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Interaction of heat shock protein 90 B1 (Hsp90B1) with liposome reveals its potential role in protection the integrity of lipid membranes

文献类型： 外文期刊

作者： Li, Pengpeng 1 ; Zhang, Muhan 1 ; Zou, Ye 1 ; Sun, Zhilan 1 ; Sun, Chong 1 ; Geng, Zhiming 1 ; Xu, Weimin 1 ; Wang, Daoyi 1 ;

作者机构： 1.Jiangsu Acad Agr Sci, Inst Agr Prod Proc, Nanjing 210014, Jiangsu, Peoples R China

关键词： Heat shock protein;Hsp90;Phospholipid membrane;Interaction

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：6.953； 五年影响因子：6.737 ）

ISSN： 0141-8130

年卷期： 2018 年 106 卷

页码：

收录情况： SCI

摘要： 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.

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