CsgE is a curli secretion specificity factor that prevents amyloid fibre aggregation

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CsgE is a curli secretion specificity factor that prevents amyloid fibre aggregation.

Curli are extracellular amyloid fibres produced by Escherichia coli that are critical for biofilm formation and adhesion to biotic and abiotic surfaces. CsgA and CsgB are the major and minor curli subunits, respectively, while CsgE, CsgF and CsgG direct the extracellular localization and assembly of curli subunits into fibres. The secretion and stability of CsgA and CsgB are dependent on the ou...

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Secretion of curli fibre subunits is mediated by the outer membrane-localized CsgG protein.

Produced by many Enterobacteriaceae spp., curli are biologically important amyloid fibres that have been associated with biofilm formation, host cell adhesion and invasion, and immune system activation. CsgA is the major fibre subunit and CsgE, CsgF and CsgG are non-structural proteins involved in curli biogenesis. We have characterized the role of CsgG in curli subunit secretion across the out...

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Solution NMR structure of CsgE: Structural insights into a chaperone and regulator protein important for functional amyloid formation.

Curli, consisting primarily of major structural subunit CsgA, are functional amyloids produced on the surface of Escherichia coli, as well as many other enteric bacteria, and are involved in cell colonization and biofilm formation. CsgE is a periplasmic accessory protein that plays a crucial role in curli biogenesis. CsgE binds to both CsgA and the nonameric pore protein CsgG. The CsgG-CsgE com...

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Caf1A usher possesses a Caf1 subunit-like domain that is crucial for Caf1 fibre secretion.

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ژورنال

عنوان ژورنال: Molecular Microbiology

سال: 2011

ISSN: 0950-382X

DOI: 10.1111/j.1365-2958.2011.07706.x