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Local unfolding of the HSP27 monomer regulates chaperone activity
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Local unfolding of the HSP27 monomer regulates chaperone activity
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Journal Article
Local unfolding of the HSP27 monomer regulates chaperone activity
2019
Overview
The small heat-shock protein HSP27 is a redox-sensitive molecular chaperone that is expressed throughout the human body. Here, we describe redox-induced changes to the structure, dynamics, and function of HSP27 and its conserved α-crystallin domain (ACD). While HSP27 assembles into oligomers, we show that the monomers formed upon reduction are highly active chaperones in vitro, but are susceptible to self-aggregation. By using relaxation dispersion and high-pressure nuclear magnetic resonance (NMR) spectroscopy, we observe that the pair of β-strands that mediate dimerisation partially unfold in the monomer. We note that numerous HSP27 mutations associated with inherited neuropathies cluster to this dynamic region. High levels of sequence conservation in ACDs from mammalian sHSPs suggest that the exposed, disordered interface present in free monomers or oligomeric subunits may be a general, functional feature of sHSPs.
The small heat-shock protein HSP27 occurs predominantly in oligomeric forms, which makes its structural characterisation challenging. Here the authors employ CPMG and high-pressure NMR with native mass spectrometry and biophysical assays to show that the active monomeric form of HSP27 is substantially disordered and highly chaperone-active.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 140/131
/ 147/28
/ 82/58
/ HSP27 Heat-Shock Proteins - chemistry
/ HSP27 Heat-Shock Proteins - genetics
/ HSP27 Heat-Shock Proteins - metabolism
/ Humanities and Social Sciences
/ Monomers
/ Mutation
/ NMR
/ Nuclear Magnetic Resonance, Biomolecular
/ Peripheral Nervous System Diseases - genetics
/ Protein Aggregation, Pathological - genetics
/ Protein Conformation, beta-Strand - genetics
/ Protein Multimerization - genetics
/ Protein Structure, Quaternary - physiology
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - genetics
/ Recombinant Proteins - metabolism
/ Science
