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

Autor:	Rouse SL; Department of Life Sciences, Imperial College London, South Kensington Campus, London, SW72AZ, UK., Hawthorne WJ; Department of Life Sciences, Imperial College London, South Kensington Campus, London, SW72AZ, UK., Berry JL; Department of Life Sciences, Imperial College London, South Kensington Campus, London, SW72AZ, UK., Chorev DS; Chemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, UK., Ionescu SA; Chemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, UK., Lambert S; Duke-NUS Medical School, 8 College Road, Singapore, 169857, Singapore., Stylianou F; Department of Life Sciences, Imperial College London, South Kensington Campus, London, SW72AZ, UK., Ewert W; Department of Life Sciences, Imperial College London, South Kensington Campus, London, SW72AZ, UK., Mackie U; Department of Life Sciences, Imperial College London, South Kensington Campus, London, SW72AZ, UK.; Walthamstow School for Girls, London, E17 9RZ, UK., Morgan RML; Department of Life Sciences, Imperial College London, South Kensington Campus, London, SW72AZ, UK., Otzen D; Interdisciplinary Nanoscience Center (iNANO), Centre for Insoluble Protein Structures (inSPIN), Department of Molecular Biology and Genetics, Aarhus University, Aarhus C, Denmark., Herbst FA; Center for Microbial Communities, Department of Chemistry and Bioscience, Aalborg University, Aalborg, Denmark., Nielsen PH; Center for Microbial Communities, Department of Chemistry and Bioscience, Aalborg University, Aalborg, Denmark., Dueholm M; Center for Microbial Communities, Department of Chemistry and Bioscience, Aalborg University, Aalborg, Denmark., Bayley H; Chemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, UK., Robinson CV; Chemistry Research Laboratory, University of Oxford, Oxford, OX1 3TA, UK., Hare S; Department of Life Sciences, Imperial College London, South Kensington Campus, London, SW72AZ, UK., Matthews S; Department of Life Sciences, Imperial College London, South Kensington Campus, London, SW72AZ, UK. s.j.matthews@imperial.ac.uk.
Jazyk:	angličtina
Zdroj:	Nature communications [Nat Commun] 2017 Aug 15; Vol. 8 (1), pp. 263. Date of Electronic Publication: 2017 Aug 15.
DOI:	10.1038/s41467-017-00361-6
Abstrakt:	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.
Databáze:	MEDLINE
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