低温电子断层扫描技术证实了体外推断的伴侣素加速蛋白质重折叠的过时机制。

IF 3.3 3区 生物学 Q3 CELL BIOLOGY
Paolo De Los Rios, Mathieu E Rebeaud, Pierre Goloubinoff
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引用次数: 0

摘要

最近,一项关于整个细菌细胞中不同 GroEL-GroES 合子蛋白复合物群的优雅低温电子断层扫描研究(Wagner, Carvajal 等人,2024 年)有助于解决有关其机制的长期争论,并将三十年前的体外生化研究结果与新的、精细的原位观察结果相协调。使用纯化蛋白质的生物化学家经常怀疑,他们的研究结果是否忠实地反映了细胞拥挤环境中的情况,即他们的蛋白质与浓缩的代谢物混合在一起,并与细胞膜和成千上万种不同的无关蛋白质发生碰撞。在这里,低温电子断层扫描证实,仔细的体外蛋白质生物化学研究仍有广阔的前景。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
An outmoded in vitro-inferred mechanism for chaperonin-accelerated protein refolding is confirmed in cells by cryo-electron tomography.

A recent elegant cryo-electron tomography study of the populations of different GroEL-GroES chaperonins complexes in whole bacterial cells (Wagner, Carvajal et al. 2024) contributes to the resolution of a long-standing debate about their mechanism, and reconciles three-decade-old results from in vitro biochemical studies, with new, refined in situ observations. Biochemists working with purified proteins often wonder if their findings faithfully reflect the situation in the crowded environment of cells, when their proteins mingle with concentrated metabolites and bump into membranes and thousands of different unrelated proteins. Here, cryo-electron tomography confirmed that careful in vitro protein biochemistry research still has a bright future.

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来源期刊
Cell Stress & Chaperones
Cell Stress & Chaperones 生物-细胞生物学
CiteScore
7.60
自引率
2.60%
发文量
59
审稿时长
6-12 weeks
期刊介绍: Cell Stress and Chaperones is an integrative journal that bridges the gap between laboratory model systems and natural populations. The journal captures the eclectic spirit of the cellular stress response field in a single, concentrated source of current information. Major emphasis is placed on the effects of climate change on individual species in the natural environment and their capacity to adapt. This emphasis expands our focus on stress biology and medicine by linking climate change effects to research on cellular stress responses of animals, micro-organisms and plants.
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