Heirbaut, M, Lermyte, F, Martin, EM et al. (5 more authors) (2016) The preferential heterodimerization of human small heat shock proteins HSPB1 and HSPB6 is dictated by the N-terminal domain. Archives of Biochemistry and Biophysics, 610. pp. 41-50. ISSN 0003-9861
Abstract
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2016 Elsevier Inc. All rights reserved. This is an author produced version of a paper published in Archives of Biochemistry and Biophysics. Uploaded in accordance with the publisher's self-archiving policy. |
Keywords: | HSP20; HSP27; Heterooligomers; Native mass spectrometry; Chaperone; Small-angle x-ray scattering |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Biomedical Sciences (Leeds) The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Structural Molecular Biology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 16 Jan 2017 16:01 |
Last Modified: | 05 Oct 2017 20:52 |
Published Version: | https://doi.org/10.1016/j.abb.2016.10.002 |
Status: | Published |
Publisher: | Elsevier |
Identification Number: | 10.1016/j.abb.2016.10.002 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:110584 |