多酸盐比DNA更有效地区分蛋白质构成组合,促进多样化的组装和成熟行为
Saloni Goyal1, Divya Rajendran1, Anup Kumar Mani1
1Department of Biotechnology, Bhupat and Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai, India.
eLife
|July 14, 2025
概括
多酸盐 (polyP) 比DNA更有效地驱动蛋白质凝聚物组装和结构变化. 这项研究揭示了polyP.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 生物物理学的生物物理.
背景情况:
- 无序的蛋白质与核酸聚集成凝结物,调节细胞功能.
- 聚酸盐 (polyP),一种离子聚合物,也调节应激反应,但其组装机制不太了解.
研究的目的:
- 调查与多聚和DNA内在失序的蛋白质的组装机制.
- 为了比较聚和DNA对蛋白质凝聚物形成和结构的影响.
主要方法:
- 利用了来自大肠杆菌的cytidine抑制剂 (CytR) 的内在失序的DNA结合域 (DBD).
- 使用CytR的突变工程来改变其结构和尺寸.
- 分析了冷凝物质的特性,包括液体到固体的转变和溶解动态.
- 使用生物物理技术评估蛋白质的二次结构变化.
主要成果:
- CytR形成了具有多聚和DNA的转移稳定的液态凝聚物.
- 聚P诱导了CytR的液态-固态过渡和显著的二次结构变化,包括突变物中的聚二类结构.
- DNA主要导致随着时间的推移溶解的转移稳定滴,对CytR.有最小的结构影响.
- 设计的CytR变种显示了与聚的改变组装,导致溶解或聚合.
- 聚聚显示出在蛋白质组合中识别构造异质性的能力更强.
结论:
- 与DNA相比,聚酸盐是蛋白质凝聚物组合和形状变化的更强有力的驱动因素.
- 这些发现突出了聚和DNA在调节细菌蛋白质组合和应激反应方面的独特作用.
- 蛋白质结构和形状灵活性显著影响聚聚的组装动态.
关键词:
它们是DNA DNA DNA DNA.美国大肠杆菌 (E. coli).聚合物 聚合物 聚合物凝结剂是一种凝结剂.成熟 成熟 成熟 成熟.分子生物物理学分子生物物理学生物系统的物理生活系统的物理.聚酸聚酸盐是一种多酸盐.这是光谱学.结构生物学结构生物学更多相关视频
08:34OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
Published on: February 5, 2020
6.8K
07:08Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
7.4K
相关概念视频
Protein Complex Assembly
10.9K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
10.9K
Protein Folding
8.7K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
8.7K
Intrinsically Disordered Proteins
18.2K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
18.2K
Protein Complexes with Interchangeable Parts
2.6K
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...
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...
2.6K
Protein Organization
145.1K
Overview
145.1K
Molecular Chaperones and Protein Folding
18.5K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
18.5K
