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Chaperones Skp and SurA dynamically expand unfolded outer membrane protein X and synergistically disassemble oligomeric aggregates

View ORCID ProfileNeharika Chamachi, View ORCID ProfileAndreas Hartmann, Mai Quynh Ma, View ORCID ProfileGeorg Krainer, View ORCID ProfileMichael Schlierf
doi: https://doi.org/10.1101/2021.02.23.432414
Neharika Chamachi
1B CUBE – Center for Molecular Bioengineering, TU Dresden, Tatzberg 41, 01307 Dresden, Germany
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  • ORCID record for Neharika Chamachi
Andreas Hartmann
1B CUBE – Center for Molecular Bioengineering, TU Dresden, Tatzberg 41, 01307 Dresden, Germany
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Mai Quynh Ma
1B CUBE – Center for Molecular Bioengineering, TU Dresden, Tatzberg 41, 01307 Dresden, Germany
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Georg Krainer
1B CUBE – Center for Molecular Bioengineering, TU Dresden, Tatzberg 41, 01307 Dresden, Germany
2Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW Cambridge, UK
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  • For correspondence: gk422@cam.ac.uk michael.schlierf@tu-dresden.de
Michael Schlierf
1B CUBE – Center for Molecular Bioengineering, TU Dresden, Tatzberg 41, 01307 Dresden, Germany
3Cluster of Excellence Physics of Life, TU Dresden, 01062 Dresden, Germany
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  • For correspondence: gk422@cam.ac.uk michael.schlierf@tu-dresden.de
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Abstract

Periplasmic chaperones Skp and SurA are essential players in outer membrane protein (OMP) biogenesis. They prevent unfolded OMPs from misfolding during their passage through the periplasmic space and aid in the disassembly of OMP aggregates under cellular stress conditions. However, functionally important links between interaction mechanisms, structural dynamics, and energetics that underpin both Skp and SurA association with OMPs have remained largely unresolved. Here, using single-molecule fluorescence spectroscopy, we dissect the conformational dynamics and thermodynamics of Skp and SurA binding to unfolded OmpX, and explore their disaggregase activities. We show that both chaperones expand unfolded OmpX distinctly and induce microsecond chain reconfigurations in the client OMP structure. We further reveal that Skp and SurA bind their substrate in a fine-tuned thermodynamic process via enthalpy–entropy compensation. Finally, we observed synergistic activity of both chaperones in the disaggregation of oligomeric OmpX aggregates. Our findings provide an intimate view into the multi-faceted functionalities of Skp and SurA and the fine-tuned balance between conformational flexibility and underlying energetics in aiding chaperone action during OMP biogenesis.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC 4.0 International license.
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Posted February 23, 2021.
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Chaperones Skp and SurA dynamically expand unfolded outer membrane protein X and synergistically disassemble oligomeric aggregates
Neharika Chamachi, Andreas Hartmann, Mai Quynh Ma, Georg Krainer, Michael Schlierf
bioRxiv 2021.02.23.432414; doi: https://doi.org/10.1101/2021.02.23.432414
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Chaperones Skp and SurA dynamically expand unfolded outer membrane protein X and synergistically disassemble oligomeric aggregates
Neharika Chamachi, Andreas Hartmann, Mai Quynh Ma, Georg Krainer, Michael Schlierf
bioRxiv 2021.02.23.432414; doi: https://doi.org/10.1101/2021.02.23.432414

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