Schiffrin, B, Machin, JM, Karamanos, TK orcid.org/0000-0003-2297-540X et al. (4 more authors) (2022) Dynamic interplay between the periplasmic chaperone SurA and the BAM complex in outer membrane protein folding. Communications Biology, 5. 560. ISSN 2399-3642
Abstract
Correct folding of outer membrane proteins (OMPs) into the outer membrane of Gram-negative bacteria depends on delivery of unfolded OMPs to the β-barrel assembly machinery (BAM). How unfolded substrates are presented to BAM remains elusive, but the major OMP chaperone SurA is proposed to play a key role. Here, we have used hydrogen deuterium exchange mass spectrometry (HDX-MS), crosslinking, in vitro folding and binding assays and computational modelling to show that the core domain of SurA and one of its two PPIase domains are key to the SurA-BAM interaction and are required for maximal catalysis of OMP folding. We reveal that binding causes changes in BAM and SurA conformation and/or dynamics distal to the sites of binding, including at the BamA β1-β16 seam. We propose a model for OMP biogenesis in which SurA plays a crucial role in OMP delivery and primes BAM to accept substrates for folding.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © The Author(s) 2022. This is an open access article under the terms of the Creative Commons Attribution License (CC-BY 4.0), which permits unrestricted use, distribution and reproduction in any medium, provided the original work is properly cited. |
Keywords: | Membrane structure and assembly, Structural biology |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Biomolecular Mass Spectroscopy (Leeds) The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Structural Molecular Biology (Leeds) |
Funding Information: | Funder Grant number BBSRC (Biotechnology & Biological Sciences Research Council) BB/T000635/1 BBSRC (Biotechnology & Biological Sciences Research Council) BB/P000037/1 BBSRC (Biotechnology & Biological Sciences Research Council) BB/N007603/1 |
Depositing User: | Symplectic Publications |
Date Deposited: | 24 May 2022 15:31 |
Last Modified: | 08 Nov 2023 12:32 |
Status: | Published |
Publisher: | Nature Research |
Identification Number: | 10.1038/s42003-022-03502-w |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:187124 |