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Single-Strand DNA Binding Proteins

Single-Strand DNA Binding Proteins

For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...

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识别slirp作为一个g四重组结合蛋白

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识别slirp作为一个g四重组结合蛋白

相关实验视频

A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1

A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1

Published on: March 18, 2017

识别SLIRP作为一个G四重组结合蛋白

Preston Williams¹, Lin Li¹, Xiaoli Dong¹

¹Department of Chemistry, University of California Riverside , Riverside, California 92521-0403, United States.

Journal of the American Chemical Society

|September 2, 2017

在PubMed 上查看摘要

概括

此摘要是机器生成的。

研究人员发现SLIRP是一种新型蛋白质,直接与瓜四重复 (G4) 基因结构结合. 这一发现揭示了对调节G4DNA生物学的复杂细胞网络的新见解.

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PAR-CliP - A Method to Identify Transcriptome-wide the Binding Sites of RNA Binding Proteins

PAR-CliP - A Method to Identify Transcriptome-wide the Binding Sites of RNA Binding Proteins

Published on: July 2, 2010

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes

Published on: April 4, 2025

相关实验视频

A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1

A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1

Published on: March 18, 2017

PAR-CliP - A Method to Identify Transcriptome-wide the Binding Sites of RNA Binding Proteins

PAR-CliP - A Method to Identify Transcriptome-wide the Binding Sites of RNA Binding Proteins

Published on: July 2, 2010

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes

Published on: April 4, 2025

科学领域:

基因组学
分子生物学
生物化学

背景情况:

关氨酸四重复 (G4) DNA结构是关键的二次动机,参与DNA复制,转录和基因组稳定.
了解与G4结构相互作用的蛋白质是阐明它们的调节作用的关键.

研究的目的:

识别与特定的瓜四重复 (G4) DNA 结构相互作用的新型蛋白质.
描述新发现的G4相互作用蛋白的结合特性和全基因组占用率.

主要方法:

使用定量质谱分析分析了人类端粒,cMYC和cKIT中的G4结构与蛋白质的相互作用.
使用CRISPR-Cas9技术和ChIP-Seq分析来确定全基因组的SLIRP结合.
使用生物层干扰测量来量化SLIRP与G4DNA的结合亲和力.

主要成果:

SLIRP被确定为一种直接与G4DNA结合的新型蛋白质,具有高亲和力 (低纳米K_d).
SLIRP的RNA识别因子 (RRM) 域对于其强大的与G4DNA结合至关重要.
全基因组分析显示,SLIRP优先结合能够形成G4结构的富G序列.

结论:

SLIRP是一种新型的细胞蛋白,与瓜四重复基因直接相互作用.
SLIRP的发现突显了G4DNA生物学的复杂调节机制.
SLIRP与G4结构的特定结合表明它在调节G4依赖的细胞过程中的作用.