冰核蛋白自组装成大型纤维,在接近0°C的温度下触发结
Thomas Hansen1, Jocelyn Lee1, Naama Reicher2
1Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Canada.
eLife
|December 18, 2023
概括
来自细菌的冰核蛋白 (INPs) 自组装成关键的多重分子. 一个带正电荷的C端子域驱动了这种多元化,这对于形成和潜在的生物技术应用至关重要.
科学领域:
- 生物化学 生物化学
- 微生物学 微生物学
- 生物物理学的生物物理.
背景情况:
- 在零度以下的温度下形成冰需要有序的水分子.
- 来自像*Pseudomonas syringae*这样的细菌的冰核蛋白 (INPs) 调解了这种水的排序.
- 单个INP太小,无法启动冷;需要大型多元器件.
研究的目的:
- 为了研究冰核蛋白 (INP) 多元化的机制.
- 确定负责INP自组装的结构部件.
- 了解INP多元体如何在高零下温度下形成冰核.
主要方法:
- 对INP结构的基因操纵 (切断,转移,电荷修改).
- 评估修改后的INPs的冰核化能力.
- 低温电子断层扫描可视化INP多重结构.
主要成果:
- 对于多元化来说,INP的中央β-soluid的一个负电荷的C端子域对多元化至关重要.
- 改变这个子域取消了冰核活动.
- 低温电子断层扫描显示INP多元体形成~5nm宽,长达200nm的纤维.
结论:
- C端充电子域对于INP多元化和冰核化至关重要.
- INP多元器件组装成纤维,可能是通过重叠的反平行二极管.
- 这种理解为开发用于生物技术的无细胞冰核子开辟了道路.
关键词:
美国大肠杆菌 (E. coli).生物化学 生物化学生物信息学是一种生物信息学.化学生物学 化学生物学冷电子断层扫描 (Cryo-electron tomography) 是一种电子断层扫描技术.冰的核化是冰的核化.冰核化蛋白质 冰核化蛋白质分子生物物理学分子生物物理学蛋白质自我组装的蛋白质自组装结构生物学结构生物学这是一种β-solenoid.更多相关视频
09:32LabVIEW-operated Novel Nanoliter Osmometer for Ice Binding Protein Investigations
Published on: February 4, 2013
20.7K
09:43Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification
Published on: May 5, 2017
8.7K
相关概念视频
Formation of Intermediate Filaments
3.1K
Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
3.1K
Formation of Higher-order Actin Filaments
3.0K
The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...
The high-order actin...
3.0K
Mechanism of Filopodia Formation
2.3K
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
2.3K
Recrystallization: Solid–Solution Equilibria
1.1K
Recrystallization is a purification technique used to separate impurities from solid compounds. In this technique, no chemical reactions occur. Instead, it exploits physical properties only, specifically, the solubility differences between the desired compound and impurities, either at a single temperature or at different temperatures, and under other selected conditions. The solid-solution equilibrium (solubility equilibrium) of each component in the solution represents a binary phase...
1.1K
Actin Polymerization
6.6K
Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶ nucleation, elongation, and steady-state phase.
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight...
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight...
6.6K
Protein Complex Assembly
10.6K
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...
10.6K
