Abstract

Amyloid is associated with debilitating human ailments including Alzheimer's and prion diseases. Biochemical, biophysical, and imaging analyses revealed that fibers produced by Escherichia coli called curli were amyloid. The CsgA curlin subunit, purified in the absence of the CsgB nucleator, adopted a soluble, unstructured form that upon prolonged incubation assembled into fibers that were indistinguishable from curli. In vivo, curli biogenesis was dependent on the nucleation-precipitation machinery requiring the CsgE and CsgF chaperone-like and nucleator proteins, respectively. Unlike eukaryotic amyloid formation, curli biogenesis is a productive pathway requiring a specific assembly machinery.

Keywords

BiogenesisAmyloid (mycology)Escherichia coliOperonProtein subunitChaperone (clinical)ChemistryCell biologyBiochemistryBiologyBiophysicsGene

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Publication Info

Year
2002
Type
article
Volume
295
Issue
5556
Pages
851-855
Citations
1248
Access
Closed

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Cite This

Matthew R. Chapman, Lloyd S. Robinson, Jerome S. Pinkner et al. (2002). Role of <i>Escherichia coli</i> Curli Operons in Directing Amyloid Fiber Formation. Science , 295 (5556) , 851-855. https://doi.org/10.1126/science.1067484

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DOI
10.1126/science.1067484