ArticleScientific reports2020
NMR insights into the pre-amyloid ensemble and secretion targeting of the curli subunit CsgA.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 20 citations in OpenAlex.
- CsgA gatekeeper residues control nucleation but not stability of functional amyloid.Protein science : a publication of the Protein Society · 2024Article
- Structural Analysis of Proteins from Bacterial Secretion Systems and Their Assemblies by NMR Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Functional Bacterial Amyloids: Understanding Fibrillation, Regulating Biofilm Fibril Formation and Organizing Surface Assemblies.Molecules (Basel, Switzerland) · 2022Review
- Functional amyloids from bacterial biofilms - structural properties and interaction partners.Chemical science · 2022Review
- Chaperones mainly suppress primary nucleation during formation of functional amyloid required for bacterial biofilm formation.Chemical science · 2022Article
- CRISPRiFrontiers in nutrition · 2022Article
- Variability of Amyloid Propensity in Imperfect Repeats of CsgA Protein ofInternational journal of molecular sciences · 2021Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The biofilms of Enterobacteriaceae are fortified by assembly of curli amyloid fibres on the cell surface. Curli not only provides structural reinforcement, but also facilitates surface adhesion. To prevent toxic intracellular accumulation of amyloid precipitate, secretion of the major curli subunit, CsgA, is tightly regulated. In this work, we have employed solution state NMR spectroscopy to characterise the structural ensemble of the pre-fibrillar state of CsgA within the bacterial periplasm, and upon recruitment to the curli pore, CsgG, and the secretion chaperone, CsgE. We show that the N-terminal targeting sequence (N) of CsgA binds specifically to CsgG and that its subsequent sequestration induces a marked transition in the conformational ensemble, which is coupled to a preference for CsgE binding. These observations lead us to suggest a sequential model for binding and structural rearrangement of CsgA at the periplasmic face of the secretion machinery.
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Registered trials
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