Jove
Visualize
联系我们
JoVE
x logofacebook logolinkedin logoyoutube logo
关于 JoVE
概览领导团队博客JoVE 帮助中心
作者
出版流程编辑委员会范围与政策同行评审常见问题投稿
图书馆员
用户评价订阅访问资源图书馆顾问委员会常见问题
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experiments存档
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教师资源中心教师网站
使用条款与条件
隐私政策
政策

相关概念视频

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.

您也可能阅读

相关文章

通过共同作者、期刊和引用图与本文相关的文章。

排序
Same author

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

Nature communications·2025
Same author

POT1 recruits and regulates CST-Polα/primase at human telomeres.

Cell·2024
Same author

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

bioRxiv : the preprint server for biology·2023
Same author

Reconstitution of a telomeric replicon organized by CST.

Nature·2022
Same author

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

Nucleic acids research·2021
Same author

The structure of human CST reveals a decameric assembly bound to telomeric DNA.

Science (New York, N.Y.)·2020

相关实验视频

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端粒复合体是一种端粒酶过程性因子.

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
概括

POT1-TPP1蛋白质复合体与端粒DNA结合,并增强人类端粒酶的活性. 这一发现表明POT1-TPP1在调节端粒长度和稳定性方面具有双重作用.

科学领域:

  • 分子生物学分子生物学
  • 遗传学 遗传学 是一个
  • 生物化学 生物化学

背景情况:

  • 端粒保护染色体末端免受降解和融合.
  • POT1 (端粒的保护) 结合了富含G的DNA在端粒上的突起.
  • TPP1是POT1有约束力的合作伙伴,被提议成为庇护所综合体的一部分.

研究的目的:

  • 确定TPP1和POT1.1之间的结构关系.
  • 研究POT1-TPP1复合体对端粒酶活性的影响.

主要方法:

  • 人类TPP1域的晶体结构的确定.
  • 生物化学测试以评估POT1-TPP1和端粒DNA存在的端粒酶活性和过程性.

主要成果:

  • TPP1的晶体结构显示了类似于原生动物端粒结合蛋白β子单元的寡核酸/寡糖结合,这表明TPP1是POT1β子单元.
  • 与端粒DNA结合的POT1-TPP1复合体显著增加了人类端粒酶的活性和过程性.

结论:

  • TPP1被确定为人类POT1.1缺失的β子单元.
  • POT1-TPP1复合体作为端粒酶的过程性因子,增强端粒延伸,与其他端粒DNA末结合蛋白的抑制作用形成鲜明对比.

更多相关视频

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

相关实验视频

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