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Science. 2002 Feb 1;295(5556):851-5.

Role of Escherichia coli curli operons in directing amyloid fiber formation.

Author information

1
Department of Molecular Microbiology and Microbial Pathogenesis, Box 8230, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.

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.

PMID:
11823641
PMCID:
PMC2838482
DOI:
10.1126/science.1067484
[Indexed for MEDLINE]
Free PMC Article

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