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相关概念视频

Replication in Eukaryotes01:29

Replication in Eukaryotes

19.5K
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...
19.5K
Replication in Eukaryotes02:31

Replication in Eukaryotes

208.6K
Overview
208.6K
The Replisome03:01

The Replisome

39.9K
DNA replication is carried out by a large complex of proteins that act in a coordinated matter to achieve high-fidelity DNA replication. Together this complex is known as the DNA replication machinery or the replisome.
The synthesis of the leading and lagging strands is a highly coordinated process. To explain this, the “Trombone model” was proposed by Bruce Alberts in 1980. The DNA loop formation starts when a primer is synthesized on the parent lagging strand. The loop grows with...
39.9K
Chromosome Structure02:40

Chromosome Structure

28.1K
A functional eukaryotic chromosome must contain three elements: a centromere, telomeres, and numerous origins of replication.
The centromere is a DNA sequence that links sister chromatids. This is also where kinetochores, protein complexes to which spindle microtubules attach, are constructed after the chromosome is replicated. The kinetochores allow the spindle microtubules to move the chromosomes within the cell during cell division.
Telomeres consist of non-coding repetitive nucleotide...
28.1K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

3.1K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
3.1K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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相关实验视频

Updated: Apr 16, 2026

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

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细胞起源识别复合体的晶体结构.

Franziska Bleichert1, Michael R Botchan2, James M Berger1

  • 1Department of Biophysics and Biophysical Chemistry, Johns Hopkins School of Medicine, Baltimore, Maryland 21205, USA.

Nature
|March 13, 2015
PubMed
概括

原始识别复合体 (ORC) 结构揭示了控制DNA复制启动的新机制. 这种结构表明ORC可以在活性和抑制状态之间切换,影响细胞循环调节.

科学领域:

  • 结构生物学是结构生物学.
  • 分子生物学分子生物学
  • 细胞周期调节细胞周期调节

背景情况:

  • 细胞DNA复制的启动对于基因组的稳定性至关重要.
  • 异质体起源识别复合体 (ORC) 在真核生物中协调复制的开始.

研究的目的:

  • 为了确定Drosophila ORC的晶体结构.
  • 阐明ORC功能在DNA复制启动中的结构基础.

主要方法:

  • 在3.5 Å分辨率的X射线晶体学.
  • 对270 kDa的ORC核心复合体进行结构分析.

主要成果:

  • ORC结构显示出一个双层环,带有翼螺旋和AAA+域.
  • 观察到不可预期的域间交换和准螺旋DNA结合通道.
  • Orc1 AAA+域的显著旋转表明了自身抑制的机制.

结论:

  • 果 ORC 包围了 DNA,并激活了 MCM2-7 复合体来进行螺旋酶加载.
  • 结构表明ORC可以在活性和自我抑制的形状之间过渡.

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Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO

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Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes
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Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes

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Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO
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Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO

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Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes
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Iterative Optimization of DNA Duplexes for Crystallization of SeqA-DNA Complexes

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  • 这种构造性切换为细胞循环控制提供了一个新的调节机制.