EF-P对于含有连续林残留物的蛋白质的快速合成至关重要
Lili K Doerfel1, Ingo Wohlgemuth, Christina Kothe
1Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Goettingen, Germany.
概括
延长因子P (EF-P) 防止在富含プロ林蛋白的蛋白质合成过程中发生核糖体停滞. 它的翻译后修饰增强了这种功能,这对于所有细胞中的蛋白质合成至关重要.
科学领域:
- 分子生物学分子生物学
- 蛋白质合成 蛋白质合成
- 生物化学 生物化学
背景情况:
- 延长因子P (EF-P) 是一种转化因子,具有多种细胞作用.
- 它在蛋白质合成中的确切功能在很大程度上是未知的.
研究的目的:
- 阐明EF-P在蛋白质合成中的功能.
- 研究EF-P在克服核糖体停滞中的作用.
主要方法:
- 利用自然和工程模型蛋白质与连续的プロ林序列.
- 研究了EF-P对键形成和tRNA稳定性的影响.
- 分析了EF-P翻译后修改的影响.
主要成果:
- 通过EF-P,可以防止蛋白质与proline延伸 (例如,PPG,PPP) 的合成过程中的核糖体停滞.
- EF-P增强了键的形成,并稳定了基-tRNA.
- 用基化β-lysine对EF-P的翻译后修改增加了它的核糖体亲和力和催化效率.
结论:
- EF-P对于合成含有proline延伸的蛋白质至关重要.
- EF-P及其同类物eIF5A对所有细胞中的蛋白质合成至关重要.
相关概念视频
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
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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
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Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
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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.
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