Updated: May 13, 2026

In vitro Reconstitution of the Active T. castaneum Telomerase
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Published on: July 14, 2011

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

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Telomerase is a ribonucleoprotein enzyme responsible for maintaining telomere length.
  • The quaternary structure of human telomerase, specifically whether it functions as a monomer or dimer, has been a long-standing question.
  • Understanding telomerase structure is critical for comprehending its role in cellular aging and cancer.

Purpose of the Study:

  • To determine the functional state (monomer or dimer) of in vivo-assembled human telomerase.
  • To elucidate the three-dimensional structure of the active full-length human telomerase dimer.
  • To provide insights into the spatial arrangement of RNA (TER) and protein (TERT) subunits within the telomerase complex.

Main Methods:

  • Biochemical assays and labeling techniques to analyze in vivo-assembled human telomerase.
  • Single-particle electron microscopy (EM) in negative stain to determine the 3D structure.
  • Atomic model fitting of the TERT subunit into the EM density map.

Main Results:

  • In vivo-assembled human telomerase contains two TERT subunits and binds two telomeric DNA substrates.
  • Catalytic activity necessitates functional active sites on both TERT subunits, confirming dimer function.
  • The 3D structure reveals a bilobal architecture with monomers linked by a flexible interface.

Conclusions:

  • Human telomerase functions as a dimer, requiring two TERT active sites for catalytic activity.
  • The determined structure provides a molecular basis for telomerase function and regulation.
  • This structural insight aids in understanding telomere maintenance and potential therapeutic targeting.