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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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During mitosis, chromosome movements occur through the interplay of multiple piconewton level forces. In prometaphase, these forces help in chromosome assembly or congression at the equatorial plane, eventually leading to their alignment at the metaphase plate. The forces acting on the chromosomes are space and time-dependent; therefore, they vary with the position of the chromosomes as the cell progresses through mitosis. 
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The spindle assembly checkpoint is a molecular surveillance mechanism ensuring the fidelity of chromosome segregation during anaphase. The checkpoint monitors the completion of all the prerequisite steps before chromosome segregation to determine whether the segregation process should proceed or be delayed.
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Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions
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Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

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驱使护士行动的力量

Philipp Koldewey1, Frederick Stull1, Scott Horowitz1

  • 1Department of Molecular, Cellular and Developmental Biology, and the Howard Hughes Medical Institute, University of Michigan, Ann Arbor, MI 48109, USA.

Cell
|June 14, 2016
PubMed
概括
此摘要是机器生成的。

像Spy这样的分子伴侣使用静电力, 不仅仅是疏水性相互作用, 结合和折叠像Im7这样的客户蛋白. 这种机制允许陪伴者在没有特定指令的情况下协助各种蛋白质折叠.

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Detection of the pH-dependent Activity of Escherichia coli Chaperone HdeB In Vitro and In Vivo
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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells
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相关实验视频

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科学领域:

  • 分子生物学
  • 生物物理
  • 蛋白质折叠

背景情况:

  • 准确的分子力量控制的陪伴者介导蛋白质折叠仍然不完全理解.
  • 护手是细胞机械的重要组成部分,有助于蛋白质折叠,防止聚合和错误折叠.

研究的目的:

  • 阐明分子力量的详细机制,驱动伴侣-客户互动的四个关键步骤:结合,稳定,折叠和释放.
  • 挑战目前普遍存在的观点,即护卫者主要通过恐水相互作用来识别未折叠的蛋白质.

主要方法:

  • 研究了模型护航者Spy及其展开的客户端蛋白质Im7.
  • 分析了陪伴者与客户互动的不同阶段,重点关注每一步所涉及的力量.

主要成果:

  • 与人们普遍认为的相反,Spy护送器利用远程静电相互作用,初步快速结合到未折叠的Im7客户端蛋白质.
  • 短距离的疏水相互作用稳定了伴侣-客户端复合体,随后是疏水崩导致客户端蛋白折叠.
  • 通过埋葬疏水性残留物,客户端蛋白质折叠降低了Spy的亲和力,促进释放并使其自我折叠.

结论:

  • 间陪伴者采用一种由静电相互作用启动的机制,其次是疏水稳定和客户驱动的折叠,导致释放.
  • 这种陪伴机制允许客户端蛋白质自我折叠,可以解释陪伴蛋白对各种无关蛋白质的广泛基质特异性.