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A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis
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 translo...
Autores principales: | , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5557850/ https://www.ncbi.nlm.nih.gov/pubmed/28811582 http://dx.doi.org/10.1038/s41467-017-00361-6 |
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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 |
author_facet | 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 |
author_sort | Rouse, Sarah L. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5557850 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-55578502017-08-17 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 Nat Commun Article 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. Nature Publishing Group UK 2017-08-15 /pmc/articles/PMC5557850/ /pubmed/28811582 http://dx.doi.org/10.1038/s41467-017-00361-6 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article 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 |
title | 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_short | 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 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5557850/ https://www.ncbi.nlm.nih.gov/pubmed/28811582 http://dx.doi.org/10.1038/s41467-017-00361-6 |
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