A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis
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.
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Nature Portfolio
2017
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oai:doaj.org-article:afb451a29eaf4948a6eaf6a24df043392021-12-02T10:48:19ZA new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis10.1038/s41467-017-00361-62041-1723https://doaj.org/article/afb451a29eaf4948a6eaf6a24df043392017-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-00361-6https://doaj.org/toc/2041-1723Gram-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.Sarah L. RouseWilliam J. HawthorneJamie-Lee BerryDror S. ChorevSandra A. IonescuSebastian LambertFisentzos StylianouWiebke EwertUma MackieR. Marc L. MorganDaniel OtzenFlorian-Alexander HerbstPer H. NielsenMorten DueholmHagan BayleyCarol V. RobinsonStephen HareStephen MatthewsNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-13 (2017) |
| institution |
DOAJ |
| collection |
DOAJ |
| language |
EN |
| topic |
Science Q |
| spellingShingle |
Science Q 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 A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis |
| description |
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. |
| format |
article |
| author |
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 |
| author_facet |
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 |
| author_sort |
Sarah L. Rouse |
| title |
A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis |
| title_short |
A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis |
| title_full |
A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis |
| title_fullStr |
A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis |
| title_full_unstemmed |
A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis |
| title_sort |
new class of hybrid secretion system is employed in pseudomonas amyloid biogenesis |
| publisher |
Nature Portfolio |
| publishDate |
2017 |
| url |
https://doaj.org/article/afb451a29eaf4948a6eaf6a24df04339 |
| work_keys_str_mv |
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1718396668235218944 |