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Science 1 February 2002:
Vol. 295. no. 5556, pp. 851 - 855
DOI: 10.1126/science.1067484
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Reports

Role of Escherichia coli Curli Operons in Directing Amyloid Fiber Formation

Matthew R. Chapman,1 Lloyd S. Robinson,1 Jerome S. Pinkner,1 Robyn Roth,2 John Heuser,2 Mårten Hammar,3 Staffan Normark,3 Scott J. Hultgren1*

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.

1 Department of Molecular Microbiology and Microbial Pathogenesis, Box 8230,
2 Department of Cell Biology and Physiology, Box 8228, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.
3 Department of Microbiology and Tumorbiology Center (MTC), Karolinska Institute, Box 280, S-171777 Stockholm, Sweden.
*   To whom correspondence should be addressed. E-mail: hultgren{at}borcim.wustl.edu

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Science. ISSN 0036-8075 (print), 1095-9203 (online)