在冷解过程中,一种本质上有障碍的植物蛋白在体外的功能多样性是由其结构性可塑性编码的
Itzell Hernández-Sánchez1, Tobias Rindfleisch1,2,3,4, Jessica Alpers1
1Max-Planck Institute of Molecular Plant Physiology, Potsdam, Germany.
Protein science : a publication of the Protein Society
|April 25, 2024
概括
晚期胚胎生成丰富 (LEA) 蛋白质保护生物体免受脱水. 这项研究揭示了阿拉比多普西斯的COR15A蛋白质是如何形成的.
科学领域:
- 植物分子生物学 植物分子生物学
- 生物物理学的生物物理.
- 结构生物学是结构生物学.
背景情况:
- 本质上有障碍的晚期胚胎生成丰富蛋白 (LEA) 对于植物和生物体的脱水耐受性至关重要.
- 在冷,干旱和高盐度等压力条件下,LEA蛋白稳定敏感的细胞结构.
- 环境的敏感性使得LEA蛋白能够经历形状变化,形成有序结构和无膜有机体.
研究的目的:
- 为了阐明Arabidopsis thalianaLEA蛋白COR15A的功能多样性的结构基础.
- 了解COR15A如何通过其结构的表现来稳定细胞组件.
- 研究LEA蛋白质寡合化背后的分子机制.
主要方法:
- 在体外生化和生物物理分析的阿拉比多普西斯COR15A.
- 蛋白质构成组合和相互作用的结构性表征.
- 识别分子识别特征驱动蛋白质复合体的形成.
主要成果:
- 通过COR15A进行的膜稳定是通过二次结构采用进行的.
- 酶稳定是通过COR15A寡合体复合物的形成来实现的.
- 寡合化是由α-螺旋分子识别特征 (α-MoRF) 驱动的,形成非正规的卷轴.
结论:
- 在体外,COR15A的结构结构决定了它的功能多样性.
- 特定的结构变化和寡合化是LEA蛋白保护功能的关键.
- 非正规的卷轴-卷轴形成可能是LEA蛋白 homo-和 hetero-oligomerization的一个常见机制.
更多相关视频
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
13:52Studying the Supramolecular Organization of Photosynthetic Membranes within Freeze-fractured Leaf Tissues by Cryo-scanning Electron Microscopy
Published on: June 23, 2016
12.2K
相关概念视频
Intrinsically Disordered Proteins
17.8K
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...
17.8K
Protein Folding
118.0K
Overview
118.0K
Responses to Heat and Cold Stress
13.5K
Every organism has an optimum temperature range within which healthy growth and physiological functioning can occur. At the ends of this range, there will be a minimum and maximum temperature that interrupt biological processes.
13.5K
Protein and Protein Structure
79.5K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
79.5K
Molecular Chaperones and Protein Folding
17.9K
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...
17.9K
Protein Denaturation
4.1K
The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
4.1K
