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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...
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...

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Updated: Jun 19, 2026

Use of Interferon-γ Enzyme-linked Immunospot Assay to Characterize Novel T-cell Epitopes of Human Papillomavirus
13:41

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HPV E6 protein interacts physically and functionally with the cellular telomerase complex.

Xuefeng Liu1, Aleksandra Dakic, Yiyu Zhang

  • 1Department of Pathology, Georgetown University Medical School, 3900 Reservoir Road, Washington, DC 20057, USA.

Proceedings of the National Academy of Sciences of the United States of America
|October 22, 2009
PubMed
Summary
This summary is machine-generated.

High-risk HPV E6 protein directly binds human telomerase (hTERT), increasing its activity post-transcriptionally. This interaction is crucial for viral oncogenesis and replication, offering new therapeutic targets.

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Use of Interferon-γ Enzyme-linked Immunospot Assay to Characterize Novel T-cell Epitopes of Human Papillomavirus
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Published on: March 11, 2014

Area of Science:

  • Molecular Biology
  • Virology
  • Cell Biology

Background:

  • High-risk human papillomavirus (HPV) oncoproteins E6 and E7 are critical for immortalizing keratinocytes.
  • HPV E6 protein induces the human telomerase reverse transcriptase (hTERT) promoter, partly through interactions with E6AP, c-Myc, and NFX-1.

Purpose of the Study:

  • To investigate the direct interaction between HPV E6 oncoprotein and human telomerase (hTERT).
  • To elucidate the mechanism by which E6 modulates telomerase activity and its role in viral oncogenesis.

Main Methods:

  • Co-immunoprecipitation assays to detect E6/hTERT interactions.
  • Analysis of telomerase activity in cells expressing hTERT and HPV E6.
  • In vitro and in vivo degradation assays for hTERT protein.

Main Results:

  • HPV E6 protein directly binds to hTERT protein.
  • E6 associates with telomeric DNA and active telomerase complexes.
  • E6 enhances telomerase activity independently of hTERT mRNA expression and does not degrade hTERT protein.
  • C-terminal tagged hTERT, while not immortalizing fibroblasts, does immortalize keratinocytes with E7.

Conclusions:

  • HPV E6 protein activates telomerase via a post-transcriptional mechanism through direct interaction with hTERT.
  • This interaction modulates telomere function, potentially playing a role in neoplasia and viral replication.
  • Findings offer a model for viral modulation of telomerase and suggest therapeutic avenues.