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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.
Translesion DNA Polymerases02:10

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...
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...
Transcription Attenuation in Prokaryotes02:42

Transcription Attenuation in Prokaryotes

Transcriptional attenuation occurs when RNA transcription is prematurely terminated due to the formation of a terminator mRNA hairpin structure.  Bacteria use these hairpins to regulate the transcription process and control the synthesis of several amino acids including histidine, lysine, threonine, and phenylalanine. Transcription attenuation takes place in the non-coding regions of mRNA.
There are several different mechanisms used to attenuate transcription. In ribosome mediated...
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...

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Analyzing Telomeric Protein-DNA Interactions Using Single-Molecule Magnetic Tweezers
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Functional interaction between telomere protein TPP1 and telomerase.

Arthur J Zaug1, Elaine R Podell, Jayakrishnan Nandakumar

  • 1Department of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Colorado, Boulder, 80309, USA.

Genes & Development
|March 17, 2010
PubMed
Summary

Human telomere protection proteins POT1-TPP1 activate telomerase but require specific protein interactions, not just DNA binding. A key glycine in TERT’s TEN domain is crucial for this telomerase regulation.

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Published on: June 12, 2018

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Telomere maintenance is crucial for genomic stability.
  • POT1-TPP1 proteins bind telomeric DNA and regulate telomerase.
  • POT1-TPP1 binding enhances telomerase processivity.

Purpose of the Study:

  • To investigate the mechanism by which POT1-TPP1 activates telomerase.
  • To determine if POT1-TPP1 activation is DNA substrate-specific or protein-interaction-dependent.
  • To identify specific regions within telomerase and POT1-TPP1 involved in this interaction.

Main Methods:

  • Comparative analysis of human and medaka fish telomerase activity with human POT1-TPP1.
  • Site-directed mutagenesis of the TERT TEN domain, specifically Gly100.
  • Construction and testing of chimeric human-fish telomerases.
  • Cross-species testing of POT1A-TPP1 complexes with different telomerases.

Main Results:

  • Human POT1-TPP1 did not activate medaka fish telomerase.
  • Mutation of Gly100 in the TERT TEN domain abolished POT1-TPP1-mediated processivity enhancement.
  • Chimeric telomerases indicated determinants of processivity outside the TEN domain.
  • Mammalian telomerases showed specificity for their cognate TPP1 proteins.

Conclusions:

  • POT1-TPP1 activation of telomerase processivity is mediated by specific protein-protein interactions, not solely DNA binding.
  • A specific interaction between TPP1 and the Gly100 region of the TERT TEN domain is essential for high-processivity telomerase action.
  • Telomerase regulation involves complex interactions between telomeric proteins and the telomerase enzyme itself.