Journal
FEBS OPEN BIO
Volume 10, Issue 10, Pages 2081-2088Publisher
WILEY
DOI: 10.1002/2211-5463.12957
Keywords
IbpB; photo-crosslinking; small heat shock proteins; substrate binding; unnatural amino acid
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Funding
- National Natural Science Foundation of China [81300930, 41871095]
- Natural Science Foundation of Jiangsu Province [BK20130232]
- Scientific Research Foundation for the Talents by Xuzhou Medical University [D2012005]
- Qing Lan Project of Jiangsu Province
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Small heat shock proteins (sHSPs) are known to bind non-native substrates and prevent irreversible aggregation in an ATP-independent manner. However, the dynamic interaction between sHSPs and their substratesin vivois less studied. Here, by utilizing a genetically incorporated crosslinker, we characterized the interaction between sHSP IbpB and its endogenous substrates in living cells. Through photo-crosslinking analysis of five Bpa variants of IbpB, we found that the substrate binding of IbpB in living cells is reversible upon short-time exposure at 50 degrees C. Our data providein vivoevidence that IbpB engages in dynamic substrate release under nonstress conditions and suggest that photo-crosslinking may be a suitable method for investigating dynamic interaction between molecular chaperones and their substrates in living cells.
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