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周质伴侣蛋白:外膜生物发生与 envelope stress。

Periplasmic Chaperones: Outer Membrane Biogenesis and Envelope Stress.

机构信息

Department of Molecular Biology, Princeton University, Princeton, New Jersey, USA; email:

出版信息

Annu Rev Microbiol. 2024 Nov;78(1):191-211. doi: 10.1146/annurev-micro-041522-102901. Epub 2024 Nov 7.

DOI:10.1146/annurev-micro-041522-102901
PMID:39008906
Abstract

Envelope biogenesis and homeostasis in gram-negative bacteria are exceptionally intricate processes that require a multitude of periplasmic chaperones to ensure cellular survival. Remarkably, these chaperones perform diverse yet specialized functions entirely in the absence of external energy such as ATP, and as such have evolved sophisticated mechanisms by which their activities are regulated. In this article, we provide an overview of the predominant periplasmic chaperones that enable efficient outer membrane biogenesis and envelope homeostasis in . We also discuss stress responses that act to combat unfolded protein stress within the cell envelope, highlighting the periplasmic chaperones involved and the mechanisms by which envelope homeostasis is restored.

摘要

革兰氏阴性菌的信封生物发生和动态平衡是极其复杂的过程,需要多种周质伴侣来确保细胞存活。值得注意的是,这些伴侣在完全没有外部能量(如 ATP)的情况下执行着不同但专门的功能,因此它们已经进化出了复杂的调节机制。在本文中,我们概述了主要的周质伴侣,这些伴侣使有效外膜生物发生和信封动态平衡成为可能。我们还讨论了对抗细胞信封内未折叠蛋白应激的应激反应,突出了涉及的周质伴侣以及恢复信封动态平衡的机制。

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本文引用的文献

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FkpA enhances membrane protein folding using an extensive interaction surface.FkpA 通过广泛的相互作用表面增强膜蛋白折叠。
Protein Sci. 2023 Apr;32(4):e4592. doi: 10.1002/pro.4592.
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Cracking outer membrane biogenesis.破解外膜生物发生。
Biochim Biophys Acta Mol Cell Res. 2023 Feb;1870(2):119405. doi: 10.1016/j.bbamcr.2022.119405. Epub 2022 Nov 29.
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Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding.周质伴侣蛋白 SurA 与 BAM 复合物在外膜蛋白折叠中的动态相互作用。
Architecture and conformational dynamics of the BAM-SurA holo insertase complex.
BAM-SurA全酶插入酶复合物的结构与构象动力学
Sci Adv. 2025 Apr 4;11(14):eads6094. doi: 10.1126/sciadv.ads6094.
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Treponema denticola major surface protein (Msp): a key player in periodontal pathogenicity and immune evasion.齿垢密螺旋体主要表面蛋白(Msp):牙周致病性和免疫逃逸中的关键因子。
Arch Microbiol. 2025 Jan 18;207(2):36. doi: 10.1007/s00203-024-04223-w.
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Outer membrane lipoproteins: late to the party, but the center of attention.外膜脂蛋白:姗姗来迟,但备受关注。
J Bacteriol. 2025 Jan 31;207(1):e0044224. doi: 10.1128/jb.00442-24. Epub 2024 Dec 13.
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Breaking Barriers: Exploiting Envelope Biogenesis and Stress Responses to Develop Novel Antimicrobial Strategies in Gram-Negative Bacteria.突破障碍:利用包膜生物发生和应激反应开发针对革兰氏阴性菌的新型抗菌策略
Pathogens. 2024 Oct 11;13(10):889. doi: 10.3390/pathogens13100889.
Commun Biol. 2022 Jun 8;5(1):560. doi: 10.1038/s42003-022-03502-w.
4
Chaperones Skp and SurA dynamically expand unfolded OmpX and synergistically disassemble oligomeric aggregates.伴侣蛋白 Skp 和 SurA 动态扩展未折叠的 OmpX 并协同解聚寡聚体聚集物。
Proc Natl Acad Sci U S A. 2022 Mar 1;119(9). doi: 10.1073/pnas.2118919119.
5
ATP-Independent Chaperones.不依赖ATP的分子伴侣
Annu Rev Biophys. 2022 May 9;51:409-429. doi: 10.1146/annurev-biophys-090121-082906. Epub 2022 Feb 15.
6
The sacrificial adaptor protein Skp functions to remove stalled substrates from the β-barrel assembly machine.衔接蛋白 Skp 作为一种牺牲蛋白,其功能是从β桶组装机器上移除失速的底物。
Proc Natl Acad Sci U S A. 2022 Jan 4;119(1). doi: 10.1073/pnas.2114997119.
7
Structural basis of DegP protease temperature-dependent activation.DegP蛋白酶温度依赖性激活的结构基础
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8
Physical properties of the bacterial outer membrane.细菌外膜的物理性质。
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9
Chaperone Spy Protects Outer Membrane Proteins from Folding Stress via Dynamic Complex Formation.伴侣蛋白 Spy 通过动态复合物形成保护外膜蛋白免受折叠应激。
mBio. 2021 Oct 26;12(5):e0213021. doi: 10.1128/mBio.02130-21. Epub 2021 Oct 5.
10
Edge-strand of BepA interacts with immature LptD on the β-barrel assembly machine to direct it to on- and off-pathways.BepA 的边缘链与β-桶组装机器上不成熟的 LptD 相互作用,将其引导至成环和非成环途径。
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