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首页> 外文期刊>FEBS Open Bio >Functional and structural characterization of HspB1/Hsp27 from Chinese hamster ovary cells
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Functional and structural characterization of HspB1/Hsp27 from Chinese hamster ovary cells

机译：中国仓鼠卵巢细胞HspB1 / Hsp27的功能和结构表征

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摘要

Small heat shock proteins (sHsps) endow cells with stress tolerance. Of the various sHsps in mammals, HspB1, also known as Hsp27, is the most ubiquitous. To examine the structure and function of HspB1, we expressed, purified, and characterized HspB1 from Chinese hamster ( Cricetulus?griseus ) ovary cells (CgHspB1). CgHspB1 forms a large oligomeric structure. We observed a monodisperse 16‐mer with an elongated sphere, but this is affected by changes in various conditions, including temperature. Under dilute conditions, CgHspB1 dissociates into small oligomers at elevated temperatures. The dissociated conformers interacted with the gel filtration column through hydrophobic interactions. In contrast, dissociation of the oligomer was not observed by small‐angle X‐ray scattering at 55?°C. The result partially coincides with the results of size exclusion chromatography, showing that dissociation did not occur at high protein concentrations. However, a significant structural change in the oligomeric conformations appears to occur between room and higher temperatures. Reflecting their status as homeotherms, mammalian sHsps are regulated by phosphorylation. A phosphorylation mimic mutant of CgHspB1 with the replacement of Ser15 to Asp exhibited relatively lower oligomer stability and greater protective ability against thermal aggregation than the wild‐type protein. The result clearly shows a correlation between oligomer dissociation and chaperone activity.
机译：小型热激蛋白（sHsps）使细胞具有压力耐受性。在哺乳动物的各种sHsps中，HspB1（也称为Hsp27）是最普遍的。为了检查HspB1的结构和功能，我们从中国仓鼠（Cricetulus？griseus）卵巢细胞（CgHspB1）中表达，纯化和鉴定了HspB1。 CgHspB1形成大的寡聚结构。我们观察到具有分散球体的16聚体单分散体，但这受各种条件（包括温度）变化的影响。在稀释条件下，CgHspB1在升高的温度下会分解成小的低聚物。解离的构象异构体通过疏水相互作用与凝胶过滤柱相互作用。相反，在55°C下通过小角度X射线散射未观察到低聚物的解离。该结果与尺寸排阻色谱法的结果部分吻合，表明在高蛋白浓度下不会发生解离。但是，在室温和较高温度之间，似乎发生了低聚物构象的重大结构变化。哺乳动物sHsps反映了它们作为等温线的状态，受到磷酸化作用的调节。与野生型蛋白相比，CgHspB1的磷酸化模拟突变体将Ser15替换为Asp表现出相对较低的低聚物稳定性和更高的抗热聚集能力。结果清楚地表明低聚物解离与分子伴侣活性之间的相关性。

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