在水性多相系统中,细菌微分区外蛋白的界面组装
A A Dharani T Abeysinghe1, Eric J Young2,3, Andrew T Rowland1
1Department of Chemistry, Pennsylvania State University, State College, PA, 16801, USA.
Small (Weinheim an der Bergstrasse, Germany)
|December 1, 2023
概括
研究人员将细菌微分区 (BMC) 蛋白与液体液相分离 (LLPS) 结合起来,创建了新的分区. 这些蛋白质涂层的滴滴为合成细胞提供了一种新策略,通过酶或RNA等载荷来组织仿生功能.
科学领域:
- 生物化学 生物化学
- 合成生物学 合成生物学
- 材料科学 材料科学 材料科学
背景情况:
- 分体化对生命至关重要,通过各种结构 (如脂质膜,蛋白质或生物聚合物相分离) 来实现.
- 细菌微分区 (BMC) 蛋白被称为自我组装,在细菌中形成基于蛋白质的分区.
- 液体-液体相分离 (LLPS) 是一种生物物理过程,通过细胞组件的自发去混合来创建没有膜的隔间.
研究的目的:
- 通过将BMC外蛋白与LLPS集成来开发新的细分形式.
- 研究BMC蛋白在不同相隔系统中的液体-液体接口上的组装行为.
- 探索这些工程隔间在合成细胞内组织仿生功能方面的潜力.
主要方法:
- 使用聚乙烯基醇/德克斯两相水性系统和聚氨酸/聚亚斯巴酸复合合体系统来创建液体-液体接口.
- 在这些相隔系统的接口处组装的细菌微分区 (BMC) 蛋白.
- 研究了多电解质比率和蛋白质度对界面组装和与聚合竞争的影响.
- 开发了一种三相系统,通过将协体液滴封装在富含德克斯的液滴中,用于可调节的蛋白质定位.
主要成果:
- 在PEG/dextran和协体系统的液体-液体接口上成功组装了BMC外蛋白.
- 协同体系统中的界面组件对阴离子和阴离子聚的比率敏感,表明电静电控制.
- 蛋白质度和聚的可用性影响了接口组装和聚合之间的竞争.
- 一个三相系统通过调整聚电解质电荷比率来证明BMC蛋白的可调节界面定位.
结论:
- BMC外蛋白可以被引导在液体-液体接口上组装,从而创建新的蛋白质涂层滴.
- 这些通过LLPS和蛋白质自我组装形成的工程液滴,代表了合成细胞设计的新策略.
- 在这些区间内封装酶或RNA等货物的能力使生物模拟函数的组织成为可能.
相关概念视频
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
Mechanisms of Membrane Domain Formation
3.0K
Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with...
Another mechanism for membrane domain formation involves membrane proteins interacting with...
3.0K
Protein-protein Interfaces
12.5K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
12.5K
SNAREs and Membrane Fusion
10.9K
Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
10.9K
Cytoskeletal Proteins in Bacteria
3.4K
Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...
3.4K
Fluid Mosaic Model
11.9K
Scientists identified the plasma membrane in the 1890s and its principal chemical components (lipids and proteins) by 1915. The model for plasma membrane structure, proposed in 1935 by Hugh Davson and James Danielli, was the first model to be widely accepted in the scientific community. The model was based on the plasma membrane's "railroad track" appearance in early electron micrographs. Davson and Danielli theorized that the plasma membrane's structure resembled a sandwich...
11.9K


