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A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis

DOI: 10.1038/s41467-017-00361-6 DOI Help

Authors: Sarah L. Rouse (Imperial College London) , William J. Hawthorne (Imperial College London) , Jamie-lee Berry (Imperial College London) , Dror S. Chorev (University of Oxford) , Sandra A. Ionescu (University of Oxford) , Sebastian Lambert (Imperial College London) , Fisentzos Stylianou (Imperial College London) , Wiebke Ewert (Imperial College London) , Uma Mackie (Imperial College London) , R. Marc L. Morgan (Imperial College London) , Daniel Otzen (Aarhus University) , Florian-alexander Herbst (Aalborg University) , Per H. Nielsen (Aalborg University) , Morten Dueholm (Aalborg University) , Hagan Bayley (University of Oxford) , Carol V. Robinson (University of Oxford) , Stephen Hare (Imperial College London) , Stephen Matthews (Imperial College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 8

State: Published (Approved)
Published: August 2017
Diamond Proposal Number(s): 12579

Open Access Open Access

Abstract: Gram-negative bacteria possess specialised biogenesis machineries that facilitate the export of amyloid subunits for construction of a biofilm matrix. The secretion of bacterial functional amyloid requires a bespoke outer-membrane protein channel through which unfolded amyloid substrates are translocated. Here, we combine X-ray crystallography, native mass spectrometry, single-channel electrical recording, molecular simulations and circular dichroism measurements to provide high-resolution structural insight into the functional amyloid transporter from Pseudomonas, FapF. FapF forms a trimer of gated β-barrel channels in which opening is regulated by a helical plug connected to an extended coil-coiled platform spanning the bacterial periplasm. Although FapF represents a unique type of secretion system, it shares mechanistic features with a diverse range of peptide translocation systems. Our findings highlight alternative strategies for handling and export of amyloid protein sequences.

Journal Keywords: Biofilms; Membrane proteins; X-ray crystallography

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography

Documents:
s41467-017-00361-6.pdf