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相关概念视频

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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...
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DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart,...
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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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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.
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Updated: Sep 13, 2025

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触发因素加快了新生链条的紧缩和折叠.

Katharina Till1, Anne-Bart Seinen1, Florian Wruck1

  • 1AMOLF, Amsterdam 1098 XG, Netherlands.

Proceedings of the National Academy of Sciences of the United States of America
|July 25, 2025
PubMed
概括
此摘要是机器生成的。

触发因子伴侣加速新生的链条直接在核糖体上折叠. 这种共翻译折叠会影响蛋白质的组装和聚合.

关键词:
陪伴者 (chaperones) 是指一个陪伴者.光学子,一个光学子.蛋白质折叠 蛋白质的折叠核糖体是核糖体中的一个.

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科学领域:

  • 分子生物学分子生物学
  • 生物物理学的生物物理.

背景情况:

  • 在核糖体的新生链形状控制是不太了解.
  • 护航者通常远离核糖体起作用,但在翻译过程中会出现蛋白质折叠的挑战.

研究的目的:

  • 研究大肠杆菌伴侣触发因子 (TF) 在新生链在核糖体上的结构控制中的作用.
  • 阐明TF在翻译过程中影响蛋白质折叠的机制.

主要方法:

  • 选择性核糖体造型结合光学子和单分子光.
  • 使用二叶酸减少酶 (DHFR) 作为模型系统.

主要成果:

  • 触发因子 (TF) 已被证明可以加速在核糖体上新生的链条折叠.
  • 由于新生的链条折叠和崩,TF表现出短暂的扫描,随后是稳定的结合.
  • TF结合诱导新生的链崩,稳定部分折叠,压缩延长TF结合.
  • TF加速折叠取决于蛋白质结构至关重要的特定片的出现.

结论:

  • 触发因子在促进核糖体的共翻译折叠方面发挥着至关重要的作用.
  • 通过TF介导的折叠加速影响共翻译蛋白组合,聚合和翻译暂停.
  • 这些发现表明TF在整个生命中对蛋白质生物发生的重要性.