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 and Stephen Matthews ()
Additional contact information
Sarah L. Rouse: South Kensington Campus
William J. Hawthorne: South Kensington Campus
Jamie-Lee Berry: South Kensington Campus
Dror S. Chorev: University of Oxford
Sandra A. Ionescu: University of Oxford
Sebastian Lambert: Duke-NUS Medical School
Fisentzos Stylianou: South Kensington Campus
Wiebke Ewert: South Kensington Campus
Uma Mackie: South Kensington Campus
R. Marc L. Morgan: South Kensington Campus
Daniel Otzen: Aarhus University
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: South Kensington Campus
Stephen Matthews: South Kensington Campus

Nature Communications, 2017, vol. 8, issue 1, 1-13

Abstract: 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.

Date: 2017
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-017-00361-6 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00361-6

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-017-00361-6

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().