Interaction of heat shock protein 90 B1 (Hsp90B1) with liposome reveals its potential role in protection the integrity of lipid membranes
Interaction of heat shock protein 90 B1 (Hsp90B1) with liposome reveals its potential role in protection the integrity of lipid membranes
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热休克蛋白 90 B1 (Hsp90B1) 与脂质体的相互作用揭示了其在保护脂质膜完整性方面的潜在作用
DOI：
10.1016/j.ijbiomac.2017.08.121
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发表时间：
2018-01-01
影响因子：
8.2
通讯作者：
Wang, Daoying
中科院分区：
文献类型：
--
作者：
Li, Pengpeng;Zhang, Muhan;Wang, Daoying
90 kDa的热休克蛋白（Hsp90）是维持蛋白质内稳态所必需的分子伴侣。除了伴侣活性外，Hsp90在细胞膜上还表现出其他细胞功能，然而它如何与细胞膜相互作用仍然不清楚。我们在此报道Hsp90B1与磷脂膜相互作用。我们首先从绿头鸭（Anas platyrhynchos）中克隆了Hsp90B1的全长开放阅读框（ApHsp90B1），然后对该基因进行异源表达和纯化。表面等离子体共振（SPR）分析表明，纯化的ApHsp90B1以高亲和力（解离常数KD为176 ± 25 nM）与磷脂膜相互作用，并且这种相互作用在较宽的pH范围内发生，在酸性条件下尤为明显。色氨酸荧光和远紫外圆二色谱研究发现，ApHsp90B1与磷脂膜的相互作用诱导了色氨酸残基微环境的改变以及ApHsp90B1某些区域的构象变化，这可能是添加磷脂囊泡后其ATP酶活性增加的原因。重要的是，ApHsp90B1与磷脂囊泡的相互作用显著降低了膜磷脂的脂解作用，这表明Hsp90B1与膜的相互作用能够保持膜的完整性。因此，本研究首次证明Hsp90B1对磷脂膜具有高亲和力，并表明Hsp90B1通过其与膜磷脂的相互作用在稳定膜方面发挥重要作用。（C）2017爱思唯尔有限公司。保留所有权利。
Heat shock proteins of 90 kDa (Hsp90) are molecular chaperones essential for protein homeostasis. Besides chaperone activity, Hsp90 exhibits other cellular functions at membranes, yet how it interacts with membranes remains elusive. We report here that Hsp90B1 interacts with phospholipid membranes. We first cloned the full-length open reading frame of Hsp90B1 from Anas platyrhnchos (ApHsp90B1), and the gene was then heterologously expressed and purified. SPR analysis show the purified ApHsp90B1 interacts with phospholipid membranes with high affinity (K-D 176 +/- 25 nM), and the interaction occurs over a wide range of pH, which is especially distinct under acidic conditions. Tryptophan fluorescence and far-UV CD spectra studies find that the interaction of ApHsp90B1 with phospholipid membrane induces microenvironment changes of tryptophan residues and conformational change of some regions in ApHsp90B1, which might be the reason of its increased ATPase activity upon addition phospholipid vesicles. Importantly, the interaction of ApHsp90B1 with phospholipid vesicles significantly reduces lipolysis of the membrane phospholipid, suggesting that the interaction of Hsp90B1 with membrane could preserve membrane integrity. The present study therefore demonstrates for the first time that Hsp90B1 exhibits high affinity for phospholipid membrane and suggest Hsp90B1 play an important role in membrane-stabilizing via its interaction with membrane phospholipids. (C) 2017 Elsevier B.V. All rights reserved.