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

Sarah L Rouse; William J Hawthorne; Jamie-Lee Berry; Dror S Chorev; Sandra A Ionescu; Sebastian Lambert; Fisentzos Stylianou; Wiebke Ewert; Uma Mackie; R Marc L Morgan; Daniel Otzen; Florian-Alexander Herbst; Per H Nielsen; Morten Dueholm; Hagan Bayley; Carol V Robinson; Stephen Hare; Stephen Matthews

doi:10.1038/s41467-017-00361-6

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

Sarah L Rouse, William J Hawthorne, Jamie-Lee Berry, Dror S Chorev, Sandra A Ionescu, Sebastian Lambert, Fisentzos Stylianou, Wiebke Ewert, Uma Mackie, R Marc L Morgan, Daniel Otzen, Florian-Alexander Herbst, Per H Nielsen, Morten Dueholm, Hagan Bayley, Carol V Robinson, Stephen Hare, Stephen Matthews

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

51 Citationer (Scopus)

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.

Originalsprog	Engelsk
Artikelnummer	263
Tidsskrift	Nature Communications
Vol/bind	8
Nummer	1
ISSN	2041-1723
DOI	https://doi.org/10.1038/s41467-017-00361-6
Status	Udgivet - 1 dec. 2017

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10.1038/s41467-017-00361-6Licens: CC BY

https://www.nature.com/articles/s41467-017-00361-6.pdfLicens: CC BY

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Rouse, S. L., Hawthorne, W. J., Berry, J.-L., Chorev, D. S., Ionescu, S. A., Lambert, S., Stylianou, F., Ewert, W., Mackie, U., Morgan, R. M. L., Otzen, D., Herbst, F.-A., Nielsen, P. H., Dueholm, M., Bayley, H., Robinson, C. V., Hare, S., & Matthews, S. (2017). A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis. Nature Communications, 8(1), Artikel 263. https://doi.org/10.1038/s41467-017-00361-6

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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.",

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Rouse, SL, Hawthorne, WJ, Berry, J-L, Chorev, DS, Ionescu, SA, Lambert, S, Stylianou, F, Ewert, W, Mackie, U, Morgan, RML, Otzen, D, Herbst, F-A, Nielsen, PH, Dueholm, M, Bayley, H, Robinson, CV, Hare, S & Matthews, S 2017, 'A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis', Nature Communications, bind 8, nr. 1, 263. https://doi.org/10.1038/s41467-017-00361-6

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AU - Rouse, Sarah L

AU - Hawthorne, William J

AU - Berry, Jamie-Lee

AU - Chorev, Dror S

AU - Ionescu, Sandra A

AU - Lambert, Sebastian

AU - Stylianou, Fisentzos

AU - Ewert, Wiebke

AU - Mackie, Uma

AU - Morgan, R Marc L

AU - Otzen, Daniel

AU - Herbst, Florian-Alexander

AU - Nielsen, Per H

AU - Dueholm, Morten

AU - Bayley, Hagan

AU - Robinson, Carol V

AU - Hare, Stephen

AU - Matthews, Stephen

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N2 - 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.

AB - 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.

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

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