Role of Escherichia coli curli operons in directing amyloid fiber formation.
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.
Chapman
Matthew R
MR
Department of Molecular Microbiology and Microbial Pathogenesis, Box 8230, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.
Robinson
Lloyd S
LS
Pinkner
Jerome S
JS
Roth
Robyn
R
Heuser
John
J
Hammar
Marten
M
Normark
Staffan
S
Hultgren
Scott J
SJ
D018829:Adhesins, Bacterial / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D000682:Amyloid / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D001704:Biopolymers; D002942:Circular Dichroism; D003224:Congo Red / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D009154:Mutation; D009876:Operon; D017433:Protein Structure, Secondary; D021122:Protein Subunits
D018829:Adhesins, Bacterial; D000682:Amyloid; D001426:Bacterial Proteins; D001704:Biopolymers; C109182:CsgB protein, E coli; D029968:Escherichia coli Proteins; D021122:Protein Subunits; C489688:csgA protein, E coli; C077481:Crl protein, Bacteria; D003224:Congo Red