大肠杆菌小热休克蛋白 IbpB 的两种新寡聚体在热应激条件下表现出最大的保持伴侣活性

IF 3.5 4区生物学 Q1 Biochemistry, Genetics and Molecular Biology

FEBS Letters Pub Date : 2024-09-17 DOI:10.1002/1873-3468.15019

Md Azaharuddin, Rakhi Dasgupta, Abhijit Das, Susmita Nandi, Anabadya Pal, Soumajit Chakrabarty, Pathikrit Bandopadhyay, Sourav Ghosh, Sanchita Nandy, Upasana Sett, Tarakdas Basu

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引用次数: 0

摘要

大肠杆菌小型热休克蛋白 IbpB（分子量：16 KDa）具有保持伴侣蛋白的活性，在 30 °C时以两个分子量分别为 2.0-3.0 MDa 和 600-700 KDa 的大寡聚体存在于细胞中。我们在此报告了在 50 °C 热应激条件下细胞中存在的另外两个分子量分别为 400 和 130 KDa 的低聚物。这两种较小的低聚物具有最强的伴侣活性，这一点可以从单独的低聚物在 52 和 60 °C下分别抑制 L-乳酸脱氢酶失活和聚集的程度中观察到。这表明两种较大的低聚物是活性较差的贮存形式，在热应力作用下会部分解离成具有较高保持酶活性的较小低聚物。

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Two new oligomers of E. coli small heat‐shock protein IbpB identified under heat stress exhibit maximum holding chaperone activity

Escherichia coli small heat‐shock protein IbpB (MW: 16 KDa) has holding chaperone activity and is present in cells at 30 °C as two large oligomers of MW 2.0–3.0 MDa and 600–700 KDa. We report here about the presence of two additional oligomers of MW around 400 and 130 KDa in cells under heat‐stress at 50 °C. These two smaller oligomers possess the most chaperone activity, as observed from the extent of inhibition of inactivation and aggregation separately, of L‐Lactate dehydrogenase in the presence of the individual oligomers at 52 and 60 °C, respectively. It is suggested here that the two larger oligomers act as poorly active storage forms, which under heat stress dissociate partially into smaller oligomers with high holdase activity.

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来源期刊

FEBS Letters 生物-生化与分子生物学

CiteScore

7.00

自引率

2.90%

发文量

303

审稿时长

1.0 months

期刊介绍： FEBS Letters is one of the world''s leading journals in molecular biology and is renowned both for its quality of content and speed of production. Bringing together the most important developments in the molecular biosciences, FEBS Letters provides an international forum for Minireviews, Research Letters and Hypotheses that merit urgent publication.