大肠杆菌小热休克蛋白IbpB的寡聚物多分散性和寡聚物依赖性保持伴侣活性研究进展。

IF 3.3 3区 生物学 Q3 CELL BIOLOGY
Md Azaharuddin, Anabadya Pal, Sangeeta Mitra, Rakhi Dasgupta, Tarakdas Basu
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引用次数: 0

摘要

MW 16KDa的包涵体相关蛋白IbpA和IbpB是大肠杆菌的两种小的热休克蛋白(sHSPs),它们只具有保持而不具有折叠的伴侣活性。IbpB的体外保持酶活性高于IbpA,并且在组合中,它们具有协同作用。IbpA和IbpB单体首先形成均聚二聚体,其作为构建块随后低聚以制备具有MDa范围的MW的重低聚物;对于IbpB,重低聚物的MW范围为2.0-3.0 MDa,而对于IbpA低聚物,MDa中的值没有如此指定/报告。通过温度升高,IbpB的这种大的低聚物,但不是IbpA的低聚体,离解以制备约600-700KDa的MW的相对小的低聚器组件。IbpB的较大低聚物被认为是非活性储存形式,其在面临热或氧化应激时离解成具有ATP独立的保持伴侣活性的较小低聚物。这些较小的低聚物与应激诱导的部分变性/未折叠结合,从而成为聚集的蛋白质,使其免受永久性损伤和聚集。在压力消退时,IbpB将结合的底物蛋白转移到ATP依赖性双伴侣系统DnaKJE-ClpB,该系统具有保持酶和折叠酶特性,最终使蛋白重折叠。在大肠杆菌的两种sHSPs IbpA和IbpB中,本文仅介绍了IbpB的研究进展。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

A review on oligomeric polydispersity and oligomers-dependent holding chaperone activity of the small heat-shock protein IbpB of Escherichia coli.

A review on oligomeric polydispersity and oligomers-dependent holding chaperone activity of the small heat-shock protein IbpB of Escherichia coli.

Inclusion body-associated proteins IbpA and IbpB of MW 16 KDa are the two small heat-shock proteins (sHSPs) of Escherichia coli, and they have only holding, but not folding, chaperone activity. In vitro holdase activity of IbpB is more than that of IbpA, and in combination, they synergise. Both IbpA and IbpB monomers first form homodimers, which as building blocks subsequently oligomerize to make heavy oligomers with MW of MDa range; for IbpB, the MW range of heavy oligomers is 2.0-3.0 MDa, whereas for IbpA oligomers, the values in MDa are not so specified/reported. By temperature upshift, such large oligomers of IbpB, but not of IbpA, dissociate to make relatively small oligomeric assemblies of MW around 600-700KDa. The larger oligomers of IbpB are assumed to be inactive storage form, which on facing heat or oxidative stress dissociate into smaller oligomers of ATP-independent holding chaperone activity. These smaller oligomers bind with stress-induced partially denatured/unfolded and thereby going to be aggregated proteins, to give them protection against permanent damage and aggregation. On withdrawal of stress, IbpB transfers the bound substrate protein to the ATP-dependent bi-chaperone system DnaKJE-ClpB, having both holdase and foldase properties, to finally refold the protein. Of the two sHSPs IbpA and IbpB of E. coli, this review covers the recent advances in research on IbpB only.

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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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