Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 610, Issue -, Pages 41-50Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2016.10.002
Keywords
HSP20; HSP27; Heterooligomers; Native mass spectrometry; Chaperone; Small-angle x-ray scattering
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Funding
- Research Foundation Flanders (FWO) [G093615N, WO03315N, 11L4115N]
- KU Leuven grant [OT13/097]
- Department of Pharmaceutical and Pharmacological Sciences, KU Leuven
- Hercules Foundation Flanders
- European Community's Seventh Framework Programme under BioStruct-X initiative [6131]
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Small heat shock proteins are ATP-independent molecular chaperones. Their function is to bind partially unfolded proteins under stress conditions. In vivo, members of this chaperone family are known to preferentially assemble together forming large, polydisperse heterooligomers. The exact molecular mechanisms that drive specific heteroassociation are currently unknown. Here we study the oligomers formed between human HSPB1 and HSPB6. Using small-angle X-ray scattering we could characterize two distinct heterooligomeric species present in solution. By employing native mass spectrometry we show that such assemblies are formed purely from heterodimeric building blocks, in line with earlier cross linking studies. Crucially, a detailed analysis of truncation variants reveals that the preferential association between these two sHSPs is solely mediated by their disordered N-terminal domains. (C) 2016 Elsevier Inc. All rights reserved.
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