Rouse, Sarah L, Hawthorne, William J, Berry, Jamie-Lee, Chorev, Dror S, Ionescu, Sandra A, Lambert, Sebastian, Stylianou, Fisentzos, Ewert, Wiebke, Mackie, Uma, Morgan, R Marc L, Otzen, Daniel, Herbst, Florian-Alexander, Nielsen, Per H, Dueholm, Morten, Bayley, Hagan, Robinson, Carol V, Hare, Stephen and Matthews, Stephen (2017) A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis. Nature Communications, 8 (1). a263 1-13. ISSN 2041-1723

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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.

Item Type:	Article
Schools and Departments:	School of Life Sciences > Biochemistry
Depositing User:	Stephen Hare
Date Deposited:	21 Sep 2017 15:30
Last Modified:	14 Aug 2020 09:30
URI:	http://sro.sussex.ac.uk/id/eprint/70269

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