托尔-帕尔复合体在细菌外膜脂质恒温中的主要作用
Wee Boon Tan1,2, Shu-Sin Chng3,4
1Department of Chemistry, National University of, Singapore, Singapore.
Nature communications
|March 7, 2025
概括
托尔 - 帕尔复合体维持了外膜脂质平衡在阴性细菌,对信封完整性至关重要. 这项研究表明,它在脂质平衡中起着主要的作用,与细胞分裂功能分开.
科学领域:
- 微生物学 微生物学
- 细胞生物学 细胞生物学
- 生物化学 生物化学
背景情况:
- 格拉姆阴性细菌具有独特的外膜 (OM),对于结构完整性和屏障功能至关重要.
- 已知Tol-Pal复合体参与维持OM稳定性和脂质平衡.
- 它的确切作用很难确定,因为它位于细胞隔膜,并参与细胞分裂.
研究的目的:
- 区分Tol-Pal复合体在OM脂质稳态中的功能与其在细胞分裂中的作用.
- 为了研究Tol-Pal复合体保持OM完整性的能力,独立于细胞分裂.
主要方法:
- 在大肠杆菌中设计一个模拟的Tol-Pal复合体,以破坏隔膜局部.
- 分析表达改性Tol-Pal复合体的细菌的脂质平衡和OM完整性.
主要成果:
- 工程设计的,局部定位的Tol-Pal复合体有效地维持了OM中的脂质平衡.
- 这种恢复脂质稳定导致OM完整性和屏障功能的恢复.
- 证实Tol-Pal复合体在OM脂质稳定中的功能与其在细胞分裂过程中的作用无关.
结论:
- 托尔-帕尔综合体的主要功能是确保OM脂质平衡.
- 这一功能对于维护包膜完整性和格兰氏阴性细菌的屏障特性至关重要.
- 从细胞分裂中解脱Tol-Pal在脂质稳定中的作用,可以更清楚地了解其基本机制.
更多相关视频
12:57Isolation and Chemical Characterization of Lipid A from Gram-negative Bacteria
Published on: September 16, 2013
31.6K
10:24Separation of the Cell Envelope for Gram-negative Bacteria into Inner and Outer Membrane Fractions with Technical Adjustments for Acinetobacter baumannii
Published on: April 10, 2020
13.1K
相关概念视频
Structure of Porins
2.9K
Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
2.9K
Protein Transport to the Outer Chloroplast Membrane
1.9K
Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
1.9K
Asymmetric Lipid Bilayer
7.1K
Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
7.1K
Membrane Lipids
21.1K
Lipids are an essential component of all biological membranes. The average lipid content in mammalian membranes is 50%, though it can be as low as 20% in the inner mitochondrial membrane or as high as 80% in the myelin sheath present around the nerve cells.
Phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, and sphingomyelin are the most common phospholipids present in mammalian membranes. At physiological pH, phosphatidylserine is negatively charged, while the other three...
Phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, and sphingomyelin are the most common phospholipids present in mammalian membranes. At physiological pH, phosphatidylserine is negatively charged, while the other three...
21.1K
Protein Transport to the Thylakoids
2.2K
Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...
2.2K
Multi-pass Transmembrane Proteins and β-barrels
5.2K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
5.2K
