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

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A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis. / 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; Matthews, Stephen.

I: Nature Communications, Bind 8, Nr. 1, 263, 2017.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

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

APA

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), [263]. https://doi.org/10.1038/s41467-017-00361-6

CBE

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. 8(1):Article 263. https://doi.org/10.1038/s41467-017-00361-6

MLA

Vancouver

Rouse SL, Hawthorne WJ, Berry J-L, Chorev DS, Ionescu SA, Lambert S o.a. A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis. Nature Communications. 2017;8(1). 263. https://doi.org/10.1038/s41467-017-00361-6

Author

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 ; Matthews, Stephen. / A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis. I: Nature Communications. 2017 ; Bind 8, Nr. 1.

Bibtex

@article{6a46df8ede7f4afa8beb1b20cbb3cb54,
title = "A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis",
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.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.",
keywords = "Journal Article",
author = "Rouse, {Sarah L} and Hawthorne, {William J} and Jamie-Lee Berry and Chorev, {Dror S} and Ionescu, {Sandra A} and Sebastian Lambert and Fisentzos Stylianou and Wiebke Ewert and Uma Mackie and Morgan, {R Marc L} and Daniel Otzen and Florian-Alexander Herbst and Nielsen, {Per H} and Morten Dueholm and Hagan Bayley and Robinson, {Carol V} and Stephen Hare and Stephen Matthews",
year = "2017",
doi = "10.1038/s41467-017-00361-6",
language = "English",
volume = "8",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",
number = "1",

}

RIS

TY - JOUR

T1 - A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis

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

PY - 2017

Y1 - 2017

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.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.

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.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.

KW - Journal Article

U2 - 10.1038/s41467-017-00361-6

DO - 10.1038/s41467-017-00361-6

M3 - Journal article

C2 - 28811582

VL - 8

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

M1 - 263

ER -