Role of Escherichia coli curli operons in directing amyloid fiber formation

Science. 2002 Feb 1;295(5556):851-5. doi: 10.1126/science.1067484.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adhesins, Bacterial / chemistry
  • Adhesins, Bacterial / genetics
  • Adhesins, Bacterial / metabolism
  • Adhesins, Bacterial / ultrastructure
  • Amyloid / chemistry
  • Amyloid / metabolism*
  • Amyloid / ultrastructure
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Bacterial Proteins / ultrastructure
  • Biopolymers
  • Circular Dichroism
  • Congo Red / metabolism
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism*
  • Escherichia coli Proteins / ultrastructure
  • Mutation
  • Operon*
  • Protein Structure, Secondary
  • Protein Subunits

Substances

  • Adhesins, Bacterial
  • Amyloid
  • Bacterial Proteins
  • Biopolymers
  • CsgB protein, E coli
  • Escherichia coli Proteins
  • Protein Subunits
  • csgA protein, E coli
  • Crl protein, Bacteria
  • Congo Red