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Conditional Disorder in Small Heat-shock Proteins

机译：小型热冲击蛋白的条件障碍

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Small heat-shock proteins (sHSPs) are molecular chaperones that respond to cellular stresses to combat protein aggregation. HSP27 is a critical human sHSP that forms large, dynamic oligomers whose quaternary structures and chaperone activities depend on environmental factors. Upon exposure to cellular stresses, such as heat shock or acidosis, HSP27 oligomers can dissociate into dimers and monomers, which leads to significantly enhanced chaperone activity. The structured core of the protein, the alpha-crystallin domain (ACD), forms dimers and can prevent the aggregation of substrate proteins to a similar degree as the full-length protein. When the ACD dimer dissociates into monomers, it partially unfolds and exhibits enhanced activity. Here, we used solution-state NMR spectroscopy to characterize the structure and dynamics of the HSP27 ACD monomer. Web show that the monomer is stabilized at low pH and that its backbone chemical shifts, N-15 relaxation rates, and H-1-N-15 residual dipolar couplings suggest structural changes and rapid motions in the region responsible for dimerization. By analyzing the solvent accessible and buried surface areas of sHSP structures in the context of a database of dimers that are known to dissociate into disordered monomers, we predict that ACD dimers from sHSPs across all kingdoms of life may partially unfold upon dissociation. We propose a general model in which conditional disorder-the partial unfolding of ACDs upon monomerization-is a common mechanism for sHSP activity. (C) 2020 Elsevier Ltd. All rights reserved.
机译：小型热休克蛋白（SHSP）是对抗蛋白质聚集的细胞应激的分子伴侣。 HSP27是一种关键的人SHSP，形成大型动态低聚物，其第四纪结构和伴侣活动取决于环境因素。在暴露于细胞应激后，例如热冲击或酸中毒，HSP27低聚物可以解离二聚体和单体，这导致显着增强的伴侣伴伴侣活性。蛋白质，α-晶域（ACD），形成二聚体的结构化核心，可以防止底物蛋白的聚集在与全长蛋白相似的程度。当ACD二聚体离解成单体时，它部分展开并表现出增强的活性。这里，我们使用解决方案 - 状态NMR光谱来表征HSP27 ACD单体的结构和动态。网表明单体在低pH下稳定，其骨干化学变换，N-15弛豫率和H-1-N-15残留的双极联轴器表明，负责二聚化的区域的结构变化和快速运动。通过分析在已知解离混乱的单体的二聚体数据库中的SHSP结构的溶剂可接近和掩埋表面区域，我们预测来自SHSP的ACD二聚体在所有王国范围内可能在解离时部分展开。我们提出了一种通用模型，其中有条件紊乱 - 单体化后ACD的部分展开 - 是SHSP活性的常见机制。 （c）2020 elestvier有限公司保留所有权利。

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