秩序脱离混乱:一个内在展开的陪伴者的工作周期
Dana Reichmann1, Ying Xu, Claudia M Cremers
1Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
Cell
|March 6, 2012
概括
在氧化应激过程中,热冲击蛋白33 (Hsp33) 使用它自己的无序区域来结合部分折叠的蛋白质. 这种相互作用稳定了Hsp33,在压力下降时释放客户端.
科学领域:
- 分子生物学分子生物学
- 生物化学 生物化学
- 蛋白质折叠 蛋白质的折叠
背景情况:
- 氧化应激导致蛋白质展开,需要保护机制.
- 像Hsp33这样的氧化还原调节的伴侣体对于细胞防御抗氧化损伤至关重要.
- 激活Hsp33需要部分展开,这是一种新型护送级别的特征.
研究的目的:
- 阐明伴侣蛋白,特别是Hsp33识别和结合客户端蛋白的机制.
- 研究本质上无序区域在Hsp33基质歧视中的作用.
- 了解Hsp33如何在不同的氧化还原条件下调节客户端蛋白质的释放.
主要方法:
- 使用生物物理技术研究了Hsp33与客户端蛋白质的相互作用.
- 分析了Hsp33内在无序区域在基质结合中的作用.
- 在不同的氧化还原状态下,描述了Hsp33和客户端蛋白质的结构变化.
主要成果:
- Hsp33通过其内在无序区域来区分未折叠和部分结构的蛋白质.
- 客户端蛋白与二次结构元素的结合稳定了Hsp33的无序区域,增强了亲和力.
- 在非压力条件下,Hsp33中二硫化物键的反转会破坏客户端蛋白质的稳定,促进折叠能力.
结论:
- Hsp33使用内部的顺序转变来控制客户端蛋白质的结合和释放.
- 这种机制使得能量独立的陪伴者能够在压力期间管理蛋白质折叠中间体.
- Hsp33在细胞对氧化应激和蛋白质平衡的反应中起到至关重要的调节作用.
相关概念视频
Molecular Chaperones and Protein Folding
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...
Molecular Chaperones and Protein Folding
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...
Bacterial Protein Maturation
Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
Regulation of the Unfolded Protein Response
Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
Protein Folding
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Overview


