Nucleation and growth of a bacterial functional amyloid at single-fiber resolution
| Autor: | Claire Valotteau, Yves F. Dufrêne, Han Remaut, Imke Van den Broeck, Nani Van Gerven, Wim Jonckheere, Cécile Feuillie, Mike Sleutel |
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| Přispěvatelé: | Vrije Universiteit Brussel (VUB), Université Catholique de Louvain = Catholic University of Louvain (UCL), Department of Bio-engineering Sciences, Structural Biology Brussels, Faculty of Sciences and Bioengineering Sciences, Cellular Processes governed by protein conformational changes |
| Jazyk: | angličtina |
| Předmět: |
0301 basic medicine
Amyloid Amyloid/chemistry Escherichia coli/chemistry nucleation [PHYS.PHYS.PHYS-BIO-PH]Physics [physics]/Physics [physics]/Biological Physics [physics.bio-ph] Single fiber Nucleation macromolecular substances Fibril curli Article biofilm 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Bacterial Proteins/chemistry mental disorders Escherichia coli Molecular Biology Atomic force microscopy Resolution (electron density) functional amyloid Cell Biology Amyloid fibril [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology Crystallography 030104 developmental biology Monomer chemistry Biophysics high-speed AFM |
| Zdroj: | Nature Chemical Biology Nature Chemical Biology, Nature Publishing Group, 2017, 13 (8), pp.902-908. ⟨10.1038/nchembio.2413⟩ Nature chemical biology |
| ISSN: | 1552-4469 1552-4450 |
| DOI: | 10.1038/nchembio.2413 |
| Popis: | International audience; Curli are functional amyloids produced by proteobacteria like Escherichia coli, as part of the extracellular matrix that holds cells together into biofilms. The molecular events during curli nucleation and fiber extension remain largely unknown. Combining observations from curli amyloidogenesis in bulk solutions with real-time in situ nanoscopic imaging at the single fiber level, we show that curli display polar growth, and detect two kinetic regimes of fiber elongation. Single fibers exhibit stop-and-go dynamics characterized by bursts of steady-state growth alternated with periods of stagnation. At high subunit concentrations fibers show constant, unperturbed burst growth. Curli follow a one-step nucleation process, where monomers contemporaneously fold and oligomerize into minimal fiber units that have growth characteristics identical to the mature fibrils. Kinetic data and interaction studies of curli fibrillation in the presence of the natural inhibitor CsgC show the inhibitor binds curli fibers and predominantly acts at the level of fiber elongation. Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use |
| Databáze: | OpenAIRE |
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