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  • 1
    Publication Date: 2002-02-02
    Description: 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.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2838482/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2838482/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chapman, Matthew R -- Robinson, Lloyd S -- Pinkner, Jerome S -- Roth, Robyn -- Heuser, John -- Hammar, Marten -- Normark, Staffan -- Hultgren, Scott J -- 1 F32 AI10502-01A1/AI/NIAID NIH HHS/ -- AI29549/AI/NIAID NIH HHS/ -- AI48689/AI/NIAID NIH HHS/ -- DK51406/DK/NIDDK NIH HHS/ -- F32 AI010502/AI/NIAID NIH HHS/ -- F32 AI010502-03/AI/NIAID NIH HHS/ -- NIA P50 AG05681-17/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 1;295(5556):851-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology and Microbial Pathogenesis, Box 8230, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11823641" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/chemistry/genetics/metabolism/ultrastructure ; Amyloid/chemistry/*metabolism/ultrastructure ; Bacterial Proteins/chemistry/genetics/*metabolism/ultrastructure ; Biopolymers ; Circular Dichroism ; Congo Red/metabolism ; Escherichia coli/genetics/*metabolism ; Escherichia coli Proteins/chemistry/genetics/*metabolism/ultrastructure ; Mutation ; *Operon ; Protein Structure, Secondary ; Protein Subunits
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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