@article{rouse:2017:10.1038/s41467-017-00361-6,
author = {rouse, S and hawthorne and berry and Chorev, D and Ionescu, S and Lambert, S and Stylianou, F and Ewert, W and Mackie, U and Morgan and Otzen, D and Herbst, F-A and Nielsen, P and Dueholm, M and Bayley, H and Robinson, C and Hare, S and Matthews, S},
doi = {10.1038/s41467-017-00361-6},
journal = {Nature Communications},
title = {A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis},
url = {http://dx.doi.org/10.1038/s41467-017-00361-6},
volume = {8},
year = {2017}
}

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TY  - JOUR
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.
AU  - rouse,S
AU  - hawthorne
AU  - berry
AU  - Chorev,D
AU  - Ionescu,S
AU  - Lambert,S
AU  - Stylianou,F
AU  - Ewert,W
AU  - Mackie,U
AU  - Morgan
AU  - Otzen,D
AU  - Herbst,F-A
AU  - Nielsen,P
AU  - Dueholm,M
AU  - Bayley,H
AU  - Robinson,C
AU  - Hare,S
AU  - Matthews,S
DO  - 10.1038/s41467-017-00361-6
PY  - 2017///
SN  - 2041-1723
TI  - A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis
T2  - Nature Communications
UR  - http://dx.doi.org/10.1038/s41467-017-00361-6
UR  - http://hdl.handle.net/10044/1/49696
VL  - 8
ER  - 

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