通过质谱检测探测了与核糖体结合的新生多的折叠稳定性
Ruiyue Tan1, Margaret Hoare1, Kevin A Welle2
1Department of Biology, University of Rochester, Rochester, NY 14627.
概括
核糖体显著影响新生的蛋白质折叠的稳定性. 这项研究引入了一种质谱法来测量这些变化,揭示了静电相互作用是关键.
科学领域:
- 分子生物学分子生物学
- 蛋白质组学是指蛋白质组学.
- 生物物理学的生物物理.
背景情况:
- 蛋白质折叠通常在核糖体内发生共同翻译.
- 核糖体接近蛋白质折叠热力学的影响还不太清楚.
- 新生的多链在合成过程中与核糖体密切相互作用.
研究的目的:
- 开发一种方法来测量与核糖体结合的新生多链的折叠稳定性.
- 为了研究核糖体如何影响蛋白质折叠热力学.
- 为了确定核糖体诱导的稳定性调节背后的机制.
主要方法:
- 开发了一种基于质谱的方法,利用甲氨酸氧化作为折叠探针.
- 量化测量了核糖体新生链的全球以下折叠稳定性.
- 在可溶性和与核糖体结合的状态下分析了模型蛋白的折叠热力学 (dihydrofolate reductase,化学毒素蛋白Y,DNA聚合酶IV).
主要成果:
- 核糖体显著改变新生的多的折叠稳定性.
- 核糖体诱导的稳定性调制在不同的折叠域中有所不同.
- 调制取决于局部电荷分布,并涉及与核糖体表面的静电相互作用.
结论:
- 建立了强大的蛋白质组方法来分析与核糖体结合的新生多的局部稳定性.
- 证明了核糖体可以调节蛋白质折叠热力学.
- 突出了静电相互作用在影响折叠的核糖体新生多相互作用中的作用.
相关概念视频
Ribosome Profiling
3.6K
Ribosome profiling or ribo-sequencing is a deep sequencing technique that produces a snapshot of active translation in a cell. It selectively sequences the mRNAs protected by ribosomes to get an insight into a cell’s translation landscape at any given point in time.
Applications of ribosome profiling
Ribosome profiling has many applications, including in vivo monitoring of translation inside a particular organ or tissue type and quantifying new protein synthesis levels.
The technique...
Applications of ribosome profiling
Ribosome profiling has many applications, including in vivo monitoring of translation inside a particular organ or tissue type and quantifying new protein synthesis levels.
The technique...
3.6K
Protein Folding
8.1K
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...
8.1K
Protein Folding Quality Check in the RER
3.7K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
3.7K
Bacterial Protein Maturation
36
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...
36
Protein Organization
138.5K
Overview
138.5K
Termination of Translation
25.5K
The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
25.5K


