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

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  • 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, Duke-NUS Medical School
  • ,
  • Fisentzos Stylianou, Imperial College London
  • ,
  • Wiebke Ewert, Imperial College London
  • ,
  • Uma Mackie, Imperial College London, Walthamstow School for Girls
  • ,
  • R Marc L Morgan, Imperial College London
  • ,
  • Daniel Otzen
  • 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

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.Gram-negative bacteria assemble biofilms from amyloid fibres, which translocate across the outer membrane as unfolded amyloid precursors through a secretion system. Here, the authors characterise the structural details of the amyloid transporter FapF in Pseudomonas.

OriginalsprogEngelsk
Artikelnummer263
TidsskriftNature Communications
Vol/bind8
Nummer1
ISSN2041-1723
DOI
StatusUdgivet - 2017

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