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Replication in Eukaryotes02:31

Replication in Eukaryotes

Overview
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...
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...
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.

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Telomerase RNA structural heterogeneity in living human cells detected by DMS-MaPseq.

Nature communications·2025
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POT1 recruits and regulates CST-Polα/primase at human telomeres.

Cell·2024
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Telomerase RNA structural heterogeneity in living human cells detected by DMS-MaPseq.

bioRxiv : the preprint server for biology·2023
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Reconstitution of a telomeric replicon organized by CST.

Nature·2022
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CST does not evict elongating telomerase but prevents initiation by ssDNA binding.

Nucleic acids research·2021
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The structure of human CST reveals a decameric assembly bound to telomeric DNA.

Science (New York, N.Y.)·2020

関連する実験動画

Updated: May 11, 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

POT1-TPP1テロメア複合体はテロメラーゼプロセシビティ因子である.

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.

Nature
|January 24, 2007
PubMed
まとめ

POT1-TPP1タンパク質複合体はテロメアDNAと結合し,ヒトのテロメラーゼ活性を増強する. この発見は,POT1-TPP1がテロメアの長さと安定性を調節する二重の役割を果たしていることを示唆しています.

さらに関連する動画

Droplet Digital TRAP (ddTRAP): Adaptation of the Telomere Repeat Amplification Protocol to Droplet Digital Polymerase Chain Reaction
06:38

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

Published on: May 3, 2019

Analyzing Telomeric Protein-DNA Interactions Using Single-Molecule Magnetic Tweezers
11:21

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

Published on: August 30, 2024

関連する実験動画

Last Updated: May 11, 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

Droplet Digital TRAP (ddTRAP): Adaptation of the Telomere Repeat Amplification Protocol to Droplet Digital Polymerase Chain Reaction
06:38

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

Published on: May 3, 2019

Analyzing Telomeric Protein-DNA Interactions Using Single-Molecule Magnetic Tweezers
11:21

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

Published on: August 30, 2024

科学分野:

  • 分子生物学は分子生物学である.
  • 遺伝学 遺伝学とは
  • バイオケミストリー バイオケミストリー

背景:

  • テロメアは染色体の末端を分解と融合から保護する.
  • POT1 (テロメアの保護) は,G豊富なDNAのオーバーハングをテロメアに結合する.
  • TPP1はPOT1の拘束力のあるパートナーであり,シェルター・コンプレックスの一部として提案されています.

研究 の 目的:

  • TPP1とPOT1.1の構造的関係を決定する.
  • テロメラーゼ活性に対するPOT1-TPP1複合体の効果を調査する.

主な方法:

  • 人間のTPP1ドメインの結晶構造の決定.
  • POT1-TPP1およびテロメアDNAの存在下でのテロメラーゼ活性およびプロセシビティの評価のための生化学的測定法.

主要な成果:

  • TPP1の結晶構造は,原生種のテロメア末端結合タンパク質βサブユニットに似たオリゴヌクレオチド/オリゴサカライド結合折れを示しており,TPP1がPOT1βサブユニットであることを示唆しています.
  • テロメアDNAに結合したPOT1-TPP1複合体は,ヒトテロメラーゼの活性とプロセシビティを著しく増加させた.

結論:

  • TPP1は,ヒトPOT1.1の欠落しているβサブユニットとして特定されています.
  • POT1-TPP1複合体はテロメラーゼのプロセシビティ因子として作用し,テロメア延長を強化し,他のテロメアDNA末端結合タンパク質の抑制作用と対照的です.