类似actin的ParM纤维的结构显示了等离子体分离的结构
Tanmay A M Bharat1, Garib N Murshudov1, Carsten Sachse2
1Structural Studies Division, MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Nature
|April 28, 2015
概括
最简单的线粒机械使用类似于actin的ParM纤维来分离大肠杆菌中的等离子体. 结构研究揭示了这些细丝如何形成动态,将等离子体推向细胞极点.
科学领域:
- 微生物学 微生物学
- 结构生物学 结构生物学
- 分子生物学分子生物学
背景情况:
- 在大肠杆菌中等离子体分离依赖于ParMRC系统.
- 类似于动素的ParM纤维形成双极,以分离等离子体.
研究的目的:
- 为了阐明ParM纤维的近原子结构和排列.
- 了解 ParM 纤维的动态不稳定性的机制.
- 在实验室和细菌细胞内研究ParM导线结构.
主要方法:
- 电子冷显微镜 (cryo-EM) 用于高分辨率的光纤结构.
- 在不同核酸状态 (例如,AMPPNP) 中确定ParM导线结构.
- 全细胞电子冷图,用于细胞内丝的可视化.
主要成果:
- 帕尔M线丝的近原子分辨率结构显示出强大的纵向和较弱的横向相互作用.
- 与AMPPNP结合的ParM纤维的结构以4.3 Å的分辨率确定.
- 反平行ParM双体的重建,形成,在细胞中大量存在.
结论:
- 帕尔M纤维构成已知最简单的用于等离子体分离的线粒机械.
- 动态不稳定机制与ParM子单元的核酸状态有关.
- 帕姆双重体的存在支持了R1等离子体分离的异步模型.
相关概念视频
Cytoskeletal Proteins in Bacteria
4.5K
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...
4.5K
Generation of Straight or Branched Actin Filaments
4.0K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
4.0K
Mechanism of Filopodia Formation
3.5K
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...
3.5K
Formation of Higher-order Actin Filaments
3.9K
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...
3.9K
Assembly of Cytoskeletal Filaments
28.5K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
28.5K
Actin Polymerization
9.1K
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...
9.1K


