Abstract:
:Heat shock proteins of 90kDa (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 (KD 176±25nM), 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.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Li P,Zhang M,Zou Y,Sun Z,Sun C,Geng Z,Xu W,Wang Ddoi
10.1016/j.ijbiomac.2017.08.121subject
Has Abstractpub_date
2018-01-01 00:00:00pages
1250-1257eissn
0141-8130issn
1879-0003pii
S0141-8130(17)32337-1journal_volume
106pub_type
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journal_title:International journal of biological macromolecules
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